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Conserved domains on  [gi|1595488123|ref|NP_001356067|]
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aldehyde dehydrogenase family 3 member A2 isoform 2 [Homo sapiens]

Protein Classification

aldehyde dehydrogenase family protein( domain architecture ID 10162992)

aldehyde dehydrogenase family protein catalyzes the oxidation of aldehydes, similar to human aldehyde dehydrogenase family 3 member B1 that oxidizes medium and long chain saturated and unsaturated aldehydes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
5-444 0e+00

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


:

Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 833.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07132     4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:cd07132    84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:cd07132   164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPK 324
Cdd:cd07132   244 DYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:cd07132   324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGN 403
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNS 444
Cdd:cd07132   404 SGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
 
Name Accession Description Interval E-value
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
5-444 0e+00

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 833.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07132     4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:cd07132    84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:cd07132   164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPK 324
Cdd:cd07132   244 DYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:cd07132   324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGN 403
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNS 444
Cdd:cd07132   404 SGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
5-447 0e+00

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 649.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PTZ00381   13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:PTZ00381   93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:PTZ00381  173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE--GQKIAFGGETDEATRYIAPTVLTDVD 322
Cdd:PTZ00381  253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIVNPD 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 323 PKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGV 402
Cdd:PTZ00381  333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1595488123 403 GSSGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNSQSK 447
Cdd:PTZ00381  413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFK 457
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
5-423 2.29e-106

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 324.77  E-value: 2.29e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGEIDFMLENLpEWV--TAK 82
Cdd:COG1012    49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP--------LAEARGEVDRAADFL-RYYagEAR 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  83 PVKKNVLTMLD---EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQD 158
Cdd:COG1012   120 RLYGETIPSDApgtRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAG 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 159 LYIVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMN 236
Cdd:COG1012   200 VLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGN 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 CGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDE 308
Cdd:COG1012   280 AGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAELLTGGRrpDGE 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDV 388
Cdd:COG1012   360 GGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDG 439
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1595488123 389 IMHFTLNsFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:COG1012   440 TTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETK 473
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
5-423 2.29e-92

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 288.28  E-value: 2.29e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGEIDFMLENLPEWVTA--- 81
Cdd:pfam00171  35 IAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP--------LAEARGEVDRAIDVLRYYAGLarr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  82 -----KPVKKNVLtmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-L 155
Cdd:pfam00171 107 ldgetLPSDPGRL-----AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 156 DQDLYIVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGK 233
Cdd:pfam00171 182 PAGVLNVVTGSGAEVGEALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGA 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 234 YMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETD 307
Cdd:pfam00171 262 FGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAG 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 308 EAT-RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN 386
Cdd:pfam00171 342 LDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIN 421
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1595488123 387 DVIMhFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:pfam00171 422 DYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
93-420 3.77e-50

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 177.69  E-value: 3.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  93 DEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETT 171
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG------ETDEATrYIAPTV 317
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIekgkaEGATLATGGgrpenvGLQNGF-FVEPTV 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 318 LTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSF 397
Cdd:TIGR01804 364 FADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEA 441
                         330       340
                  ....*....|....*....|...
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:TIGR01804 442 PFGGYKQSGIGRENGKAALAHYT 464
 
Name Accession Description Interval E-value
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
5-444 0e+00

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 833.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07132     4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:cd07132    84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:cd07132   164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPK 324
Cdd:cd07132   244 DYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:cd07132   324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGN 403
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNS 444
Cdd:cd07132   404 SGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
5-426 0e+00

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.


Pssm-ID: 143406 [Multi-domain]  Cd Length: 426  Bit Score: 721.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07087     4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:cd07087    84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:cd07087   164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPK 324
Cdd:cd07087   244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:cd07087   324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGN 403
                         410       420
                  ....*....|....*....|..
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPCL 426
Cdd:cd07087   404 SGMGAYHGKAGFDTFSHLKSVL 425
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
5-458 0e+00

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 656.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07136     4 VEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:cd07136    84 KTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:cd07136   164 GGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPK 324
Cdd:cd07136   244 DYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVTWD 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:cd07136   324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGN 403
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPCLLKSLKREgaNKLRYPPNSqskvdwGKFFLLKR 458
Cdd:cd07136   404 SGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYK------GKKKKLKK 449
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
5-447 0e+00

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 649.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PTZ00381   13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:PTZ00381   93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:PTZ00381  173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE--GQKIAFGGETDEATRYIAPTVLTDVD 322
Cdd:PTZ00381  253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIVNPD 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 323 PKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGV 402
Cdd:PTZ00381  333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1595488123 403 GSSGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNSQSK 447
Cdd:PTZ00381  413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFK 457
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
5-424 0e+00

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.


Pssm-ID: 143453 [Multi-domain]  Cd Length: 436  Bit Score: 613.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07135    11 HSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEKV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLT-MLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVI 163
Cdd:cd07135    91 KDGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07135   171 QGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE--GQKIAFGGETDEATRYIAPTVLTDV 321
Cdd:cd07135   251 PDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIPPTIVSDV 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 322 DPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGG 401
Cdd:cd07135   331 SWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGG 410
                         410       420
                  ....*....|....*....|...
gi 1595488123 402 VGSSGMGAYHGKHSFDTFSHQRP 424
Cdd:cd07135   411 VGDSGYGAYHGKYGFDTFTHERT 433
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
9-426 0e+00

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 545.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   9 RQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPVKKNV 88
Cdd:cd07134     8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  89 LTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVE 168
Cdd:cd07134    88 LLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYIL 248
Cdd:cd07134   168 VAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVF 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 249 CEASLQNQIVWKIKETVKEFYGEN--IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRYIAPTVLTDV 321
Cdd:cd07134   248 VHESVKDAFVEHLKAEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRYIAPTVLTNV 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 322 DPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGG 401
Cdd:cd07134   328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGG 407
                         410       420
                  ....*....|....*....|....*
gi 1595488123 402 VGSSGMGAYHGKHSFDTFSHQRPCL 426
Cdd:cd07134   408 VNNSGIGSYHGVYGFKAFSHERAVL 432
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
2-426 0e+00

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.


Pssm-ID: 143455 [Multi-domain]  Cd Length: 432  Bit Score: 529.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTA 81
Cdd:cd07137     2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  82 KPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYI 161
Cdd:cd07137    82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 162 VINGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNC-GQT 240
Cdd:cd07137   162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 241 CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRYIAPT 316
Cdd:cd07137   242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNS 396
Cdd:cd07137   322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
                         410       420       430
                  ....*....|....*....|....*....|
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFSHQRPCL 426
Cdd:cd07137   402 LPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
7-424 0e+00

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.


Pssm-ID: 143451 [Multi-domain]  Cd Length: 434  Bit Score: 525.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   7 RVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADL-CKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPVK 85
Cdd:cd07133     6 RQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  86 KNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVING 165
Cdd:cd07133    86 VGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVTG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPD 245
Cdd:cd07133   166 GADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 246 YILCEASLQNQIVWKIKETVKEFYGeNIKESPDYERIINLRHFKRILSLLE-----GQKI---AFGGETDEATRYIAPTV 317
Cdd:cd07133   246 YVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdarakGARVielNPAGEDFAATRKLPPTL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 318 LTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSF 397
Cdd:cd07133   325 VLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDL 404
                         410       420
                  ....*....|....*....|....*..
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFSHQRP 424
Cdd:cd07133   405 PFGGVGASGMGAYHGKEGFLTFSHAKP 431
PLN02203 PLN02203
aldehyde dehydrogenase
5-448 3.37e-160

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 462.66  E-value: 3.37e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PLN02203   12 VAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPKKA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:PLN02203   92 KLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID---KDCDLDIVCRRITWGKYMNC-GQT 240
Cdd:PLN02203  172 GGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCaGQA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 241 CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIA----FGGETDEATRYIAPT 316
Cdd:PLN02203  252 CIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGSIDEKKLFIEPT 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNS 396
Cdd:PLN02203  332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDS 411
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKREgaNKLRYPPNSQSKV 448
Cdd:PLN02203  412 LPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPPWNDFKL 461
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
5-427 4.35e-139

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 406.98  E-value: 4.35e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGEIDFMLENL---PEWVTA 81
Cdd:cd07078     4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP--------IEEALGEVARAADTFryyAGLARR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  82 KPVKKNVLTMLD-EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDL 159
Cdd:cd07078    76 LHGEVIPSPDPGeLAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 160 YIVINGGVEET-TELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNC 237
Cdd:cd07078   156 LNVVTGDGDEVgAALASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 238 GQTCIAPDYILCEASLQNQIVWKIKETVKEFYGEN-IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEAT- 310
Cdd:cd07078   236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdakaeGAKLLCGGKRLEGGk 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 311 -RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVI 389
Cdd:cd07078   316 gYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1595488123 390 MHFTLNsFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLL 427
Cdd:cd07078   396 VGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
5-457 8.33e-139

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 408.28  E-value: 8.33e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PLN02174   16 VTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:PLN02174   96 KTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKY-MNCGQTCIA 243
Cdd:PLN02174  176 GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACIS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRYIAPTVLT 319
Cdd:PLN02174  256 PDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILL 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPF 399
Cdd:PLN02174  336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPF 415
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488123 400 GGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKreGANKLRYPPNSQskvdwGKFFLLK 457
Cdd:PLN02174  416 GGVGESGMGAYHGKFSFDAFSHKKAVLYRSLF--GDSAVRYPPYSR-----GKLRLLK 466
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
6-427 2.18e-114

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 341.52  E-value: 2.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   6 RRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEfnvysqevITVLGEIDFMLENL---PEWVTAK 82
Cdd:cd06534     1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPI--------EEALGEVARAIDTFryaAGLADKL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  83 PVKKNVLTMLD-EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLY 160
Cdd:cd06534    73 GGPELPSPDPGgEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 161 IVING-GVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCG 238
Cdd:cd06534   153 NVVPGgGDEVGAALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 QTCIAPDYILCEASLQNQIVWKIKetvkefygenikespdyeriinlrhfkrilsllegqkiafggetdeatryiapTVL 318
Cdd:cd06534   233 QICTAASRLLVHESIYDEFVEKLV-----------------------------------------------------TVL 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 319 TDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSfP 398
Cdd:cd06534   260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA-P 338
                         410       420
                  ....*....|....*....|....*....
gi 1595488123 399 FGGVGSSGMGAYHGKHSFDTFSHQRPCLL 427
Cdd:cd06534   339 FGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
5-423 2.29e-106

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 324.77  E-value: 2.29e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGEIDFMLENLpEWV--TAK 82
Cdd:COG1012    49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP--------LAEARGEVDRAADFL-RYYagEAR 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  83 PVKKNVLTMLD---EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQD 158
Cdd:COG1012   120 RLYGETIPSDApgtRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAG 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 159 LYIVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMN 236
Cdd:COG1012   200 VLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGN 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 CGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDE 308
Cdd:COG1012   280 AGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAELLTGGRrpDGE 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDV 388
Cdd:COG1012   360 GGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDG 439
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1595488123 389 IMHFTLNsFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:COG1012   440 TTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETK 473
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
5-423 2.29e-92

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 288.28  E-value: 2.29e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGEIDFMLENLPEWVTA--- 81
Cdd:pfam00171  35 IAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP--------LAEARGEVDRAIDVLRYYAGLarr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  82 -----KPVKKNVLtmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-L 155
Cdd:pfam00171 107 ldgetLPSDPGRL-----AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 156 DQDLYIVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGK 233
Cdd:pfam00171 182 PAGVLNVVTGSGAEVGEALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGA 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 234 YMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETD 307
Cdd:pfam00171 262 FGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAG 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 308 EAT-RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN 386
Cdd:pfam00171 342 LDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIN 421
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1595488123 387 DVIMhFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:pfam00171 422 DYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
5-423 7.53e-90

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 281.42  E-value: 7.53e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEfNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07099    24 VARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR-ADAGLEVLLALEAIDWAARNAPRVLAPRKV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVI 163
Cdd:cd07099   103 PTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQVV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07099   183 TGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCIS 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE-TDEATRYIAPT 316
Cdd:cd07099   263 VERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDdavakGAKALTGGArSNGGGPFYEPT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNS 396
Cdd:cd07099   343 VLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPA 422
                         410       420
                  ....*....|....*....|....*..
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07099   423 LPFGGVKDSGGGRRHGAEGLREFCRPK 449
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
5-413 6.03e-74

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.


Pssm-ID: 143416 [Multi-domain]  Cd Length: 465  Bit Score: 240.66  E-value: 6.03e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07098    24 IAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSEL----SENTAKILAKLLPQY-LDQDL 159
Cdd:cd07098   104 PGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQvawsSGFFLSIIRECLAACgHDPDL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 160 YIVINGgVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNC 237
Cdd:cd07098   184 VQLVTC-LPETAEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSS 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 238 GQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE-----T 306
Cdd:cd07098   263 GQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadaveKGARLLAGGKryphpE 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN 386
Cdd:cd07098   343 YPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
                         410       420
                  ....*....|....*....|....*..
gi 1595488123 387 DVIMHFTLNSFPFGGVGSSGMGAYHGK 413
Cdd:cd07098   423 DFGVNYYVQQLPFGGVKGSGFGRFAGE 449
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
9-419 6.80e-67

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 222.14  E-value: 6.80e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   9 RQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvYSQEVITVLGEIDFMlENLPEWvtAKPVKKNV 88
Cdd:cd07088    45 EAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKT----LSLARVEVEFTADYI-DYMAEW--ARRIEGEI 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  89 LTMLDEA---YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVIN 164
Cdd:cd07088   118 IPSDRPNeniFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVT 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELL--KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCI 242
Cdd:cd07088   198 GRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCT 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 243 APDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATR--YIA 314
Cdd:cd07088   278 CAERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPEGEKgyFYE 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 315 PTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV----TGNDVIM 390
Cdd:cd07088   358 PTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETyinrENFEAMQ 437
                         410       420
                  ....*....|....*....|....*....
gi 1595488123 391 HFtlnsfpFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07088   438 GF------HAGWKKSGLGGADGKHGLEEY 460
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
94-423 5.56e-65

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 216.24  E-value: 5.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAK-ILAKL-----LPQyldqDLYIVINGGV 167
Cdd:cd07104    91 ESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGlLIAEIfeeagLPK----GVLNVVPGGG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 168 EETTELL--KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPD 245
Cdd:cd07104   167 SEIGDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAG 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 246 YILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIAPTVLT 319
Cdd:cd07104   247 RILVHESVYDEFVEKLVAKAKALpVGDPRDPDTVIGPLINERQVDRVHAIVEdavaaGARLLTGGTYEG--LFYQPTVLS 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVimhfTLNS--- 396
Cdd:cd07104   325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ----TVNDeph 400
                         330       340
                  ....*....|....*....|....*..
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07104   401 VPFGGVKASGGGRFGGPASLEEFTEWQ 427
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
7-421 8.00e-64

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 213.65  E-value: 8.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   7 RVRQAFLSGRSRPLRFRLqqlEALRRMVqerekDILTAIAADLCKS-------EFNVYSQEVITVLGEIDFMLENLPEWV 79
Cdd:cd07102    26 RARAAQKGWRAVPLEERK---AIVTRAV-----ELLAANTDEIAEEltwqmgrPIAQAGGEIRGMLERARYMISIAEEAL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  80 TAKPV--KKNVltmldEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LD 156
Cdd:cd07102    98 ADIRVpeKDGF-----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAgLP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 157 QDLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYM 235
Cdd:cd07102   173 EGVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFF 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 236 NCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET--- 306
Cdd:cd07102   253 NSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaiakGARALIDGALfpe 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 -DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTG 385
Cdd:cd07102   333 dKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFM 412
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1595488123 386 N--DvimhFTLNSFPFGGVGSSGMGAYHGKHSFDTFSH 421
Cdd:cd07102   413 NrcD----YLDPALAWTGVKDSGRGVTLSRLGYDQLTR 446
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
96-423 2.05e-63

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 212.81  E-value: 2.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  96 YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLpqyLDQDL----YIVINGGVEETT 171
Cdd:cd07093   112 YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA---NEAGLppgvVNVVHGFGPEAG 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07093   189 AALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILV 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATR-----YIAPTVL 318
Cdd:cd07093   269 QRSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVelaraEGATILTGGGRPELPDleggyFVEPTVI 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 319 TDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimhfTLNSF- 397
Cdd:cd07093   349 TGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTV---------WVNCWl 419
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1595488123 398 ------PFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07093   420 vrdlrtPFGGVKASGIGREGGDYSLEFYTELK 451
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
100-423 2.23e-63

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 212.57  E-value: 2.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELLKQ-- 176
Cdd:cd07150   118 RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDdp 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07150   198 RVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 IVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDeaTRYIAPTVLTDVDPKTKVMQE 330
Cdd:cd07150   278 FVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVEdavakGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFRE 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 331 EIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHN-HKLIKrMIDETSSGGVTGNDVIMHFTLNSfPFGGVGSSGMGA 409
Cdd:cd07150   356 ETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDlQRAFK-LAERLESGMVHINDPTILDEAHV-PFGGVKASGFGR 433
                         330
                  ....*....|....
gi 1595488123 410 YHGKHSFDTFSHQR 423
Cdd:cd07150   434 EGGEWSMEEFTELK 447
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
10-419 5.31e-62

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 208.83  E-value: 5.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  10 QAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvYSQevitVLGEIDFMLENLpEW----------- 78
Cdd:cd07103    30 AAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKP----LAE----ARGEVDYAASFL-EWfaeearriygr 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  79 -VTAKPVKKNVLTMldeayiqPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LD 156
Cdd:cd07103   101 tIPSPAPGKRILVI-------KQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 157 QDLYIVINGGVEETTELLKQRFD--HIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKY 234
Cdd:cd07103   174 AGVLNVVTGSPAEIGEALCASPRvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKF 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 235 MNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDE 308
Cdd:cd07103   254 RNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEdavakGAKVLTGGKRLG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 AT-RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGND 387
Cdd:cd07103   334 LGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINT 413
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1595488123 388 VIMhfTLNSFPFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07103   414 GLI--SDAEAPFGGVKESGLGREGGKEGLEEY 443
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
95-419 2.83e-60

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 205.33  E-value: 2.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTEL 173
Cdd:cd07144   138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSA 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07144   218 LAEHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 252 SLQNQIVWKIKETVKEFY--GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE----TDEATRYIAPTVLTD 320
Cdd:cd07144   298 SIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEkgkkeGAKLVYGGEkapeGLGKGYFIPPTIFTD 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV---TGNDviMHFTLnsf 397
Cdd:cd07144   378 VPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSND--SDVGV--- 452
                         330       340
                  ....*....|....*....|..
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07144   453 PFGGFKMSGIGRELGEYGLETY 474
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
101-420 1.48e-59

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 202.46  E-value: 1.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVING-GVEETTELLKQR- 177
Cdd:cd07109   117 PHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGlGAEAGAALVAHPg 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07109   197 VDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEV 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF---YGEnikESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATR----YIAPTVLTDVDPKT 325
Cdd:cd07109   277 LERLVERFRALrvgPGL---EDPDLGPLISAKQLDRVEGFVArararGARIVAGGRIAEGAPaggyFVAPTLLDDVPPDS 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGND------VIMhftlnsfPF 399
Cdd:cd07109   354 RLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNygagggIEL-------PF 426
                         330       340
                  ....*....|....*....|.
gi 1595488123 400 GGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07109   427 GGVKKSGHGREKGLEALYNYT 447
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
100-420 2.39e-59

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 201.27  E-value: 2.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLpqyLDQDL----YIVINGGVEETTELLK 175
Cdd:cd07105    97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVF---HEAGLpkgvLNVVTHSPEDAPEVVE 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 176 QRFDH-----IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07105   174 ALIAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVH 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 251 ASLQNQIVWKIKETVKEfygenIKESPDYERI-INLRHFKRILSLLE-----GQKIAFGGETD--EATRYIAPTVLTDVD 322
Cdd:cd07105   254 ESIADEFVEKLKAAAEK-----LFAGPVVLGSlVSAAAADRVKELVDdalskGAKLVVGGLADesPSGTSMPPTILDNVT 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 323 PKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMH--FTLnsfPFG 400
Cdd:cd07105   329 PDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHdePTL---PHG 405
                         330       340
                  ....*....|....*....|
gi 1595488123 401 GVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07105   406 GVKSSGYGRFNGKWGIDEFT 425
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
100-413 2.65e-59

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 201.60  E-value: 2.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGvEETTELLKQ--R 177
Cdd:cd07106   113 KPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGG-DELGPALTShpD 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07106   192 IRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEF 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQE 330
Cdd:cd07106   272 CEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdakakGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDE 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 331 EIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHFTLN-SFPFGGVGSSGMGA 409
Cdd:cd07106   352 EQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---THGALDpDAPFGGHKQSGIGV 428

                  ....
gi 1595488123 410 YHGK 413
Cdd:cd07106   429 EFGI 432
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
9-423 7.05e-59

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 200.93  E-value: 7.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   9 RQAFLSG-RSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLP--EWVTAKPVK 85
Cdd:cd07089    29 RRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADsfPWEFDLPVP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  86 kNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYldqdly 160
Cdd:cd07089   109 -ALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaetdLPAG------ 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 161 iVIN---GGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYM 235
Cdd:cd07089   182 -VVNvvtGSDNAVGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMH 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 236 NCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEA 309
Cdd:cd07089   261 NAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIargrdEGARLVTGGGRPAG 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 310 TR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN 386
Cdd:cd07089   341 LDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN 420
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1595488123 387 DViMHFTLNSfPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07089   421 GG-GGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETK 455
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
100-423 2.98e-58

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 199.10  E-value: 2.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELL--KQ 176
Cdd:cd07118   118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMteHP 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07118   198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 IVWKIKE-TVKEFYGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDE--ATRYIAPTVLTDVDPKTKVM 328
Cdd:cd07118   278 FVAAVVArSRKVRVGDPLDPETKVGAIINEAQLAKITDYVdagraEGATLLLGGERLAsaAGLFYQPTIFTDVTPDMAIA 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 329 QEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMG 408
Cdd:cd07118   358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIG 435
                         330
                  ....*....|....*
gi 1595488123 409 AYHGKHSFDTFSHQR 423
Cdd:cd07118   436 RELGRYGVEEYTELK 450
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
5-423 3.45e-58

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 198.93  E-value: 3.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPL----RFRLqqleaLRRMVqerekDILTAIAADLCKSEfnvySQEVITVLGEIDFMLENLPEW-- 78
Cdd:cd07114    25 VAAARAAFEGGAWRKLtpteRGKL-----LRRLA-----DLIEANAEELAELE----TRDNGKLIRETRAQVRYLAEWyr 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  79 ------------VTakPV-KKNVLtmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAK 145
Cdd:cd07114    91 yyagladkiegaVI--PVdKGDYL-----NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 146 ILAKL-----LPQYLDQdlyiVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDK 218
Cdd:cd07114   164 ELAKLaeeagFPPGVVN----VVTGFGPETGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 219 DCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKefygeNIK-ESPDYER-----IINLRHFKRIL 292
Cdd:cd07114   240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARAR-----AIRvGDPLDPEtqmgpLATERQLEKVE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 293 SLL-----EGQKIAFGGET-----DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALY 362
Cdd:cd07114   315 RYVarareEGARVLTGGERpsgadLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595488123 363 VFSHNHKLIKRMIDETSSGGVTGNDvimhFTLNSF--PFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07114   395 IWTRDLARAHRVARAIEAGTVWVNT----YRALSPssPFGGFKDSGIGRENGIEAIREYTQTK 453
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
96-408 2.51e-57

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 196.39  E-value: 2.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  96 YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELL- 174
Cdd:cd07092   113 MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALv 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 -KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:cd07092   193 aHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESV 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRY-IAPTVLTDVDPKTKV 327
Cdd:cd07092   273 YDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEI 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 328 MQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTL-NSFPFGGVGSSG 406
Cdd:cd07092   353 VQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLaAEMPHGGFKQSG 429

                  ..
gi 1595488123 407 MG 408
Cdd:cd07092   430 YG 431
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
95-408 4.04e-57

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 196.66  E-value: 4.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYI-VING-----GVE 168
Cdd:cd07091   135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVnIVPGfgptaGAA 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETTELlkqRFDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07091   215 ISSHM---DVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRI 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 248 LCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATRYIAPTVLTD 320
Cdd:cd07091   292 FVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIesgkkEGATLLTGGERhGSKGYFIQPTVFTD 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTLNSF--- 397
Cdd:cd07091   372 VKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN------TYNVFdaa 445
                         330
                  ....*....|..
gi 1595488123 398 -PFGGVGSSGMG 408
Cdd:cd07091   446 vPFGGFKQSGFG 457
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
101-408 6.64e-57

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 195.51  E-value: 6.64e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQ-YLDQDLYIVINGGVEET-TELLK-QR 177
Cdd:cd07149   123 PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVgDALVTdPR 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAkhLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07149   203 VRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEF 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEAtrYIAPTVLTDVDPKTKVMQEE 331
Cdd:cd07149   281 LERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEEWVEeavegGARLLTGGKRDGA--ILEPTVLTDVPPDMKVVCEE 358
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488123 332 IFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvIMHFTLNSFPFGGVGSSGMG 408
Cdd:cd07149   359 VFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIND-SSTFRVDHMPYGGVKESGTG 434
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
5-408 9.81e-55

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 189.88  E-value: 9.81e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEwvtAK-- 82
Cdd:cd07108    25 VAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYFGGLAGE---LKge 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  83 --PVKKNVLTmldeaYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLY 160
Cdd:cd07108   102 tlPFGPDVLT-----YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 161 IVINGGVEETTELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWG-KYMNC 237
Cdd:cd07108   177 NVITGYGEECGAALVDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQ 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 238 GQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE------GQKIAFGGETDEAT 310
Cdd:cd07108   257 GQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglstsGATVLRGGPLPGEG 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 311 R-----YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTG 385
Cdd:cd07108   337 PladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQV 416
                         410       420
                  ....*....|....*....|...
gi 1595488123 386 NDviMHFTLNSFPFGGVGSSGMG 408
Cdd:cd07108   417 NQ--GGGQQPGQSYGGFKQSGLG 437
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
83-420 1.18e-54

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 189.74  E-value: 1.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  83 PVKKNVLtmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPqylDQ 157
Cdd:cd07112   111 PTGPDAL-----ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLP---AG 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 158 DLYIVINGGVEETTEL-LKQRFDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDC-DLDIVCRRITWGKY 234
Cdd:cd07112   183 VLNVVPGFGHTAGEALgLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIF 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 235 MNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDE 308
Cdd:cd07112   263 WNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIesgkaEGARLVAGGKRVL 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTG 385
Cdd:cd07112   343 TETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV 422
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1595488123 386 N-----DVIMhftlnsfPFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07112   423 NcfdegDITT-------PFGGFKQSGNGRDKSLHALDKYT 455
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
89-408 2.00e-54

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 189.48  E-value: 2.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  89 LTMLDE---AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVING 165
Cdd:cd07559   121 LSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTG 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLK--QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI-----DKDCDLDIVCRRITWGKYMNCG 238
Cdd:cd07559   201 FGSEAGKPLAshPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQG 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 QTCIAPDYILCEASLQNQIVWKIKETVkefygENIKE-SP-DYERII----NLRHFKRILSLL-----EGQKIAFGGE-- 305
Cdd:cd07559   281 EVCTCPSRALVQESIYDEFIERAVERF-----EAIKVgNPlDPETMMgaqvSKDQLEKILSYVdigkeEGAEVLTGGErl 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 306 ---TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGG 382
Cdd:cd07559   356 tlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGR 435
                         330       340       350
                  ....*....|....*....|....*....|
gi 1595488123 383 VTGNdvimhfTLNSFP----FGGVGSSGMG 408
Cdd:cd07559   436 VWVN------CYHQYPahapFGGYKKSGIG 459
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
9-419 4.12e-54

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 188.10  E-value: 4.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   9 RQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADL-CKSEFNVYSQeVITVLGEIDFMLENLPEWVTAKPVKKN 87
Cdd:cd07138    46 RRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMgAPITLARAAQ-VGLGIGHLRAAADALKDFEFEERRGNS 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  88 VLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLpqyLDQDL----YIVI 163
Cdd:cd07138   125 LVVR--------EPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEIL---DEAGLpagvFNLV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLK--QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDivcRRITWG---KYMNCG 238
Cdd:cd07138   194 NGDGPVVGEALSahPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLE---KAVPRGvaaCFANSG 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 QTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG----ETDE 308
Cdd:cd07138   271 QSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIqkgieEGARLVAGGpgrpEGLE 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHN----HKLIKRMidetSSGGVT 384
Cdd:cd07138   351 RGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADperaRAVARRL----RAGQVH 426
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1595488123 385 GNDVIMHFtlnSFPFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07138   427 INGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
95-429 5.85e-54

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 187.51  E-value: 5.85e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGvEETTEL 173
Cdd:cd07090   110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQRFD--HIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07090   189 LCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 252 SLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE----TD--EATRYIAPTVLT 319
Cdd:cd07090   269 SIKDEFTERLVERTKKIrIGDPLDEDTQMGALISEEHLEKVLGYIesakqEGAKVLCGGErvvpEDglENGFYVSPCVLT 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimhFTLNS--F 397
Cdd:cd07090   349 DCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT----YNISPveV 424
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFSHqrpclLKS 429
Cdd:cd07090   425 PFGGYKQSGFGRENGTAALEHYTQ-----LKT 451
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
83-420 1.39e-53

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 186.49  E-value: 1.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  83 PVKKNVLTmldeaYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYI 161
Cdd:cd07115   104 PVRGPFLN-----YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLN 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 162 VINGGVEETTELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQ 239
Cdd:cd07115   179 VVTGFGEVAGAALVEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQ 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 240 TCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATR-Y 312
Cdd:cd07115   259 MCTAGSRLLVHESIYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfF 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 313 IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhf 392
Cdd:cd07115   339 VEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN------ 412
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1595488123 393 TLNSF----PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07115   413 TYNRFdpgsPFGGYKQSGFGREMGREALDEYT 444
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
101-423 6.00e-53

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 184.42  E-value: 6.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAK-ILAKLLPQY-LDQDLYIVINGGVEETTELLK-QR 177
Cdd:cd07152   110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGvVIARLFEEAgLPAGVLHVLPGGADAGEALVEdPN 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07152   190 VAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAY 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF-----YGENIKESPdyerIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIAPTVLTDVDPKTKV 327
Cdd:cd07152   270 TAKLAAKAKHLpvgdpATGQVALGP----LINARQLDRVHAIVDdsvaaGARLEAGGTYDG--LFYRPTVLSGVKPGMPA 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 328 MQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVimhfTLNS---FPFGGVGS 404
Cdd:cd07152   344 FDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPFGGMGA 419
                         330       340
                  ....*....|....*....|
gi 1595488123 405 SGMGAYHG-KHSFDTFSHQR 423
Cdd:cd07152   420 SGNGSRFGgPANWEEFTQWQ 439
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
94-420 8.59e-53

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 185.21  E-value: 8.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYLDQdlyIVINGGVE 168
Cdd:cd07119   127 ISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELieeagLPAGVVN---LVTGSGAT 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETTEL-LKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07119   204 VGAELaESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRL 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 248 LCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATR---YIAPT 316
Cdd:cd07119   284 LVEESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGKrpTGDELAkgyFVEPT 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNS 396
Cdd:cd07119   364 IFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAE 441
                         330       340
                  ....*....|....*....|....
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07119   442 APWGGYKQSGIGRELGPTGLEEYQ 465
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
5-412 1.62e-52

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 183.71  E-value: 1.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRF-RLQQLEALRRMVQEREKDILTAIAAD--LCKSEFNVYSQEVITVL-----------GEIdF 70
Cdd:cd07146    23 LREALALAASYRSTLTRYqRSAILNKAAALLEARREEFARLITLEsgLCLKDTRYEVGRAADVLrfaaaealrddGES-F 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  71 MLENLPewvTAKPVKknvltmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL 150
Cdd:cd07146   102 SCDLTA---NGKARK---------IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 151 LPQY-LDQDLYIVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAA-KHLTpvtLELGGKSPCYIDKDCDLDIVC 226
Cdd:cd07146   170 LYEAgLPPDMLSVVTGEPGEIGDELIThpDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDPLIVMDDADLERAA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 227 RRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIIN---LRHF-KRILSLLE-GQKI 300
Cdd:cd07146   247 TLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDeeaAIQIeNRVEEAIAqGARV 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 301 AFGGETDEAtrYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 380
Cdd:cd07146   327 LLGNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDV 404
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1595488123 381 GGVTGNDViMHFTLNSFPFGGVGSSGMGAYHG 412
Cdd:cd07146   405 GTVNVNEV-PGFRSELSPFGGVKDSGLGGKEG 435
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
100-419 2.13e-52

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 184.51  E-value: 2.13e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELL---- 174
Cdd:PLN02278  159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDALlasp 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 KQRfdHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQ 254
Cdd:PLN02278  239 KVR--KITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIY 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 255 NQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATRYiAPTVLTDVDPKTK 326
Cdd:PLN02278  317 DKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVqdavsKGAKVLLGGKrhSLGGTFY-EPTVLGDVTEDML 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 327 VMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSG 406
Cdd:PLN02278  396 IFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTE--VAPFGGVKQSG 473
                         330
                  ....*....|...
gi 1595488123 407 MGAYHGKHSFDTF 419
Cdd:PLN02278  474 LGREGSKYGIDEY 486
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
2-423 1.01e-51

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 181.78  E-value: 1.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVySQEVITVLGEIDFMLEnLPEWVTA 81
Cdd:cd07110    22 DAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVDDVAGCFEYYAD-LAEQLDA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  82 KpvKKNVLTMLDE---AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAK------LLP 152
Cdd:cd07110   100 K--AERAVPLPSEdfkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEiaaeagLPP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 153 QYLDqdlyiVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRIT 230
Cdd:cd07110   178 GVLN-----VVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAM 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 231 WGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVkefygENIKESPDYER------IINLRHFKRILSLL-----EGQK 299
Cdd:cd07110   253 FGCFWNNGQICSATSRLLVHESIADAFLERLATAA-----EAIRVGDPLEEgvrlgpLVSQAQYEKVLSFIargkeEGAR 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 300 IAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMID 376
Cdd:cd07110   328 LLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAE 407
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1595488123 377 ETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07110   408 ALEAGIVWINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNYLEVK 452
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
100-419 1.69e-51

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 181.23  E-value: 1.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELLKQ-R 177
Cdd:cd07139   136 EPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADREVGEYLVRHpG 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07139   216 VDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEV 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATR--YIAPTVLTDVDPKTKVM 328
Cdd:cd07139   296 VEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIakgraEGARLVTGGGRpAGLDRgwFVEPTLFADVDNDMRIA 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 329 QEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNH----KLIKRMidetSSGGVTGNDVIMHFTLnsfPFGGVGS 404
Cdd:cd07139   376 QEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVerglAVARRI----RTGTVGVNGFRLDFGA---PFGGFKQ 448
                         330
                  ....*....|....*
gi 1595488123 405 SGMGAYHGKHSFDTF 419
Cdd:cd07139   449 SGIGREGGPEGLDAY 463
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
100-421 2.02e-51

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 181.39  E-value: 2.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELLKQ-- 176
Cdd:cd07131   134 QPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEhp 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07131   214 DVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDE 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 IVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE-----TDEATRYIAPTVLTDVDPKT 325
Cdd:cd07131   294 FLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNeigkeEGATLLLGGErltggGYEKGYFVEPTVFTDVTPDM 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN------DVIMhftlnsfPF 399
Cdd:cd07131   374 RIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaptigaEVHL-------PF 446
                         330       340
                  ....*....|....*....|....*
gi 1595488123 400 GGVGSSGMGayH---GKHSFDTFSH 421
Cdd:cd07131   447 GGVKKSGNG--HreaGTTALDAFTE 469
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
95-408 3.09e-51

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 180.24  E-value: 3.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEET-TE 172
Cdd:cd07145   117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgDE 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 173 LLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07145   197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 252 SLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATrYIAPTVLTDVDPKT 325
Cdd:cd07145   277 EVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndaveKGGKILYGGKRDEGS-FFPPTVLENDTPDM 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMhFTLNSFPFGGVGSS 405
Cdd:cd07145   356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGGFKKS 434

                  ...
gi 1595488123 406 GMG 408
Cdd:cd07145   435 GIG 437
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
2-413 5.37e-51

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 179.81  E-value: 5.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYsQEVITVLGEIDFMLENLPEWVta 81
Cdd:cd07101    21 EAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EEVLDVAIVARYYARRAERLL-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  82 KPVKKN----VLTMLDEAYiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LD 156
Cdd:cd07101    98 KPRRRRgaipVLTRTTVNR---RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLP 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 157 QDLYIVINGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMN 236
Cdd:cd07101   175 RDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSN 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 CGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET--DE 308
Cdd:cd07101   255 AGQLCVSIERIYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDdavakGATVLAGGRArpDL 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDv 388
Cdd:cd07101   335 GPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE- 413
                         410       420
                  ....*....|....*....|....*..
gi 1595488123 389 IMHFTLNSF--PFGGVGSSGMGAYHGK 413
Cdd:cd07101   414 GYAAAWASIdaPMGGMKDSGLGRRHGA 440
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
95-420 1.12e-50

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 179.65  E-value: 1.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTEL 173
Cdd:cd07143   138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNA 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQ--RFDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07143   218 ISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 251 ASLQNQIVWKIKETVKEF-----YGENIKESPDYERIinlrHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLT 319
Cdd:cd07143   298 EGIYDKFVKRFKEKAKKLkvgdpFAEDTFQGPQVSQI----QYERIMSYIEsgkaeGATVETGGKRHGNEGYfIEPTIFT 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNhklIKRMIdETSSGGVTGNDVIMHFTLNSF-- 397
Cdd:cd07143   374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNN---INNAI-RVANALKAGTVWVNCYNLLHHqv 449
                         330       340
                  ....*....|....*....|...
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07143   450 PFGGYKQSGIGRELGEYALENYT 472
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
93-420 3.77e-50

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 177.69  E-value: 3.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  93 DEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETT 171
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG------ETDEATrYIAPTV 317
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIekgkaEGATLATGGgrpenvGLQNGF-FVEPTV 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 318 LTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSF 397
Cdd:TIGR01804 364 FADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEA 441
                         330       340
                  ....*....|....*....|...
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:TIGR01804 442 PFGGYKQSGIGRENGKAALAHYT 464
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
95-408 4.85e-50

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 177.63  E-value: 4.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYI-VINGGVEETTEL 173
Cdd:cd07113   136 AFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLnVVNGKGAVGAQL 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEAS 252
Cdd:cd07113   216 ISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRS 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 253 LQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATRYIAPTVLTDVDPKT 325
Cdd:cd07113   296 KFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEAlAGEGYFVQPTLVLARSADS 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHFTLN-SFPFGGVGS 404
Cdd:cd07113   376 RLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGMKQ 452

                  ....
gi 1595488123 405 SGMG 408
Cdd:cd07113   453 SGIG 456
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
2-412 5.86e-50

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 176.80  E-value: 5.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADlCKsefNVYSQEVITVLGEIDfMLENLPEWVTA 81
Cdd:cd07107    22 DRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALD-CG---NPVSAMLGDVMVAAA-LLDYFAGLVTE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  82 kpVKKNVLTMLDEA--YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDL 159
Cdd:cd07107    97 --LKGETIPVGGRNlhYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 160 YIVINGGVEETTELLKQRFD--HIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGkyMN- 236
Cdd:cd07107   175 FNILPGDGATAGAALVRHPDvkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNf 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 --CGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG--ET 306
Cdd:cd07107   253 twCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrPE 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 DEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV 383
Cdd:cd07107   333 GPALEggfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYV 412
                         410       420
                  ....*....|....*....|....*....
gi 1595488123 384 TGNDVIMHFTlnSFPFGGVGSSGMGAYHG 412
Cdd:cd07107   413 WINGSSRHFL--GAPFGGVKNSGIGREEC 439
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
5-419 9.33e-50

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 175.73  E-value: 9.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQL----EALRR--------MVQEREKDILTAIA-----ADLCksefnvysqevitvlge 67
Cdd:cd07100     5 LDRAHAAFLAWRKTSFAERAALLrklaDLLRErkdelarlITLEMGKPIAEARAevekcAWIC----------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  68 iDFMLENLPEWVTAKPVKknvlTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKIL 147
Cdd:cd07100    68 -RYYAENAEAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAI 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 148 AKLLPQY-LDQDLYIVINGGVEETTELLK-QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIV 225
Cdd:cd07100   143 EELFREAgFPEGVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 226 CRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDY---ERiinlrhfKRILSLLEGQ--- 298
Cdd:cd07100   223 VKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDLgplAR-------KDLRDELHEQvee 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 299 ------KIAFGGET-DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLI 371
Cdd:cd07100   296 avaagaTLLLGGKRpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERA 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1595488123 372 KRMIDETSSGGVTGNDviMHFTLNSFPFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07100   376 ERVARRLEAGMVFING--MVKSDPRLPFGGVKRSGYGRELGRFGIREF 421
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
23-420 9.47e-50

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 176.73  E-value: 9.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  23 RLQQLEALRRMVQEREKDILTAIAADL----CKSEFNVYSQEVIT---------VLGEIdfmlenLPEWVTAKpvkknvl 89
Cdd:cd07151    56 RAEILEKAAQILEERRDEIVEWLIRESgstrIKANIEWGAAMAITreaatfplrMEGRI------LPSDVPGK------- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  90 tmldEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAK-ILAKL-----LPQYLdqdLYIVI 163
Cdd:cd07151   123 ----ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGlLLAKIfeeagLPKGV---LNVVV 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLKQ---RFdhIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT 240
Cdd:cd07151   196 GAGSEIGDAFVEHpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQI 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 241 CIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIA 314
Cdd:cd07151   274 CMAINRIIVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEqaveeGATLLVGGEAEG--NVLE 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 315 PTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTL 394
Cdd:cd07151   352 PTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEP 431
                         410       420
                  ....*....|....*....|....*.
gi 1595488123 395 NSfPFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07151   432 HV-PFGGEKNSGLGRFNGEWALEEFT 456
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
89-408 1.59e-49

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 176.11  E-value: 1.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  89 LTMLDE---AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVING 165
Cdd:cd07117   121 ANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTG 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07117   201 KGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCA 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKEtvkEFygENIK----ESPDYE--RIINLRHFKRILSLL-----EGQKIAFGGE-----TD 307
Cdd:cd07117   281 GSRIFVQEGIYDEFVAKLKE---KF--ENVKvgnpLDPDTQmgAQVNKDQLDKILSYVdiakeEGAKILTGGHrltenGL 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 308 EATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNd 387
Cdd:cd07117   356 DKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN- 434
                         330       340
                  ....*....|....*....|....*
gi 1595488123 388 vimhfTLNSFP----FGGVGSSGMG 408
Cdd:cd07117   435 -----TYNQIPagapFGGYKKSGIG 454
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
100-419 4.58e-49

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 173.38  E-value: 4.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELL--KQ 176
Cdd:PRK10090   70 RALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELagNP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:PRK10090  150 KVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 IVWKIKETVKEF-YGENIKES-PDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATRYI-APTVLTDVDPKTKVM 328
Cdd:PRK10090  230 FVNRLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQEMSIM 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 329 QEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN----DVIMHFtlnsfpFGGVGS 404
Cdd:PRK10090  310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINrenfEAMQGF------HAGWRK 383
                         330
                  ....*....|....*
gi 1595488123 405 SGMGAYHGKHSFDTF 419
Cdd:PRK10090  384 SGIGGADGKHGLHEY 398
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
8-408 7.33e-49

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 173.77  E-value: 7.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   8 VRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAAD-------------LCKSEFNVYSQEVITVLGEIdfmlen 74
Cdd:cd07094    30 ARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEggkpikdarvevdRAIDTLRLAAEEAERIRGEE------ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  75 LPEWVTAKPVKKNVLTMldeayiqPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL-PQ 153
Cdd:cd07094   104 IPLDATQGSDNRLAWTI-------REPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 154 YLDQDLYIVINGGVEETTELL--KQRFDHIFYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDKDCDLDIVCRRITW 231
Cdd:cd07094   177 GVPEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 232 GKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE 305
Cdd:cd07094   255 GGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVERWVEeaveaGARLLCGGE 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 306 TDEATRYiaPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTG 385
Cdd:cd07094   335 RDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMV 412
                         410       420
                  ....*....|....*....|...
gi 1595488123 386 NDViMHFTLNSFPFGGVGSSGMG 408
Cdd:cd07094   413 NDS-SAFRTDWMPFGGVKESGVG 434
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
94-409 4.80e-48

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415 [Multi-domain]  Cd Length: 473  Bit Score: 172.05  E-value: 4.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYLdqdLYIVINGGVE 168
Cdd:cd07097   128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEIleeagLPAGV---FNLVMGSGSE 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETTELLK-QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07097   205 VGQALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRL 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 248 LCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATR--YIAPTVL 318
Cdd:cd07097   285 IVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGERlKRPDEgyYLAPALF 364
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 319 TDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVIMHFTLns 396
Cdd:cd07097   365 AGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAGVDYHV-- 442
                         330
                  ....*....|...
gi 1595488123 397 fPFGGVGSSGMGA 409
Cdd:cd07097   443 -PFGGRKGSSYGP 454
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
5-412 4.39e-47

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 170.44  E-value: 4.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYsQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PRK09407   60 FARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAF-EEVLDVALTARYYARRAPKLLAPRRR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  85 KkNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVI 163
Cdd:PRK09407  139 A-GALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVV 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:PRK09407  218 TGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCIS 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKefygeNIKESPDYE------RIINLRHFKRILSLLE-----GQKIAFGGET--DEAT 310
Cdd:PRK09407  298 IERIYVHESIYDEFVRAFVAAVR-----AMRLGAGYDysadmgSLISEAQLETVSAHVDdavakGATVLAGGKArpDLGP 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 311 RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIM 390
Cdd:PRK09407  373 LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYA 452
                         410       420
                  ....*....|....*....|...
gi 1595488123 391 H-FTLNSFPFGGVGSSGMGAYHG 412
Cdd:PRK09407  453 AaWGSVDAPMGGMKDSGLGRRHG 475
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
96-408 4.95e-47

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 169.32  E-value: 4.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  96 YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELL- 174
Cdd:PRK13473  133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALv 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 -KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PRK13473  213 gHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGI 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE------GQKIAFGGET-DEATRYIAPTVLTDVDPKT 325
Cdd:PRK13473  293 YDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFVErakalgHIRVVTGGEApDGKGYYYEPTLLAGARQDD 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTLNS-FPFGGVGS 404
Cdd:PRK13473  373 EIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMLVSeMPHGGQKQ 449

                  ....
gi 1595488123 405 SGMG 408
Cdd:PRK13473  450 SGYG 453
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
68-406 4.80e-46

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 167.42  E-value: 4.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  68 IDFM----LENLpEWVTAKPVkknvLTMLDEA----YIqpqPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSEl 139
Cdd:PRK03137  138 IDFLeyyaRQML-KLADGKPV----ESRPGEHnryfYI---PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPAS- 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 140 seNTAKILAKL--------LPQYldqdlyiVIN---GGVEETTELL----KQRFdhIFYTGNTAVGKIVMEAAAK----- 199
Cdd:PRK03137  209 --DTPVIAAKFvevleeagLPAG-------VVNfvpGSGSEVGDYLvdhpKTRF--ITFTGSREVGLRIYERAAKvqpgq 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 200 -HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPD 278
Cdd:PRK03137  278 iWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAY 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 279 YERIINLRHFKRILSLLE-GQ---KIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFIN 353
Cdd:PRK03137  358 MGPVINQASFDKIMSYIEiGKeegRLVLGGEGDDSKGYfIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIAN 437
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488123 354 EREKPLALYVFSHNHKLIKRMIDETSSG------GVTGNDVIMHftlnsfPFGGVGSSG 406
Cdd:PRK03137  438 NTEYGLTGAVISNNREHLEKARREFHVGnlyfnrGCTGAIVGYH------PFGGFNMSG 490
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
95-419 5.39e-46

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 166.52  E-value: 5.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPqylDQDLYIVINGGVEE 169
Cdd:cd07142   135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLaaeagLP---DGVLNIVTGFGPTA 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 170 TTELLKQR-FDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07142   212 GAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 248 LCEASLQNQIVWKIKE-----TVKEFYGENIKESPDyeriINLRHFKRILSLL-----EGQKIAFGGE-TDEATRYIAPT 316
Cdd:cd07142   292 FVHESIYDEFVEKAKAralkrVVGDPFRKGVEQGPQ----VDKEQFEKILSYIehgkeEGATLITGGDrIGSKGYYIQPT 367
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVimhFTL 394
Cdd:cd07142   368 IFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDV---FDA 444
                         330       340
                  ....*....|....*....|....*
gi 1595488123 395 nSFPFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07142   445 -SIPFGGYKMSGIGREKGIYALNNY 468
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
5-409 2.11e-45

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 165.86  E-value: 2.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQL----EALRR--------MVQE-----REKDILTAIAADLCksefNVYSQEvitvlge 67
Cdd:cd07124    75 VQAARAAFPTWRRTPPEERARLLlraaALLRRrrfelaawMVLEvgknwAEADADVAEAIDFL----EYYARE------- 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  68 idfMLENLPEWVTAKPVKKNVLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKIL 147
Cdd:cd07124   144 ---MLRLRGFPVEMVPGEDNRYVY--------RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 148 AKL-----LPQYldqdlyiVIN---GGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAK------HLTPVTLELGGK 211
Cdd:cd07124   213 VEIleeagLPPG-------VVNflpGPGEEVGDYLVEhpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGK 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 212 SPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKR 290
Cdd:cd07124   286 NAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGARDR 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 291 ILSLLE----GQKIAFGGETDE-ATR--YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYV 363
Cdd:cd07124   366 IRRYIEigksEGRLLLGGEVLElAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGV 445
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1595488123 364 FSHNHKLIKRMIDETSSG------GVTGNDVIMHftlnsfPFGGVGSSGMGA 409
Cdd:cd07124   446 FSRSPEHLERARREFEVGnlyanrKITGALVGRQ------PFGGFKMSGTGS 491
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
95-408 3.93e-45

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 164.27  E-value: 3.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFV-----LTIqpligAIAAGNAVIIKPSE----LSENTAKILAKLLPQY-LDQDLYIVIN 164
Cdd:cd07086   127 LMEQWNPLGVVGVITAFNFPVAvpgwnAAI-----ALVCGNTVVWKPSEttplTAIAVTKILAEVLEKNgLPPGVVNLVT 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLK-QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07086   202 GGGDGGELLVHdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTT 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET---DEATRYIA 314
Cdd:cd07086   282 TRRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEiaksqGGTVLTGGKRidgGEPGNYVE 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 315 PTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS--------GGVTGN 386
Cdd:cd07086   362 PTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcgivnvnIPTSGA 441
                         330       340
                  ....*....|....*....|..
gi 1595488123 387 DVIMhftlnsfPFGGVGSSGMG 408
Cdd:cd07086   442 EIGG-------AFGGEKETGGG 456
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
101-408 4.19e-45

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 163.57  E-value: 4.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL-PQYLDQDLYIVINGGVEETTELLK-QRF 178
Cdd:cd07147   123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADLLVTdERI 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 179 DHIFYTGNTAVG-KIVMEAAAKHltpVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07147   203 KLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEF 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATryIAPTVLTDVDPKTKVMQEE 331
Cdd:cd07147   280 KSRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVNeavdaGAKLLTGGKRDGAL--LEPTILEDVPPDMEVNCEE 357
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488123 332 IFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDViMHFTLNSFPFGGVGSSGMG 408
Cdd:cd07147   358 VFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDV-PTFRVDHMPYGGVKDSGIG 433
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
94-408 2.21e-44

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 162.36  E-value: 2.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTE 172
Cdd:cd07082   134 IAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGD 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 173 LL--KQRFDHIFYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07082   214 PLvtHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVH 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 251 ASLQNQIVWKIKETVkefygENIK------ESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATrYIAPTVLT 319
Cdd:cd07082   292 ESVADELVELLKEEV-----AKLKvgmpwdNGVDITPLIDPKSADFVEGLIDdavakGATVLNGGGREGGN-LIYPTLLD 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlNSFPF 399
Cdd:cd07082   366 PVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP-DHFPF 444

                  ....*....
gi 1595488123 400 GGVGSSGMG 408
Cdd:cd07082   445 LGRKDSGIG 453
PLN02467 PLN02467
betaine aldehyde dehydrogenase
2-423 1.31e-43

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 160.67  E-value: 1.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   2 ELEVRRVRQAFLSGRSR-----PLRFRLQQLEALRRMVQEReKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLEnLP 76
Cdd:PLN02467   48 DAAVEAARKAFKRNKGKdwartTGAVRAKYLRAIAAKITER-KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYAD-LA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  77 EWVTAK---PVKknvLTMLD-EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-- 150
Cdd:PLN02467  126 EALDAKqkaPVS---LPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADIcr 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 151 ---LPQYLdqdLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVC 226
Cdd:PLN02467  203 evgLPPGV---LNVVTGLGTEAGAPLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAV 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 227 RRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKefygeNIKESPDYER------IINLRHFKRILSLL----- 295
Cdd:PLN02467  280 EWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAK-----NIKISDPLEEgcrlgpVVSEGQYEKVLKFIstaks 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 296 EGQKIAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIK 372
Cdd:PLN02467  355 EGATILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCE 434
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595488123 373 RMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:PLN02467  435 RVSEAFQAGIVWINCSQPCFC--QAPWGGIKRSGFGRELGEWGLENYLSVK 483
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
100-420 1.38e-42

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 157.12  E-value: 1.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQ--YLDQDLYIVINGGVEETTELL--K 175
Cdd:cd07120   116 EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHLvaS 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 176 QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQN 255
Cdd:cd07120   196 PDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIAD 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 256 QIVWKIKEtvkefYGENIKESPDYER------IINLRHFKRILSLLE------GQKIAFGGETDEATR---YIAPTVLTD 320
Cdd:cd07120   276 EVRDRLAA-----RLAAVKVGPGLDPasdmgpLIDRANVDRVDRMVEraiaagAEVVLRGGPVTEGLAkgaFLRPTLLEV 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTL-NSFPF 399
Cdd:cd07120   351 DDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLfAEAEE 427
                         330       340
                  ....*....|....*....|.
gi 1595488123 400 GGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07120   428 GGYRQSGLGRLHGVAALEDFI 448
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
95-420 2.70e-42

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 156.74  E-value: 2.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL------PQyldqdlyiVIN--GG 166
Cdd:cd07141   139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIkeagfpPG--------VVNvvPG 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 167 VEETTELL---KQRFDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCI 242
Cdd:cd07141   211 YGPTAGAAissHPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCC 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 243 APDYILCEASLQNQIVWKI-----KETVKEFYGENIKESPDyeriINLRHFKRILSLL-----EGQKIAFGGET-DEATR 311
Cdd:cd07141   291 AGSRTFVQESIYDEFVKRSverakKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIesgkkEGAKLECGGKRhGDKGY 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 312 YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNhklIKRMIdeTSSGGVTGNDVIMH 391
Cdd:cd07141   367 FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAI--TFSNALRAGTVWVN 441
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1595488123 392 fTLNSF----PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07141   442 -CYNVVspqaPFGGYKMSGNGRELGEYGLQEYT 473
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
94-421 1.37e-40

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 152.28  E-value: 1.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  94 EAYIQPQPLGVVLIIGAWNYP---FVLTIQPligAIAAGNAVIIKPSE---LSENTAKILAKL--LPqylDQDLYIVING 165
Cdd:PLN02766  151 QGYTLKEPIGVVGHIIPWNFPstmFFMKVAP---ALAAGCTMVVKPAEqtpLSALFYAHLAKLagVP---DGVINVVTGF 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLKQR-FDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:PLN02766  225 GPTAGAAIASHMdVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEF-----YGENIKESPDYERiinlRHFKRILSLL-----EGQKIAFGGE-TDEATRY 312
Cdd:PLN02766  305 SSRVYVQEGIYDEFVKKLVEKAKDWvvgdpFDPRARQGPQVDK----QQFEKILSYIehgkrEGATLLTGGKpCGDKGYY 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 313 IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHF 392
Cdd:PLN02766  381 IEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYF 457
                         330       340       350
                  ....*....|....*....|....*....|
gi 1595488123 393 TL-NSFPFGGVGSSGMGAYHGKHSFDTFSH 421
Cdd:PLN02766  458 AFdPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
95-420 1.79e-39

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 149.28  E-value: 1.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPqylDQDLYIVINGGVEE 169
Cdd:PRK09847  151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakeagLP---DGVLNVVTGFGHEA 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 170 TTEL-LKQRFDHIFYTGNTAVGKIVM-EAAAKHLTPVTLELGGKSPCYIDKDC-DLDIVCRRITWGKYMNCGQTCIAPDY 246
Cdd:PRK09847  228 GQALsRHNDIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTR 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 247 ILCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATrYIAPTVLTD 320
Cdd:PRK09847  308 LLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIRegeskGQLLLDGRNAGLAA-AIGPTIFVD 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV---TGNDVIMhftlnSF 397
Cdd:PRK09847  387 VDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGDM-----TV 461
                         330       340
                  ....*....|....*....|...
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:PRK09847  462 PFGGYKQSGNGRDKSLHALEKFT 484
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
1-419 6.04e-39

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 147.28  E-value: 6.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   1 MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKsefnVYSQ---EVITVLGEIDF------- 70
Cdd:cd07085    40 VDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGK----TLADargDVLRGLEVVEFacsiphl 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  71 -MLENLPEwvtakpVKKNVltmldEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAK 149
Cdd:cd07085   116 lKGEYLEN------VARGI-----DTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 150 LLPQY-LDQDLYIVINGGVEETTELLkqrfDH-----IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLD 223
Cdd:cd07085   185 LLQEAgLPDGVLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLE 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 224 IVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EG 297
Cdd:cd07085   261 QTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLIesgveEG 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 298 QKIAFGGETDEATRY-----IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIK 372
Cdd:cd07085   341 AKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAAR 420
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1595488123 373 RMIDETSSGGVtGNDVIMHFTLNSFPFGGVGSSGMGAYH--GKHSFDTF 419
Cdd:cd07085   421 KFQREVDAGMV-GINVPIPVPLAFFSFGGWKGSFFGDLHfyGKDGVRFY 468
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
96-408 5.44e-38

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 144.95  E-value: 5.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  96 YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYldqdlyiVINGgVEET 170
Cdd:cd07140   142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtvkagFPKG-------VINI-LPGS 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 171 TELLKQRF-DH-----IFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07140   214 GSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRIL-----SLLEGQKIAFGG-ETDEATRYIAPT 316
Cdd:cd07140   294 AGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVeycerGVKEGATLVYGGkQVDRPGFFFEPT 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKN--VDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTL 394
Cdd:cd07140   374 VFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN------TY 447
                         330
                  ....*....|....*...
gi 1595488123 395 N----SFPFGGVGSSGMG 408
Cdd:cd07140   448 NktdvAAPFGGFKQSGFG 465
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
2-414 8.96e-38

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 144.08  E-value: 8.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVL-------GEIDFMLEN 74
Cdd:cd07111    62 DAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVArhfyhhaGWAQLLDTE 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  75 LPEWvtakpvkknvltmldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY 154
Cdd:cd07111   142 LAGW---------------------KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 155 -LDQDLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWG 232
Cdd:cd07111   201 gLPPGVLNIVTGNGSFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDA 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 233 KYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLEGQKiAFGGETDEATR 311
Cdd:cd07111   281 IWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGA 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 312 -------YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVT 384
Cdd:cd07111   360 dlpskgpFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVW 439
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1595488123 385 GNdvimhfTLNSF----PFGGVGSSGMGAYHGKH 414
Cdd:cd07111   440 IN------GHNLFdaaaGFGGYRESGFGREGGKE 467
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
100-419 9.81e-38

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 144.95  E-value: 9.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPqylDQDLYIVINGGVEETTELL 174
Cdd:PLN02466  194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLlheagLP---PGVLNVVSGFGPTAGAALA 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 KQR-FDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEAS 252
Cdd:PLN02466  271 SHMdVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHER 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 253 LQNQIVWK-----IKETVKEFYGENIKESPDyeriINLRHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLTDV 321
Cdd:PLN02466  351 VYDEFVEKakaraLKRVVGDPFKKGVEQGPQ----IDSEQFEKILRYIKsgvesGATLECGGDRFGSKGYyIQPTVFSNV 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 322 DPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVIMhftlNSFPF 399
Cdd:PLN02466  427 QDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFD----AAIPF 502
                         330       340
                  ....*....|....*....|
gi 1595488123 400 GGVGSSGMGAYHGKHSFDTF 419
Cdd:PLN02466  503 GGYKMSGIGREKGIYSLNNY 522
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
93-408 3.47e-36

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 139.63  E-value: 3.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  93 DEAYIQPQPLGVVLIIGAWNYPfvltIQ-------PligAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVIN 164
Cdd:PRK13252  134 SFVYTRREPLGVCAGIGAWNYP----IQiacwksaP---ALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQ 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GgVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCI 242
Cdd:PRK13252  207 G-DGRVGAWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCT 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 243 APDYILCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATR--- 311
Cdd:PRK13252  286 NGTRVFVQKSIKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIekgkaEGARLLCGGErlTEGGFAnga 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 312 YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimh 391
Cdd:PRK13252  366 FVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGIC-------- 437
                         330       340
                  ....*....|....*....|....
gi 1595488123 392 fTLNSF-------PFGGVGSSGMG 408
Cdd:PRK13252  438 -WINTWgespaemPVGGYKQSGIG 460
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
11-412 1.12e-34

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 135.78  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  11 AFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvYSQEVITVLGEIDFM---------LENLPEWVTA 81
Cdd:cd07083    67 AFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKN----WVEAIDDVAEAIDFIryyaraalrLRYPAVEVVP 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  82 KPVKKNVLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSE----LSENTAKIL--AKLLP--- 152
Cdd:cd07083   143 YPGEDNESFY--------VGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFheAGFPPgvv 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 153 QYLDQDLYIVINGGVEEttellkQRFDHIFYTGNTAVGKIVMEAAAKHLT------PVTLELGGKSPCYIDKDCDLDIVC 226
Cdd:cd07083   215 QFLPGVGEEVGAYLTEH------ERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVV 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 227 RRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLEGQK----IA 301
Cdd:cd07083   289 EGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegqLV 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 302 FGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD--EAINFINEREKPLALYVFSHNHKLIKRMIDET 378
Cdd:cd07083   369 LGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREF 448
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1595488123 379 SSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHG 412
Cdd:cd07083   449 HVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
1-416 1.27e-34

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 134.99  E-value: 1.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   1 MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSeFNVYSQEVITVLGEIDFMLENLPEWVT 80
Cdd:PRK13968   31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP-INQARAEVAKSANLCDWYAEHGPAMLK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  81 AKPVkknvLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDL 159
Cdd:PRK13968  110 AEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgIPQGV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 160 YIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCG 238
Cdd:PRK13968  186 YGWLNADNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTG 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 QTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERI--INLR---HFKRILSLLEGQKIAFGGETDE-ATR 311
Cdd:PRK13968  266 QVCAAAKRFIIEEGIASAFTERFVAAAAALkMGDPRDEENALGPMarFDLRdelHHQVEATLAEGARLLLGGEKIAgAGN 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 312 YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimh 391
Cdd:PRK13968  346 YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV-------- 417
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1595488123 392 fTLNSF-------PFGGVGSSGMG---AYHGKHSF 416
Cdd:PRK13968  418 -FINGYcasdarvAFGGVKKSGFGrelSHFGLHEF 451
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
89-429 1.05e-33

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.


Pssm-ID: 143434 [Multi-domain]  Cd Length: 479  Bit Score: 132.58  E-value: 1.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  89 LTMLDE---AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVING 165
Cdd:cd07116   121 ISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNG 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 -GVEETTELL-KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSP-----CYIDKDcdlDIVCRRITWGKYM--- 235
Cdd:cd07116   201 fGLEAGKPLAsSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffaDVMDAD---DAFFDKALEGFVMfal 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 236 NCGQTCIAPDYILCEASLQNQIVWKIKETVKEFygenIKESP-DYERII----NLRHFKRILSLL-----EGQKIAFGGE 305
Cdd:cd07116   278 NQGEVCTCPSRALIQESIYDRFMERALERVKAI----KQGNPlDTETMIgaqaSLEQLEKILSYIdigkeEGAEVLTGGE 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 306 -----TDEATRYIAPTVLTDVDpKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 380
Cdd:cd07116   354 rnelgGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQA 432
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1595488123 381 GGVTGNdvIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRpCLLKS 429
Cdd:cd07116   433 GRVWTN--CYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK-NLLVS 478
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
100-419 1.50e-33

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 132.34  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVING-----GVEETTEL 173
Cdd:PRK11241  145 QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGELTSNP 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQRFDhifYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PRK11241  225 LVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRIL-----SLLEGQKIAFGGETDE-ATRYIAPTVLTDVDPKTK 326
Cdd:PRK11241  302 YDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAK 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 327 VMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNsfPFGGVGSSG 406
Cdd:PRK11241  382 VAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASG 459
                         330
                  ....*....|...
gi 1595488123 407 MGAYHGKHSFDTF 419
Cdd:PRK11241  460 LGREGSKYGIEDY 472
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
5-406 5.05e-33

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 130.08  E-value: 5.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNvySQ-EVITVLGEIDFML----ENLPEWV 79
Cdd:cd07095     6 VAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWE--AQtEVAAMAGKIDISIkayhERTGERA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  80 TAKPVKKNVLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL-PQYLDQD 158
Cdd:cd07095    84 TPMAQGRAVLRH--------RPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 159 LYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDKDCDLDIVCRRITWGKY 234
Cdd:cd07095   156 VLNLVQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 235 MNCGQTC------IAPDYILCEASLQnQIVWKIKETV-------KEFYGENI--KESPDYERIINLRHFKRILSLLEGQK 299
Cdd:cd07095   234 LTAGQRCtcarrlIVPDGAVGDAFLE-RLVEAAKRLRigapdaePPFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMER 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 300 IafggetDEATRYIAPTVLtDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETS 379
Cdd:cd07095   313 L------VAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
                         410       420
                  ....*....|....*....|....*..
gi 1595488123 380 SGGVTGNDVIMhFTLNSFPFGGVGSSG 406
Cdd:cd07095   386 AGIVNWNRPTT-GASSTAPFGGVGLSG 411
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
1-411 6.74e-29

methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130783  Cd Length: 477  Bit Score: 118.83  E-value: 6.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   1 MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVysqevitvLGEIDFMLE------N 74
Cdd:TIGR01722  40 VDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDA--------LGDVARGLEvvehacG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  75 LPEWVTAKPVKkNVLTMLDEAYIQpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY 154
Cdd:TIGR01722 112 VNSLLKGETST-QVATRVDVYSIR-QPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 155 -LDQDLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWG 232
Cdd:TIGR01722 190 gAPDGVLNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGA 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 233 KYMNCGQTCIAPDYILCEASLQnQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG-- 304
Cdd:TIGR01722 270 AYGAAGQRCMAISAAVLVGAAD-EWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLIaggaaEGAEVLLDGrg 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 305 ---ETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSG 381
Cdd:TIGR01722 349 ykvDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVG 428
                         410       420       430
                  ....*....|....*....|....*....|
gi 1595488123 382 GVtGNDVIMHFTLNSFPFGGVGSSGMGAYH 411
Cdd:TIGR01722 429 QV-GVNVPIPVPLPYFSFTGWKDSFFGDHH 457
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
98-380 1.83e-27

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 114.61  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  98 QPQPLGVVLIIGAWNYPF-VLTIQPLIGAIAaGNAVIIKPSELSENTA----KILAKLLPQY-LDQDLYIVINGGVEETT 171
Cdd:cd07130   129 QWNPLGVVGVITAFNFPVaVWGWNAAIALVC-GNVVVWKPSPTTPLTAiavtKIVARVLEKNgLPGAIASLVCGGADVGE 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLK-QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILce 250
Cdd:cd07130   208 ALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI-- 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 251 asLQNQIVWKIKETVKEFY-----GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE-TDEATRYIAPTVLT 319
Cdd:cd07130   286 --VHESIYDEVLERLKKAYkqvriGDPLDDGTLVGPLHTKAAVDNYLAAIEeaksqGGTVLFGGKvIDGPGNYVEPTIVE 363
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595488123 320 dVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 380
Cdd:cd07130   364 -GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGS 423
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
95-408 4.40e-27

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 113.28  E-value: 4.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYLDQDLYIVINGGVEE 169
Cdd:cd07148   118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLlheagLPEGWCQAVPCENAVAEKL 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 170 TTEllkQRFDHIFYTGNTAVGKIVMEAAAKHlTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07148   198 VTD---PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRYiAPTVLTDVDP 323
Cdd:cd07148   274 PAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEEWVNeavaaGARLLCGGKRLSDTTY-APTVLLDPPR 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 324 KTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimH--FTLNSFPFGG 401
Cdd:cd07148   353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaFRVDWMPFAG 429

                  ....*..
gi 1595488123 402 VGSSGMG 408
Cdd:cd07148   430 RRQSGYG 436
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
94-416 1.20e-26

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 112.14  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL-----PQYLDQDLyIVINGGVE 168
Cdd:PRK09406  116 RAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFrragfPDGCFQTL-LVGSGAVE 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETteLLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYIL 248
Cdd:PRK09406  195 AI--LRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFI 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 249 CEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET-DEATRYIAPTVLTDV 321
Cdd:PRK09406  273 VHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQVDdavaaGATILCGGKRpDGPGWFYPPTVITDI 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 322 DPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSFPFGG 401
Cdd:PRK09406  353 TPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFGG 430
                         330
                  ....*....|....*...
gi 1595488123 402 VGSSGMG---AYHGKHSF 416
Cdd:PRK09406  431 VKRSGYGrelSAHGIREF 448
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
101-384 7.44e-25

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.


Pssm-ID: 143403 [Multi-domain]  Cd Length: 442  Bit Score: 106.55  E-value: 7.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQ--YLDQDLYIVINGGVEETTELLKQ-R 177
Cdd:cd07084   100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVmeAAAKHLTPVTLELGGKSPCYIDKDCD-LDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07084   180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKT 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 ivwKIKETVKEFYGENIKESPDYERIINLRHFKRILSL--LEGQKIAFGGETDEATRY-------IAPTVLTDVDP---K 324
Cdd:cd07084   258 ---PLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIpsiygacVASALFVPIDEilkT 334
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEA-INFINEREK-PLALYVFSHNHKLIKRMIDETSSGGVT 384
Cdd:cd07084   335 YELVTEEIFGPFAIVVEYKKDQLAlVLELLERMHgSLTAAIYSNDPIFLQELIGNLWVAGRT 396
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
101-409 1.14e-23

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 103.68  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYLDQdlyiVINGGVEETTELLK 175
Cdd:PLN00412  158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCfhlagFPKGLIS----CVTGKGSEIGDFLT 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 176 QR--FDHIFYTGNTAVGKIVMEAAakhLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PLN00412  234 MHpgVNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESV 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEG--QKIA-FGGETDEATRYIAPTVLTDVDPKTKVMQE 330
Cdd:PLN00412  311 ADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDakEKGAtFCQEWKREGNLIWPLLLDNVRPDMRIAWE 390
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488123 331 EIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlNSFPFGGVGSSGMGA 409
Cdd:PLN00412  391 EPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGP-DHFPFQGLKDSGIGS 468
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
2-406 7.10e-23

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 101.19  E-value: 7.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSqEVITVLGEIDFML----ENLPE 77
Cdd:PRK09457   40 DAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT-EVTAMINKIAISIqayhERTGE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  78 WVTAKPVKKNVLtmldeayiQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LP 152
Cdd:PRK09457  119 KRSEMADGAAVL--------RHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLP 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 153 QYldqdlyiVIN---GGVEETTELLKQR-FDHIFYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDKDCDLDIV 225
Cdd:PRK09457  191 AG-------VLNlvqGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAA 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 226 CRRITWGKYMNCGQTCIAPDYILCEASLQNQ-IVWKIKETVK-----EFYGEnikESPDYERIINLRHFKRilsLLEGQK 299
Cdd:PRK09457  262 VHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKrltvgRWDAE---PQPFMGAVISEQAAQG---LVAAQA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 300 --IAFGGET-------DEATRYIAPTVLtDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKL 370
Cdd:PRK09457  336 qlLALGGKSllemtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDRED 414
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1595488123 371 IKRMIDETSSGGVTGNDvimhfTLN----SFPFGGVGSSG 406
Cdd:PRK09457  415 YDQFLLEIRAGIVNWNK-----PLTgassAAPFGGVGASG 449
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
5-409 9.32e-20

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 91.87  E-value: 9.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGE----IDF-------MLE 73
Cdd:cd07125    75 LAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKT--------LADADAEvreaIDFcryyaaqARE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  74 NLPEWVTAKPV-KKNVLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL- 151
Cdd:cd07125   147 LFSDPELPGPTgELNGLEL--------HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLh 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 152 ----PQYLdqdLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKH---LTPVTLELGGKSPCYIDKDCDLD 223
Cdd:cd07125   219 eagvPRDV---LQLVPGDGEEIGEALVAHpRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPE 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 224 IVCRRITWGKYMNCGQTC-----------IAPDYI--LCEASLQNQI--VWKIKETVkefyGENIKESpdyeriiNLRHF 288
Cdd:cd07125   296 QAVKDVVQSAFGSAGQRCsalrllylqeeIAERFIemLKGAMASLKVgdPWDLSTDV----GPLIDKP-------AGKLL 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 289 KRILSLLEGQK--IAFGGETDEATRYIAPTVLTDVdpKTKVMQEEIFGPILPIV--PVKNVDEAINFINEREKPLALYVF 364
Cdd:cd07125   365 RAHTELMRGEAwlIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIH 442
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1595488123 365 SHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGA 409
Cdd:cd07125   443 SRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP 487
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
5-421 3.96e-19

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 90.19  E-value: 3.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   5 VRRVRQAFLSGRSRPL----RFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVY-SQEVIT-VLGEIDF-MLENLPe 77
Cdd:PLN02419  157 VSAAKQAFPLWRNTPIttrqRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFrGLEVVEhACGMATLqMGEYLP- 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  78 wvtakpvkkNVLTMLDEAYIQpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQ 157
Cdd:PLN02419  236 ---------NVSNGVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLP 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 158 DLYIVINGGVEETTELL--KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYM 235
Cdd:PLN02419  306 DGVLNIVHGTNDTVNAIcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFG 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 236 NCGQTCIAPDYILC---EASLQNQIVWKIKeTVKEFYGEniKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET- 306
Cdd:PLN02419  386 AAGQRCMALSTVVFvgdAKSWEDKLVERAK-ALKVTCGS--EPDADLGPVISKQAKERICRLIQsgvddGAKLLLDGRDi 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 ----DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGG 382
Cdd:PLN02419  463 vvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQ 542
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1595488123 383 VtGNDVIMHFTLNSFPFGGVGSSGMG--AYHGKHSFDTFSH 421
Cdd:PLN02419  543 I-GINVPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
101-425 1.47e-17

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 85.27  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYP-FVLTIQPLIgAIAAGNAVIIK--PSE--LSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELL 174
Cdd:PLN02315  154 PLGIVGVITAFNFPcAVLGWNACI-ALVCGNCVVWKgaPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCGGAEIGEAIA 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 KQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PLN02315  233 KDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEF-YGENIKES----PDYERIiNLRHFKRILSLLEGQ--KIAFGGETDEAT-RYIAPTVLtDVDPKT 325
Cdd:PLN02315  313 YDDVLEQLLTVYKQVkIGDPLEKGtllgPLHTPE-SKKNFEKGIEIIKSQggKILTGGSAIESEgNFVQPTIV-EISPDA 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSG-GVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:PLN02315  391 DVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDcGIVNVNIPTNGAEIGGAFGGEKA 470
                         330       340
                  ....*....|....*....|.
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPC 425
Cdd:PLN02315  471 TGGGREAGSDSWKQYMRRSTC 491
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
100-412 2.61e-17

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273518 [Multi-domain]  Cd Length: 500  Bit Score: 84.19  E-value: 2.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQ--YLDQDLYIVINGGVEETTELLK-Q 176
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEagFPAGTIQLLPGRGADVGAALTSdP 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHL---TPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLEGQKiAFGGETDEATR----------YIAPTV--LTD 320
Cdd:TIGR01238 319 ADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMS-QTQKKIAQLTLddsracqhgtFVAPTLfeLDD 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPktkvMQEEIFGPILPIVPVK--NVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFP 398
Cdd:TIGR01238 398 IAE----LSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQP 473
                         330
                  ....*....|....
gi 1595488123 399 FGGVGSSGMGAYHG 412
Cdd:TIGR01238 474 FGGQGLSGTGPKAG 487
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
98-406 1.96e-13

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.


Pssm-ID: 143441 [Multi-domain]  Cd Length: 522  Bit Score: 72.23  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  98 QPQPLGVVliIGAWN---Y-P---FVLTIQPL-IGAIAA---------GNAVIIKPSelseNTAkilakLLPQYLDQDLY 160
Cdd:cd07123   151 AQQPLSSP--AGVWNrleYrPlegFVYAVSPFnFTAIGGnlagapalmGNVVLWKPS----DTA-----VLSNYLVYKIL 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 161 I-------VIN---GGVEETTELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLT-----P-VTLELGGKSPCYIDKDCDL 222
Cdd:cd07123   220 EeaglppgVINfvpGDGPVVGDTVLASphLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADV 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 223 DIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEfygenIKESPDYE------RIINLRHFKRILSLLE 296
Cdd:cd07123   300 DSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKE-----IKMGDPDDfsnfmgAVIDEKAFDRIKGYID 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 297 ------GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPI--VPVKNVDEAINFINEREkPLALY--VFS 365
Cdd:cd07123   375 haksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVLTVyvYPDSDFEETLELVDTTS-PYALTgaIFA 453
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1595488123 366 HNHKLIKRM------------IDETSSGGVTGNDvimhftlnsfPFGGVGSSG 406
Cdd:cd07123   454 QDRKAIREAtdalrnaagnfyINDKPTGAVVGQQ----------PFGGARASG 496
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
94-349 2.26e-09

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 59.16  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  94 EAYIQPQPLGVVLIIGAWNYPfVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLpqyldQDlyIVINGGVEETTEL 173
Cdd:cd07077    93 ETYVRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLF-----QA--ADAAHGPKILVLY 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQR-------------FDHIFYTGntavGKIVMEAAAKH--LTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMncg 238
Cdd:cd07077   165 VPHPsdelaeellshpkIDLIVATG----GRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFF--- 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 qtciapDYILCeASLQNQIVwkiketVKEFYgenikeSPDYERIInLRHFKRILSLLEGQKIAFGGETDEATryiaPTVL 318
Cdd:cd07077   238 ------DQNAC-ASEQNLYV------VDDVL------DPLYEEFK-LKLVVEGLKVPQETKPLSKETTPSFD----DEAL 293
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1595488123 319 tdvdpktkvmqeEIFGPILPIVPVKNVDEAI 349
Cdd:cd07077   294 ------------ESMTPLECQFRVLDVISAV 312
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
101-408 2.68e-08

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 56.52  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPselSENTAKILAkllpqyldQDLYIVINGGV-EETTELL----- 174
Cdd:PRK11809   768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKP---AEQTPLIAA--------QAVRILLEAGVpAGVVQLLpgrge 836
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  175 --------KQRFDHIFYTGNTAVGKIVMEAAAKHL------TPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT 240
Cdd:PRK11809   837 tvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQR 916
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  241 CIAPDyILCeasLQNQIVWKIKETVKEFYGENIKESPDY-----------ERIINL-RHFKRILSllEGQKI---AFGGE 305
Cdd:PRK11809   917 CSALR-VLC---LQDDVADRTLKMLRGAMAECRMGNPDRlstdigpvidaEAKANIeRHIQAMRA--KGRPVfqaARENS 990
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  306 TDEAT-RYIAPTV--LTDVDPktkvMQEEIFGPILPIV--PVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 380
Cdd:PRK11809   991 EDWQSgTFVPPTLieLDSFDE----LKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHV 1066
                          330       340
                   ....*....|....*....|....*...
gi 1595488123  381 GGVTGNDVIMHFTLNSFPFGGVGSSGMG 408
Cdd:PRK11809  1067 GNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
77-383 2.04e-07

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.


Pssm-ID: 143445  Cd Length: 549  Bit Score: 53.25  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  77 EWVtaKPVKKNVLTMLDEAYiQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELS----ENTAKILAKLLP 152
Cdd:cd07127   172 EWE--KPQGKHDPLAMEKTF-TVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLA 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 153 QY-LDQDLYIVInggVEETTELLKQRF-DH-----IFYTGNTAVGKIvMEAAAKHLTPVTlELGGKSPCYIDKDCDLDIV 225
Cdd:cd07127   249 EAgFDPNLVTLA---ADTPEEPIAQTLaTRpevriIDFTGSNAFGDW-LEANARQAQVYT-EKAGVNTVVVDSTDDLKAM 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 226 CRRITWGKYMNCGQTCIAPDYILCEAS-LQNQIVWK--------IKETVKEFYGENIK--------ESPD-YERIINLRH 287
Cdd:cd07127   324 LRNLAFSLSLYSGQMCTTPQNIYVPRDgIQTDDGRKsfdevaadLAAAIDGLLADPARaaallgaiQSPDtLARIAEARQ 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 288 FKRIlsLLEGQKIAFGGETDEATRyiAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINE--REK-PLALYVF 364
Cdd:cd07127   404 LGEV--LLASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVY 479
                         330
                  ....*....|....*....
gi 1595488123 365 SHNHKLIKRMIDETSSGGV 383
Cdd:cd07127   480 STDPEVVERVQEAALDAGV 498
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
101-356 2.12e-07

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.


Pssm-ID: 143447 [Multi-domain]  Cd Length: 454  Bit Score: 53.31  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIqplIG-----AIAAGNAVIIK--PS--ELSENTAK-ILAKLLPQYLDQDLYIVINGGVEET 170
Cdd:cd07129   105 PLGPVAVFGASNFPLAFSV---AGgdtasALAAGCPVVVKahPAhpGTSELVARaIRAALRATGLPAGVFSLLQGGGREV 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 171 TELLKQrfdH-----IFYTGNTAVGKIVMEAAAKHLT--PVTLELGGKSPCYI-------DKDCDLDIVCRRITwgkyMN 236
Cdd:cd07129   182 GVALVK---HpaikaVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFIlpgalaeRGEAIAQGFVGSLT----LG 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 CGQTC------IAPDYILCEASLQnqivwKIKETVKEFYG-----ENIKESpdYERIINlrhfkRILSLLEGQKIAFGGE 305
Cdd:cd07129   255 AGQFCtnpglvLVPAGPAGDAFIA-----ALAEALAAAPAqtmltPGIAEA--YRQGVE-----ALAAAPGVRVLAGGAA 322
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595488123 306 TDEATRYiAPTVL-TDVDP--KTKVMQEEIFGPILPIVPVKNVDEAINFINERE 356
Cdd:cd07129   323 AEGGNQA-APTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
ALDH_F18-19_ProA-GPR cd07079
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ...
6-354 1.47e-06

Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).


Pssm-ID: 143398  Cd Length: 406  Bit Score: 50.51  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123   6 RRVRQAFLsgrsrplrfRLQQL------EALRRM---VQEREKDILTAIAADLCKSEFNVYSQEVIT--VLGE--IDFML 72
Cdd:cd07079     5 KRAKAASR---------ALATLsteqknAALLAIadaLEANRDEILEANAKDLAAAREAGLSEALLDrlLLTPerIEAMA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  73 E------NLPEwvtakPVKKnVLTM--LD---EAYIQPQPLGVVLIIgawnY---PFVlTIQPLIGAIAAGNAVIIKPSE 138
Cdd:cd07079    76 EglrqvaALPD-----PVGE-VLRGwtLPnglQIEKVRVPLGVIGII----YesrPNV-TVDAAALCLKSGNAVILRGGS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 139 LSENTAKILAKLLPQ-----YLDQDLYIVI-NGGVEETTELLKQRfDH----IFYTGNTAVGKIVMEAaakhLTPVtLEl 208
Cdd:cd07079   145 EALHSNRALVEIIQEaleeaGLPEDAVQLIpDTDREAVQELLKLD-DYidliIPRGGAGLIRFVVENA----TIPV-IK- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 209 GGKSPC--YIDKDCDLDIVCRRITWGKYMNCGqTCIAPDYILCEASLQNQIVWKIKETVKEfygENIKespdyeriinLR 286
Cdd:cd07079   218 HGDGNChvYVDESADLEMAVRIVVNAKTQRPS-VCNALETLLVHRDIAEEFLPKLAEALRE---AGVE----------LR 283
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488123 287 HFKRILSLLEGQKIAfgGETDEATRYIAptvltdvdpktkvmqeeifgPILPIVPVKNVDEAINFINE 354
Cdd:cd07079   284 GDEETLAILPGAKPA--TEEDWGTEYLD--------------------LILAVKVVDSLDEAIAHINR 329
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
101-381 1.58e-06

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.


Pssm-ID: 143444  Cd Length: 489  Bit Score: 50.57  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKP----SELSENTAKILAKL-LPQyldQDLYIVINGGVEETTELLK 175
Cdd:cd07126   142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVdskvSVVMEQFLRLLHLCgMPA---TDVDLIHSDGPTMNKILLE 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 176 QRFDHIFYTGNTAV---------GKIVMEAAA---KHLTPVTLELGgkspcYIDKDCDLDivcrritwgKYMNCGQTCIA 243
Cdd:cd07126   219 ANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQD---------AYACSGQKCSA 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILC-EASLQNQIVWKIKETVKEFYGENIKESP----DYERIINlrHFKRILSlLEGQKIAFGGEtdEATRYIAPTVL 318
Cdd:cd07126   285 QSILFAhENWVQAGILDKLKALAEQRKLEDLTIGPvltwTTERILD--HVDKLLA-IPGAKVLFGGK--PLTNHSIPSIY 359
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488123 319 TDVDP-------KTKVMQE-------EIFGPILPIVPVKNVDEAINF-INER-EKPLALYVFSHNHKLIKRMIDETSSG 381
Cdd:cd07126   360 GAYEPtavfvplEEIAIEEnfelvttEVFGPFQVVTEYKDEQLPLVLeALERmHAHLTAAVVSNDIRFLQEVLANTVNG 438
LuxC pfam05893
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ...
93-383 2.34e-06

Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.


Pssm-ID: 399113  Cd Length: 401  Bit Score: 49.75  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  93 DEAYIQPQPLGVVLIIGAWNYPfVLTIQPLIGAIAAGNAVIIKPSElSEN--TAKILAKLLPQYLDQDL--YIVI---NG 165
Cdd:pfam05893  80 KPSYEKAFPPGLVFHVLSGNVP-LLPVMSILMGLLVKNVNLLKVSS-SDPftAAALLASFADLDPTHPLadSLSVvywDG 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLKQRFDHIF-YTGNTAVgkivmEAAAKHLTPVT--LELGGK-SPCYIDKDCDLDIVCRRI-----TWGKymn 236
Cdd:pfam05893 158 GSTQLEDLIVANADVVIaWGGEDAI-----NAIRECLKPGKqwIDFGAKiSFAVVDREAALDKAAERAaddicVFDQ--- 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 cgQTCIAPDYILCEASLQNQivwkIKETVKEFYGENIKESPDYER----------IINLRHFKRILSLLEGQkiaFGGET 306
Cdd:pfam05893 230 --QACLSPQTVFVESDDKIT----PDEFAERLAAALAKRARILPKavldideaakISSDRAECKLDYAFAGE---RGVWS 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 DEATRYiapTVLTDVDpktkvmQEEIFGPI---LPIVPVKNVDEAINFINEREKPL---ALYVFSHNhklIKRMIDETSS 380
Cdd:pfam05893 301 DFHQRW---TVIWSDG------QEELNSPLnrtVNVVPVPSLSDVVRYVSENRTYLqtcGLAPYSGR---LPYLDRKLAL 368

                  ...
gi 1595488123 381 GGV 383
Cdd:pfam05893 369 AGV 371
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
103-375 8.36e-06

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.


Pssm-ID: 143446 [Multi-domain]  Cd Length: 513  Bit Score: 48.03  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 103 GVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKP----SELSENTAKIL--AKLLPQYLDQdlyiVINGGVEETTELLkQ 176
Cdd:cd07128   146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPatatAYLTEAVVKDIveSGLLPEGALQ----LICGSVGDLLDHL-G 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKI--VMEAAAKHLTPVTLELGGKSPCYIDKDC-------DLDI--VCRRITwgkyMNCGQTCIAPD 245
Cdd:cd07128   221 EQDVVAFTGSAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpefDLFVkeVAREMT----VKAGQKCTAIR 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 246 YILCEASLQNQIVWKIKE-TVKEFYGENIKESPDYERIINLRHF----KRILSLLEGQKIAFGGETDEATR--------Y 312
Cdd:cd07128   297 RAFVPEARVDAVIEALKArLAKVVVGDPRLEGVRMGPLVSREQRedvrAAVATLLAEAEVVFGGPDRFEVVgadaekgaF 376
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595488123 313 IAPTVLT--DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMI 375
Cdd:cd07128   377 FPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
100-138 1.08e-05

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 48.01  E-value: 1.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1595488123  100 QPLGVVLIIGAWNYPfvLTIqpLIG----AIAAGNAVIIKPSE 138
Cdd:COG4230    679 RGRGVFVCISPWNFP--LAI--FTGqvaaALAAGNTVLAKPAE 717
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
97-349 2.19e-05

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143400 [Multi-domain]  Cd Length: 439  Bit Score: 46.88  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  97 IQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYL-----DQDLYIVINGGVEETT 171
Cdd:cd07081    91 IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAvaagaPENLIGWIDNPSIELA 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQR--FDHIFYTGntavGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07081   171 QRLMKFpgIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIV--------WKIK----ETVKEFYGENIKESPDyerIINLRHFKriLSLLEGQKIAfggetdEATR--YIAP 315
Cdd:cd07081   247 VDSVYDEVMrlfegqgaYKLTaeelQQVQPVILKNGDVNRD---IVGQDAYK--IAAAAGLKVP------QETRilIGEV 315
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1595488123 316 TVLTDVDPktkvMQEEIFGPILPIVPVKNVDEAI 349
Cdd:cd07081   316 TSLAEHEP----FAHEKLSPVLAMYRAANFADAD 345
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
100-138 1.20e-04

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 44.86  E-value: 1.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1595488123  100 QPLGVVLIIGAWNYPfvLTIqpLIG----AIAAGNAVIIKPSE 138
Cdd:PRK11905   675 KPLGPVVCISPWNFP--LAI--FTGqiaaALVAGNTVLAKPAE 713
ALDH_EutE cd07121
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ...
123-357 4.73e-04

Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.


Pssm-ID: 143439 [Multi-domain]  Cd Length: 429  Bit Score: 42.61  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 123 IGAIAAGNAVIIKPSELSENTAKILAKLLPQYldqdlyIVINGG-------VEE-TTELLKQRFDH-----IFYTGNTAV 189
Cdd:cd07121   119 ISMLAAGNAVVFNPHPGAKKVSAYAVELINKA------IAEAGGpdnlvvtVEEpTIETTNELMAHpdinlLVVTGGPAV 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 190 GKIVMEAAAKhltpvtlELG---GKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKEtVK 266
Cdd:cd07121   193 VKAALSSGKK-------AIGagaGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQR-NG 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 267 EFYGENIKESPDYERIINLRHFKRILSLLEGQ---KIA--FGGETDEATRYIaptvLTDVDPKTKVMQEEIFGPILPIVP 341
Cdd:cd07121   265 AYVLNDEQAEQLLEVVLLTNKGATPNKKWVGKdasKILkaAGIEVPADIRLI----IVETDKDHPFVVEEQMMPILPVVR 340
                         250
                  ....*....|....*.
gi 1595488123 342 VKNVDEAINFINEREK 357
Cdd:cd07121   341 VKNFDEAIELAVELEH 356
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
100-138 2.51e-03

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 40.57  E-value: 2.51e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1595488123  100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSE 138
Cdd:PRK11904   683 HGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE 721
PRK15398 PRK15398
aldehyde dehydrogenase;
301-349 3.95e-03

aldehyde dehydrogenase;


Pssm-ID: 237956  Cd Length: 465  Bit Score: 39.50  E-value: 3.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1595488123 301 AFGGETDEATRYIaptvLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAI 349
Cdd:PRK15398  334 AAGINVPKDTRLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAI 378
ALDH_F20_ACDH cd07122
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ...
99-258 6.10e-03

Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143440 [Multi-domain]  Cd Length: 436  Bit Score: 39.01  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123  99 PQPLGVVL-IIGAWNyPFVLTIQPLIGAIAAGNAVIIKPS----ELSENTAKILAKLLPQY-LDQDLYIVI-NGGVEETT 171
Cdd:cd07122    93 AEPVGVIAaLIPSTN-PTSTAIFKALIALKTRNAIIFSPHprakKCSIEAAKIMREAAVAAgAPEGLIQWIeEPSIELTQ 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQR-FDHIFYTGNTAVGKivmeAAAKHLTPVtleLG---GKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07122   172 ELMKHPdVDLILATGGPGMVK----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSV 244
                         170
                  ....*....|.
gi 1595488123 248 LCEASLQNQIV 258
Cdd:cd07122   245 IVDDEIYDEVR 255
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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