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Conserved domains on  [gi|515870067|ref|NP_001265523|]
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methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial isoform 3 [Homo sapiens]

Protein Classification

CoA-acylating methylmalonate-semialdehyde dehydrogenase( domain architecture ID 10162887)

CoA-acylating methylmalonate-semialdehyde dehydrogenase catalyzes the NAD-dependent decarboxylation of methylmalonate semialdehyde to propionyl-CoA

CATH:  3.40.605.10
EC:  1.2.1.-
PubMed:  15272169
SCOP:  4000806

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
1-362 0e+00

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: 732.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07085  116 LKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGV 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07085  196 LNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAG 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMALSTAVLVG-EAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGY 239
Cdd:cd07085  276 QRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGY 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:cd07085  356 ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV 435
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 515870067 320 PIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:cd07085  436 PIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
 
Name Accession Description Interval E-value
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
1-362 0e+00

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: 732.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07085  116 LKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGV 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07085  196 LNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAG 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMALSTAVLVG-EAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGY 239
Cdd:cd07085  276 QRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGY 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:cd07085  356 ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV 435
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 515870067 320 PIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:cd07085  436 PIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
1-362 0e+00

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: 691.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067    1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:TIGR01722 116 LKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   81 LNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:TIGR01722 196 LNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  161 QRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYE 240
Cdd:TIGR01722 276 QRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYE 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  241 NGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVP 320
Cdd:TIGR01722 356 EGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 515870067  321 IPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:TIGR01722 436 IPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
2-378 0e+00

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 534.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   2 MGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PLN02419 230 MGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  82 NIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:PLN02419 310 NIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQ 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 162 RCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYEN 241
Cdd:PLN02419 390 RCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEK 469
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 242 GNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPI 321
Cdd:PLN02419 470 GNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI 549
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515870067 322 PVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSspaVVMPT 378
Cdd:PLN02419 550 PVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKDIHSPFS---LAIPI 603
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
1-362 7.10e-141

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: 409.13  E-value: 7.10e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:COG1012  121 LYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGV 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:COG1012  201 LNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNA 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVkg 238
Cdd:COG1012  281 GQRCTAASRLLVHESiYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG-- 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 yENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:COG1012  359 -EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWIN 437
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 515870067 319 VPIPVPLPMFSFTGSRSSFRGDtnFYGKQGIQFYTQLKTITSQW 362
Cdd:COG1012  438 DGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVTIRL 479
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
1-358 8.03e-136

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: 395.36  E-value: 8.03e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067    1 MMGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:pfam00171 107 LDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   81 LNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:pfam00171 186 LNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNA 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  160 GQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvk 237
Cdd:pfam00171 266 GQVCTATSR-LLVHEsiYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEA---- 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  238 GYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGV 317
Cdd:pfam00171 341 GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWI 420
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 515870067  318 NVPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:pfam00171 421 NDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
 
Name Accession Description Interval E-value
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
1-362 0e+00

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: 732.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07085  116 LKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGV 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07085  196 LNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAG 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMALSTAVLVG-EAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGY 239
Cdd:cd07085  276 QRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGY 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:cd07085  356 ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV 435
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 515870067 320 PIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:cd07085  436 PIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
1-362 0e+00

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: 691.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067    1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:TIGR01722 116 LKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   81 LNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:TIGR01722 196 LNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  161 QRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYE 240
Cdd:TIGR01722 276 QRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYE 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  241 NGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVP 320
Cdd:TIGR01722 356 EGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 515870067  321 IPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:TIGR01722 436 IPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
2-378 0e+00

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 534.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   2 MGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PLN02419 230 MGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  82 NIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:PLN02419 310 NIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQ 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 162 RCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYEN 241
Cdd:PLN02419 390 RCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEK 469
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 242 GNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPI 321
Cdd:PLN02419 470 GNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI 549
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515870067 322 PVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSspaVVMPT 378
Cdd:PLN02419 550 PVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKDIHSPFS---LAIPI 603
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
1-362 7.10e-141

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: 409.13  E-value: 7.10e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:COG1012  121 LYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGV 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:COG1012  201 LNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNA 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVkg 238
Cdd:COG1012  281 GQRCTAASRLLVHESiYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG-- 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 yENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:COG1012  359 -EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWIN 437
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 515870067 319 VPIPVPLPMFSFTGSRSSFRGDtnFYGKQGIQFYTQLKTITSQW 362
Cdd:COG1012  438 DGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVTIRL 479
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
1-358 8.03e-136

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: 395.36  E-value: 8.03e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067    1 MMGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:pfam00171 107 LDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   81 LNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:pfam00171 186 LNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNA 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  160 GQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvk 237
Cdd:pfam00171 266 GQVCTATSR-LLVHEsiYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEA---- 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  238 GYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGV 317
Cdd:pfam00171 341 GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWI 420
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 515870067  318 NVPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:pfam00171 421 NDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
1-359 1.58e-110

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: 329.94  E-value: 1.58e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07078   76 LHGEVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGV 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07078  156 LNVVTGdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALStAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkiKVK 237
Cdd:cd07078  236 GQVCTAAS-RLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRL 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 238 GYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGV 317
Cdd:cd07078  312 EGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWI 391
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 515870067 318 NVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07078  392 NDYSVGAEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
1-359 2.30e-102

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: 310.82  E-value: 2.30e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07131  115 LFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGV 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07131  195 VNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTT 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG 238
Cdd:cd07131  275 GQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGG 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 YENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07131  355 YEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN 434
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 515870067 319 VPI---PVPLPmF-----SFTGSRSSfrgdtnfyGKQGIQFYTQLKTIT 359
Cdd:cd07131  435 APTigaEVHLP-FggvkkSGNGHREA--------GTTALDAFTEWKAVY 474
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
1-358 2.26e-88

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: 274.51  E-value: 2.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07097  115 LSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGV 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07097  195 FNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFST 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALSTAVLV-GEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIkvKG 238
Cdd:cd07097  275 GQRCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERL--KR 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 YENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07097  353 PDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN 432
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 515870067 319 VP-----IPVPlpmfsFTGSRSSFRGdtnfYGKQG---IQFYTQLKTI 358
Cdd:cd07097  433 LPtagvdYHVP-----FGGRKGSSYG----PREQGeaaLEFYTTIKTV 471
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
1-320 5.78e-88

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: 273.67  E-value: 5.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGA 76
Cdd:cd07086  113 LYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPltaiAVTKILAEVLEKNGL 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  77 PDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAF 156
Cdd:cd07086  193 PPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAV 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 157 GAAGQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIk 235
Cdd:cd07086  273 GTAGQRCTTTRRLIVhESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRI- 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 236 vKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKY--AHLVDVG 313
Cdd:cd07086  352 -DGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCG 430

                 ....*..
gi 515870067 314 QVGVNVP 320
Cdd:cd07086  431 IVNVNIP 437
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
3-359 2.25e-86

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: 269.05  E-value: 2.25e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07093  100 GESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVN 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07093  179 VVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGE 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 162 RCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGY 239
Cdd:cd07093  259 VCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRPELPDL 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:cd07093  338 EGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNC 417
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 515870067 320 PIPVPLPMfSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07093  418 WLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
1-359 4.20e-80

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: 249.84  E-value: 4.20e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd06534   72 LGGPELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGV 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd06534  152 VNVVPGgGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALSTaVLVGEAkkwlpelvehaknlrvnagdqpgadlgplITPQAKERVCnlidsgtkegasilldgrkikvkgy 239
Cdd:cd06534  232 GQICTAASR-LLVHES-----------------------------IYDEFVEKLV------------------------- 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 engnfvgpTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:cd06534  257 --------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYIND 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 515870067 320 PIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd06534  329 SSIGVGPEAPFGGVKNSGIGREG--GPYGLEEYTRTKTVV 366
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
3-358 4.98e-78

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: 247.46  E-value: 4.98e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07114  101 GAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVN 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07114  181 VVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQ 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 162 RCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGY 239
Cdd:cd07114  261 TCVAGSR-LLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADL 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:cd07114  340 GAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT 419
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 515870067 320 PIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07114  420 YRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
3-359 8.96e-77

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: 243.88  E-value: 8.96e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:cd07103   99 GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVL 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  82 NIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAknHG--VVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07103  178 NVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfIVFDDADLDKAVDGAIASKFRN 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 159 AGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKV 236
Cdd:cd07103  256 AGQTCVC-ANRIYVHEsiYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRLGL 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 237 KGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVG 316
Cdd:cd07103  335 GGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVG 410
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 515870067 317 VNVPIPvPLPMFSFTGSRSSfrGdtnfYG----KQGIQFYTQLKTIT 359
Cdd:cd07103  411 INTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVS 450
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
1-359 2.07e-76

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: 242.44  E-value: 2.07e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDG 79
Cdd:cd07104   78 PEGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  80 TLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07104  158 VLNVVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 159 AGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGAsilldgrKI 234
Cdd:cd07104  238 QGQICMAAGR-ILVHEsvYDEFVEKLVAKAKALPV--GDPrdPDTVIGPLINERQVDRVHAIVEDAVAAGA-------RL 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 235 KVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQ 314
Cdd:cd07104  308 LTGGTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 515870067 315 VGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07104  388 VHINDQTVNDEPHVPFGGVKAS--GGGRFGGPASLEEFTEWQWIT 430
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
3-359 3.11e-72

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: 232.87  E-value: 3.11e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07091  124 GKTIPIDGNFLA-YTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVN 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07091  203 IVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNlKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQG 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG 238
Cdd:cd07091  283 QCCCAGSR-IFVQESiyDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKG 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 YengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07091  362 Y----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN 437
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 515870067 319 VpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07091  438 T-YNVFDAAVPFGGFKQSGFGREL--GEEGLEEYTQVKAVT 475
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
16-358 1.64e-71

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: 230.65  E-value: 1.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFIC 95
Cdd:cd07090  111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLC 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  96 DHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA 175
Cdd:cd07090  191 EHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSN-GTRVFVQRS 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 176 --KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVK-GYENGNFVGPTII 250
Cdd:cd07090  270 ikDEFTERLVERTKKIRI--GDplDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPEdGLENGFYVSPCVL 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 251 SNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN----VPIPVPlp 326
Cdd:cd07090  348 TDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINtyniSPVEVP-- 425
                        330       340       350
                 ....*....|....*....|....*....|..
gi 515870067 327 mfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07090  426 ---FGGYKQSGFGREN--GTAALEHYTQLKTV 452
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
16-359 2.09e-71

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: 231.73  E-value: 2.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFI 94
Cdd:cd07124  162 YVYR-PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYL 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  95 CDHPDIKAISFVGSNKAGEYIFER------GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALST 168
Cdd:cd07124  241 VEHPDVRFIAFTGSREVGLRIYERaakvqpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSR 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 169 AVLVGEA-KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKgyENGNFVGP 247
Cdd:cd07124  321 VIVHESVyDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA--AEGYFVQP 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 248 TIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPM 327
Cdd:cd07124  398 TIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVG 477
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 515870067 328 F-SFTGSRSSfrGDTnfyGKQG-----IQFyTQLKTIT 359
Cdd:cd07124  478 RqPFGGFKMS--GTG---SKAGgpdylLQF-MQPKTVT 509
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
19-358 3.25e-71

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: 229.34  E-value: 3.25e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAVNFICDHP 98
Cdd:cd07106  112 RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHP 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  99 DIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--K 176
Cdd:cd07106  191 DIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKR-LYVHESiyD 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 177 KWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPN 256
Cdd:cd07106  270 EFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEG 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 257 MTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNvPIPVPLPMFSFTGSRSS 336
Cdd:cd07106  346 SRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQS 424
                        330       340
                 ....*....|....*....|..
gi 515870067 337 FRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07106  425 GIGVE--FGIEGLKEYTQTQVI 444
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
3-359 3.97e-71

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: 229.52  E-value: 3.97e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07150  101 GETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFN 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANkentLNQLVG-AAFGA-- 158
Cdd:cd07150  181 VVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD----LDYAVRaAAFGAfm 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 159 -AGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILldgrk 233
Cdd:cd07150  257 hQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKV--GDprDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLL----- 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 234 ikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVG 313
Cdd:cd07150  329 --TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESG 406
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 515870067 314 QVGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07150  407 MVHINDPTILDEAHVPFGGVKAS--GFGREGGEWSMEEFTELKWIT 450
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
3-318 4.83e-71

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: 229.89  E-value: 4.83e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07119  117 GEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVN 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07119  196 LVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQ 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 162 RCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGY 239
Cdd:cd07119  276 VCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDEL 354
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870067 240 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07119  355 AKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
3-358 6.26e-71

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: 229.46  E-value: 6.26e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:cd07088  115 GEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVL 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  82 NIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07088  194 NIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCG 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKV 236
Cdd:cd07088  274 QVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKV--GDpfDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEG 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 237 kgyENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVG 316
Cdd:cd07088  351 ---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETY 427
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 515870067 317 VNVPIPVPLPMFSfTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07088  428 INRENFEAMQGFH-AGWKKSGLGGAD--GKHGLEEYLQTKVV 466
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
19-359 9.69e-71

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: 228.93  E-value: 9.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICD 96
Cdd:cd07138  128 REPIGVCGLITPWNWPLnQIVLKVAP-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSA 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  97 HPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAK 176
Cdd:cd07138  207 HPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 177 kwLPELVEHAK----NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKiKVKGYENGNFVGPTIISN 252
Cdd:cd07138  286 --YAEAEEIAAaaaeAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFAD 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 253 VKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPL-PmfsFT 331
Cdd:cd07138  363 VTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FG 439
                        330       340
                 ....*....|....*....|....*...
gi 515870067 332 GSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07138  440 GYKQS--GNGREWGRYGLEEFLEVKSIQ 465
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
3-359 2.77e-70

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: 226.69  E-value: 2.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07105   80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQ----HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07105  160 VVTHSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 159 AGQRCMalSTA-VLVGE--AKKWLPELVEHAKNLRvnagdQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRkik 235
Cdd:cd07105  240 SGQICM--STErIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGL--- 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 236 VKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQV 315
Cdd:cd07105  310 ADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 515870067 316 GVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07105  390 HINGMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
1-359 3.24e-70

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: 227.22  E-value: 3.24e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07118   99 LHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGV 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNqlvGAAFGA- 158
Cdd:cd07118  179 VNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAAD---AVVFGVy 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 159 --AGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGR 232
Cdd:cd07118  256 fnAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRV--GDplDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGE 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 233 KIkvkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDV 312
Cdd:cd07118  333 RL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRA 409
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 515870067 313 GQVGVNVPIP--VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07118  410 GTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
3-356 5.63e-69

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: 224.30  E-value: 5.63e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067    3 GETMPSITKDmDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:TIGR01804 116 GEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFN 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   83 IIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:TIGR01804 195 VVQGDGAEVgPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQ 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  162 RCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGY 239
Cdd:TIGR01804 275 VCSN-GTRVFVHKKikERFLARLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGL 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  240 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:TIGR01804 354 QNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT 433
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 515870067  320 --PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:TIGR01804 434 ynLYPAEAP---FGGYKQSGIGREN--GKAALAHYTEVK 467
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
3-358 1.54e-68

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: 222.70  E-value: 1.54e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07115  100 GEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLN 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07115  179 VVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQ 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 162 RCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGY 239
Cdd:cd07115  259 MCTAGSR-LLVHEsiYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGARGF 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 engnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:cd07115  338 ----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT 413
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 515870067 320 pipvplpmFSFTGSRSSFRG--DTNF---YGKQGIQFYTQLKTI 358
Cdd:cd07115  414 --------YNRFDPGSPFGGykQSGFgreMGREALDEYTEVKSV 449
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
2-359 2.70e-67

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: 220.30  E-value: 2.70e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   2 MGETMPSitkDMDLYSY-RL-PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDG 79
Cdd:cd07141  127 HGKTIPM---DGDFFTYtRHePVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPG 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  80 TLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFG 157
Cdd:cd07141  204 VVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFF 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 158 AAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIK 235
Cdd:cd07141  284 NMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHG 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 236 VKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQV 315
Cdd:cd07141  363 DKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTV 438
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 515870067 316 GVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07141  439 WVNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTEVKTVT 479
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
1-359 4.94e-67

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: 219.03  E-value: 4.94e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07109   98 LHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGA 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07109  177 LNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNA 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAG-DQPgaDLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKV 236
Cdd:cd07109  257 GQTCSAGSR-LLVHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEG 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 237 KgYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVG 316
Cdd:cd07109  334 A-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVF 412
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 515870067 317 VNVPIP---VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07109  413 VNNYGAgggIELP---FGGVKKSGHGREK--GLEALYNYTQTKTVA 453
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
18-318 6.22e-67

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: 218.98  E-value: 6.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  18 YRLPLGVCAGIAPFNFP------AMIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEA 90
Cdd:cd07082  138 RREPLGVVLAIGPFNYPlnltvsKLIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREI 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  91 VNFICDHPDIKAISFVGSNKAGEYIFERGSRhgKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaV 170
Cdd:cd07082  212 GDPLVTHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-V 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 171 LVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkikvkGYENGNFVGPT 248
Cdd:cd07082  289 LVHEsvADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPT 362
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 249 IISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07082  363 LLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
1-358 5.38e-66

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: 216.89  E-value: 5.38e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07144  125 IQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGV 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07144  204 VNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNS 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALSTaVLVGEA--KKWLPELVEHAK-NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKiKV 236
Cdd:cd07144  284 GQNCTATSR-IYVQESiyDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-AP 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 237 KGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVG 316
Cdd:cd07144  362 EGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVW 441
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 515870067 317 VNVP----IPVPlpmfsFTGSRSSfrGDTNFYGKQGIQFYTQLKTI 358
Cdd:cd07144  442 INSSndsdVGVP-----FGGFKMS--GIGRELGEYGLETYTQTKAV 480
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
16-359 5.84e-66

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: 215.92  E-value: 5.84e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFI 94
Cdd:cd07149  118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDAL 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  95 CDHPDIKAISFVGSNKAGEYIFERGsrhG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVG 173
Cdd:cd07149  198 VTDPRVRMISFTGSPAVGEAIARKA---GlKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQR-IFVH 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 174 EAKK--WLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTI 249
Cdd:cd07149  274 EDIYdeFLERFVAATKKLVV--GDplDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTV 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 250 ISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPipvplpmfs 329
Cdd:cd07149  345 LTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDS--------- 415
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 515870067 330 ftgsrSSFRGDTNFYG--------KQGIQF----YTQLKTIT 359
Cdd:cd07149  416 -----STFRVDHMPYGgvkesgtgREGPRYaieeMTEIKLVC 452
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
3-318 6.92e-66

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: 216.06  E-value: 6.92e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPD 78
Cdd:cd07145  101 GETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPP 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  79 GTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFG 157
Cdd:cd07145  181 GVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFE 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 158 AAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRK 233
Cdd:cd07145  261 NAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKV--GDplDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKR 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 234 IKvkgyenGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVG 313
Cdd:cd07145  338 DE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAG 411

                 ....*
gi 515870067 314 QVGVN 318
Cdd:cd07145  412 GVVIN 416
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
3-360 3.58e-65

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: 213.73  E-value: 3.58e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDsGAPDGTLN 82
Cdd:cd07092  104 GEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVN 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07092  179 VVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQ 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 162 RCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDsGTKEGASILLDGRKIKVKGY 239
Cdd:cd07092  259 DCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE-RAPAHARVLTGGRRAEGPGY 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 engnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:cd07092  337 ----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT 412
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 515870067 320 PIPVPLPMfSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTITS 360
Cdd:cd07092  413 HIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVMV 450
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
3-359 6.12e-65

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: 214.23  E-value: 6.12e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETM-PSIT----KDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPgATML-LAKLLQDSGA 76
Cdd:cd07113  119 GETLaPSIPsmqgERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGI 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  77 PDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAF 156
Cdd:cd07113  198 PDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGF 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 157 GAAGQRCmALSTAVLVGEAKkwLPELVEHAK----NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGR 232
Cdd:cd07113  278 LHQGQVC-AAPERFYVHRSK--FDELVTKLKqalsSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 233 KIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDV 312
Cdd:cd07113  355 ALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEA 430
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 515870067 313 GQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTIT 359
Cdd:cd07113  431 GTVWVNMHTFLD-PAVPFGGMKQSGIGRE--FGSAFIDDYTELKSVM 474
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
19-359 1.75e-64

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: 212.82  E-value: 1.75e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHP 98
Cdd:cd07139  135 REPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHP 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  99 DIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAKK- 177
Cdd:cd07139  215 GVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRYd 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 178 -WLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPN 256
Cdd:cd07139  294 eVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDND 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 257 MTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVP-LPmfsFTGSRS 335
Cdd:cd07139  372 MRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFgAP---FGGFKQ 448
                        330       340
                 ....*....|....*....|....
gi 515870067 336 SfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07139  449 S--GIGREGGPEGLDAYLETKSIY 470
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
5-359 1.05e-63

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: 210.29  E-value: 1.05e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   5 TMPSitKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII 84
Cdd:cd07110  106 PLPS--EDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVV 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  85 HGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC 163
Cdd:cd07110  184 TGTgDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQIC 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 164 MALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYEN 241
Cdd:cd07110  264 SATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRR--PAHLEK 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 242 GNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPI 321
Cdd:cd07110  341 GYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQ 420
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 515870067 322 PVpLPMFSFTG-SRSSFRGDtnfYGKQGIQFYTQLKTIT 359
Cdd:cd07110  421 PC-FPQAPWGGyKRSGIGRE---LGEWGLDNYLEVKQIT 455
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
16-358 2.55e-63

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: 210.08  E-value: 2.55e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFI 94
Cdd:cd07143  139 YTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAI 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  95 CDHPDIKAISFVGSNKAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVG 173
Cdd:cd07143  219 SSHMDIDKVAFTGSTLVGRKVMEAAAKSNlKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVQ 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 174 EA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIIS 251
Cdd:cd07143  298 EGiyDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFT 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 252 NVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPlPMFSFT 331
Cdd:cd07143  374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFG 452
                        330       340
                 ....*....|....*....|....*..
gi 515870067 332 GSRSSFRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07143  453 GYKQSGIGRE--LGEYALENYTQIKAV 477
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
19-358 5.09e-63

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: 208.64  E-value: 5.09e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDH 97
Cdd:cd07089  121 REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTD 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANkentLNQLVGAAFG----AAGQRCmALSTAVLVG 173
Cdd:cd07089  201 PRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVP 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 174 EAKKwlPELVEHAKN----LRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTI 249
Cdd:cd07089  276 RSRY--DEVVEALAAafeaLPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTL 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 250 ISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN----VPIPVPl 325
Cdd:cd07089  352 FADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINggggYGPDAP- 430
                        330       340       350
                 ....*....|....*....|....*....|...
gi 515870067 326 pmfsFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07089  431 ----FGGYKQSGLGRE--NGIEGLEEFLETKSI 457
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
16-359 5.98e-62

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: 205.67  E-value: 5.98e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFI 94
Cdd:cd07146  115 FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDEL 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  95 CDHPDIKAISFVGSNKAGEYIFERGSrhGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE 174
Cdd:cd07146  195 ITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHE 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 175 --AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTII 250
Cdd:cd07146  272 svADEFVDLLVEKSAALVV--GDpmDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVL 342
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 251 SNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNvpiPVP---LPM 327
Cdd:cd07146  343 DHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSEL 419
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 515870067 328 FSFTGSRSSFRGdtnfyGKQGIQ----FYTQLKTIT 359
Cdd:cd07146  420 SPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
3-358 6.63e-62

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: 205.53  E-value: 6.63e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07112  107 GEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLN 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSR-HGKRVQANMGAKNHGVVMPDA-NKENTLNQLVGAAFGAA 159
Cdd:cd07112  186 VVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQ 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 160 GQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIK 235
Cdd:cd07112  266 GEVCSAGSR-LLVHEsiKDEFLEKVVAAAREWKP--GDplDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVL 342
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 236 VKGyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQV 315
Cdd:cd07112  343 TET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTV 420
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 515870067 316 GVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07112  421 WVNcfdeGDITTP-----FGGFKQSGNGRDK--SLHALDKYTELKTT 460
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
16-318 8.15e-62

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 206.71  E-value: 8.15e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFI 94
Cdd:PRK03137 167 YFYI-PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  95 CDHPDIKAISFVGSNKAGEYIFER------GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALST 168
Cdd:PRK03137 246 VDHPKTRFITFTGSREVGLRIYERaakvqpGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSR 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 169 AVLVGEA-KKWLPELVEHAKNLRVNAGDQPgADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKGYengnFVGP 247
Cdd:PRK03137 326 AIVHEDVyDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQP 399
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515870067 248 TIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN 470
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
19-318 6.63e-61

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: 202.30  E-value: 6.63e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPamipLW-MF----PMAMVcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNF 93
Cdd:cd07100   94 YEPLGVVLGIMPWNFP----FWqVFrfaaPNLMA-GNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEA 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  94 ICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVG 173
Cdd:cd07100  169 IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA-AKRFIVH 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 174 E--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTI 249
Cdd:cd07100  248 EdvYDEFLEKFVEAMAALKV--GDpmDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGA----FYPPTV 321
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870067 250 ISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07100  322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
2-362 7.72e-61

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: 202.52  E-value: 7.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   2 MGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDGT 80
Cdd:cd07152   92 QGEILPSAPGRLS-LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGV 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07152  171 LHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQG 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkg 238
Cdd:cd07152  251 QICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY----- 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 yeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07152  325 --DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIN 402
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 515870067 319 VPIPVPLPMFSFTGSRSSFRGdTNFYGKQGIQFYTQlktitSQW 362
Cdd:cd07152  403 DQTVNDEPHNPFGGMGASGNG-SRFGGPANWEEFTQ-----WQW 440
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
1-361 1.42e-60

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: 202.15  E-value: 1.42e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP--GATmLLAKLLQDSGAPD 78
Cdd:cd07151  110 MEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitGGL-LLAKIFEEAGLPK 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  79 GTLNIIHGqheAVNFICD----HPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGA 154
Cdd:cd07151  189 GVLNVVVG---AGSEIGDafveHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFG 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 155 AFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGASILLD 230
Cdd:cd07151  266 KFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPY--GDPsdPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVG 342
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 231 GRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLV 310
Cdd:cd07151  343 GEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRI 415
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515870067 311 DVGQVGVNvPIPV-PLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITSQ 361
Cdd:cd07151  416 DAGMTHIN-DQPVnDEPHVPFGGEKNS--GLGRFNGEWALEEFTTDKWISVQ 464
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
3-359 7.29e-60

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: 199.97  E-value: 7.29e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPD 78
Cdd:cd07094  101 GEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  79 GTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSrhGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFG 157
Cdd:cd07094  181 GVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFY 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 158 AAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikv 236
Cdd:cd07094  259 HAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGER--- 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 237 kgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVG 316
Cdd:cd07094  336 ----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVM 411
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 515870067 317 VNVPIPVPLPMFSFTGSRSSfrgdtnFYGKQGIQF----YTQLKTIT 359
Cdd:cd07094  412 VNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
3-359 9.54e-59

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: 197.20  E-value: 9.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLN 82
Cdd:cd07108  100 GETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLN 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLV-GAAFGAAG 160
Cdd:cd07108  178 VITGYgEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIaGMRFTRQG 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRKIK 235
Cdd:cd07108  258 QSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKI--GDplDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPLPG 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 236 VKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQV 315
Cdd:cd07108  335 EGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWV 414
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 515870067 316 GVNVPIpVPLPMFSFTGSRSSFRGDTnfYGKQG-IQFYTQLKTIT 359
Cdd:cd07108  415 QVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
1-318 1.83e-58

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: 196.44  E-value: 1.83e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGT 80
Cdd:cd07107   97 LKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGV 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLV-GAAFGA 158
Cdd:cd07107  175 FNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVaGMNFTW 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 159 AGQRCMALSTAvLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKV 236
Cdd:cd07107  255 CGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEG 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 237 KGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVG 316
Cdd:cd07107  334 PALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVW 413

                 ..
gi 515870067 317 VN 318
Cdd:cd07107  414 IN 415
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
3-356 1.85e-58

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 197.61  E-value: 1.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PLN02278 142 GDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  82 NIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PLN02278 221 NVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSG 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG 238
Cdd:PLN02278 301 QTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGG 379
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 yengNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:PLN02278 380 ----TFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVN 455
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 515870067 319 VPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:PLN02278 456 EGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIK 490
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
16-358 3.92e-57

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 193.94  E-value: 3.92e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFIC 95
Cdd:PRK13252 137 YTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLT 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  96 DHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA 175
Cdd:PRK13252 217 EHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKS 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 176 KK--WLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIIS 251
Cdd:PRK13252 296 IKaaFEARLLERVERIRI--GDpmDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFT 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 252 NVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfs 329
Cdd:PRK13252 374 DCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP--- 450
                        330       340
                 ....*....|....*....|....*....
gi 515870067 330 FTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:PRK13252 451 VGGYKQSGIGREN--GIATLEHYTQIKSV 477
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
3-363 6.26e-56

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 188.79  E-value: 6.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PRK10090  53 GEIIQSDRPGENILLFKRALGVTTGILPWNFPFfLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVF 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  82 NIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PRK10090 132 NLVLGRGETVgQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSG 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRC-MALSTAVLVGEAKKWLPELVEHAKNLRV-NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG 238
Cdd:PRK10090 212 QVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFgNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKG 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 YengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:PRK10090 292 Y----YYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515870067 319 vpipvplpmfsftgsRSSFRGDTNFY------------GKQGIQFYTQLKTITSQWK 363
Cdd:PRK10090 368 ---------------RENFEAMQGFHagwrksgiggadGKHGLHEYLQTQVVYLQSD 409
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
3-358 7.40e-56

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: 190.01  E-value: 7.40e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07142  124 GMTLPA---DGPHHVYTLhePIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGV 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAVNF-ICDHPDIKAISFVGSNKAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07142  201 LNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFN 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 159 AGQRCMAlSTAVLVGEakKWLPELVEHAKN--LRVNAGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKI 234
Cdd:cd07142  281 QGQCCCA-GSRTFVHE--SIYDEFVEKAKAraLKRVVGDpfRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRI 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 235 KVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQ 314
Cdd:cd07142  358 GSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGT 433
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 515870067 315 VGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07142  434 VWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQVKAV 474
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
18-359 1.07e-55

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: 188.97  E-value: 1.07e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  18 YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDH 97
Cdd:cd07099  116 EYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PdIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA-- 175
Cdd:cd07099  196 G-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVER-VYVHESvy 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 176 KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGyengNFVGPTIISNVKP 255
Cdd:cd07099  274 DEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGG----PFYEPTVLTDVPH 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 256 NMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN-VPIPVPLPMFSFTGSR 334
Cdd:cd07099  350 DMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVK 429
                        330       340
                 ....*....|....*....|....*
gi 515870067 335 SSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07099  430 DS--GGGRRHGAEGLREFCRPKAIA 452
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
19-345 8.95e-55

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: 186.68  E-value: 8.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHP 98
Cdd:cd07147  121 RFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  99 DIKAISFVGSNKAGEYIFERGSRhgKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--K 176
Cdd:cd07147  201 RIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyD 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 177 KWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVK 254
Cdd:cd07147  278 EFKSRLVARVKALKT--GDpkDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVP 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 255 PNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN-VPipvplpmfsftgs 333
Cdd:cd07147  349 PDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVP------------- 415
                        330
                 ....*....|..
gi 515870067 334 rsSFRGDTNFYG 345
Cdd:cd07147  416 --TFRVDHMPYG 425
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
12-358 1.25e-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: 187.17  E-value: 1.25e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  12 DMDLYSYRL--PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-H 88
Cdd:cd07559  125 DEDTLSYHFhePLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgS 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  89 EAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKE--NTLNQLVGAAFGAA---GQRC 163
Cdd:cd07559  204 EAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDAddDFDDKAEEGQLGFAfnqGEVC 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 164 MALSTAvLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYEN 241
Cdd:cd07559  284 TCPSRA-LVQESiyDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDK 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 242 GNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV-- 319
Cdd:cd07559  363 GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCyh 442
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 515870067 320 PIPVPLPmfsFTGSRSSFRGDTNFygKQGIQFYTQLKTI 358
Cdd:cd07559  443 QYPAHAP---FGGYKKSGIGRETH--KMMLDHYQQTKNI 476
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
21-318 1.49e-54

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: 186.83  E-value: 1.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDI 100
Cdd:cd07111  147 PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGV 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 101 KAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKW 178
Cdd:cd07111  227 DKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR-LLVQEsvAEEL 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 179 LPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMT 258
Cdd:cd07111  306 IRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASR 381
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 259 CYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07111  382 IAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
3-358 2.45e-54

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 186.64  E-value: 2.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:PRK09847 140 GEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLN 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIF-ERGSRHGKRVQANMGAKNHGVVMPDANKentLNQLVGAA----F 156
Cdd:PRK09847 219 VVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCPD---LQQAASATaagiF 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 157 GAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKI 234
Cdd:PRK09847 296 YNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNA 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 235 KVKGYengnfVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQ 314
Cdd:PRK09847 374 GLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGS 448
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 515870067 315 VGVNV----PIPVPlpmfsFTGSRSSFRG-DTNFYgkqGIQFYTQLKTI 358
Cdd:PRK09847 449 VFVNNyndgDMTVP-----FGGYKQSGNGrDKSLH---ALEKFTELKTI 489
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
19-322 2.52e-53

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 183.57  E-value: 2.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAV-NFICDH 97
Cdd:PRK13473 136 RDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGH 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA-- 175
Cdd:PRK13473 215 PKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiy 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 176 KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG-ASILLDGRKIKVKGYengnFVGPTIISNVK 254
Cdd:PRK13473 294 DDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGAR 369
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515870067 255 PNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 322
Cdd:PRK13473 370 QDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
19-358 5.97e-53

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: 182.65  E-value: 5.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDH 97
Cdd:cd07117  134 REPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNH 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA-- 175
Cdd:cd07117  213 PGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVQEGiy 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 176 KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKP 255
Cdd:cd07117  292 DEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTN 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 256 NMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGS 333
Cdd:cd07117  372 DMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGY 448
                        330       340
                 ....*....|....*....|....*
gi 515870067 334 RSSFRGDTNFygKQGIQFYTQLKTI 358
Cdd:cd07117  449 KKSGIGRETH--KSMLDAYTQMKNI 471
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
21-363 4.56e-52

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 181.54  E-value: 4.56e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPD 99
Cdd:PLN02466 195 PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMD 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 100 IKAISFVGSNKAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAvLVGEakKW 178
Cdd:PLN02466 275 VDKLAFTGSTDTGKIVLELAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT-FVHE--RV 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 179 LPELVEHAKN--LRVNAGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVK 254
Cdd:PLN02466 352 YDEFVEKAKAraLKRVVGDpfKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQ 427
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 255 PNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN------VPIPvplpmf 328
Cdd:PLN02466 428 DDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP------ 501
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 515870067 329 sFTGSRSSFRGDTNfyGKQGIQFYTQLKTITSQWK 363
Cdd:PLN02466 502 -FGGYKMSGIGREK--GIYSLNNYLQVKAVVTPLK 533
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
3-318 2.50e-50

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 176.16  E-value: 2.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMpSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:PLN02766 141 GETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVIN 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  83 IIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PLN02766 220 VVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNlKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKG 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG 238
Cdd:PLN02766 300 EICVA-SSRVYVQEGiyDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKG 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 YengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:PLN02766 379 Y----YIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
19-358 4.75e-50

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: 174.36  E-value: 4.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHP 98
Cdd:cd07102  114 REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  99 DIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--K 176
Cdd:cd07102  194 RIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIER-IYVHESiyD 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 177 KWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVkGYENGNFVGPTIISNVKPN 256
Cdd:cd07102  273 AFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPE-DKAGGAYLAPTVLTNVDHS 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 257 MTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNvPIPVPLPMFSFTGSRSS 336
Cdd:cd07102  352 MRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDS 430
                        330       340
                 ....*....|....*....|..
gi 515870067 337 FRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07102  431 GRGVT--LSRLGYDQLTRPKSY 450
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
3-320 5.15e-50

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: 174.70  E-value: 5.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGAPD 78
Cdd:cd07130  114 GLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPltaiAVTKIVARVLEKNGLPG 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  79 GTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFER-GSRHGkRVQANMGAKNHGVVMPDANKENTLNQLVGAAFG 157
Cdd:cd07130  194 AIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAvAARFG-RSLLELGGNNAIIVMEDADLDLAVRAVLFAAVG 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 158 AAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRK 233
Cdd:cd07130  273 TAGQRCTTTRR-LIVHEsiYDEVLERLKKAYKQVRI--GDplDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKV 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 234 IKvkgyENGNFVGPTIISnVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKY--AHLVD 311
Cdd:cd07130  350 ID----GPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSD 424

                 ....*....
gi 515870067 312 VGQVGVNVP 320
Cdd:cd07130  425 CGIVNVNIG 433
PLN02467 PLN02467
betaine aldehyde dehydrogenase
19-322 8.73e-50

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 174.54  E-value: 8.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDH 97
Cdd:PLN02467 149 KEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASH 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--A 175
Cdd:PLN02467 229 PGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriA 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 176 KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkIKVKGYENGNFVGPTIISNVKP 255
Cdd:PLN02467 308 SEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG--KRPEHLKKGFFIEPTIITDVTT 385
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515870067 256 NMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 322
Cdd:PLN02467 386 SMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQP 452
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
19-359 8.83e-50

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: 173.68  E-value: 8.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQD-SGAPDGTLNIIHGQ-HEAVNFICD 96
Cdd:cd07120  115 REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEiPSLPAGVVNLFTESgSEGAAHLVA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  97 HPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE-- 174
Cdd:cd07120  195 SPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSR-VLVQRsi 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 175 AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIkVKGYENGNFVGPTIISNVK 254
Cdd:cd07120  274 ADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDD 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 255 PNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVpLPMFSFTGSR 334
Cdd:cd07120  353 PDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYR 431
                        330       340
                 ....*....|....*....|....*
gi 515870067 335 SSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07120  432 QSGLGRLH--GVAALEDFIEYKHIY 454
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
17-322 1.34e-48

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: 169.76  E-value: 1.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  17 SYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICD 96
Cdd:cd07095   94 RHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRETGEALAA 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  97 HPDIKAISFVGSNKAGEYIFER-GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVG-- 173
Cdd:cd07095  173 HEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDga 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 174 EAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKvkgyENGNFVGPTIIsNV 253
Cdd:cd07095  253 VGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV----AGTAFLSPGII-DV 327
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870067 254 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 322
Cdd:cd07095  328 TDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT 396
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
21-318 1.62e-46

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: 165.17  E-value: 1.62e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFP------AMIPlwmfpmAMVCGNTFLMKPSERVPGATM----LLAKLLQDSGAPDGTLNIIHGQHEA 90
Cdd:cd07098  120 PLGVVGAIVSWNYPfhnllgPIIA------ALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPET 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  91 VNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaV 170
Cdd:cd07098  194 AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-V 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 171 LVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPT 248
Cdd:cd07098  273 IVHEKiyDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPT 352
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 249 IISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07098  353 LLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
5-360 2.42e-46

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: 164.40  E-value: 2.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   5 TMPSITKDMDLYSyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII 84
Cdd:cd07101  105 AIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVV 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  85 HGQHEAV-NFICDHPDIkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC 163
Cdd:cd07101  182 TGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLC 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 164 MALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG--- 238
Cdd:cd07101  260 VSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGpyf 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 YEngnfvgPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07101  339 YE------PTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVN 412
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 515870067 319 VPI-----PVPLPMFSFTGSRSSFRgdtnfYGKQGIQFYTQLKTITS 360
Cdd:cd07101  413 EGYaaawaSIDAPMGGMKDSGLGRR-----HGAEGLLKYTETQTVAV 454
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
18-361 1.78e-44

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 160.81  E-value: 1.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  18 YRLPLGVCAGIAPFNFPA------MIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV 91
Cdd:PRK09407 151 LRQPKGVVGVISPWNYPLtlavsdAIP------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVV 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  92 -NFICDHPDIkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAV 170
Cdd:PRK09407 225 gTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIY 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 171 LVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG---YEngnfvg 246
Cdd:PRK09407 303 VHESiYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGplfYE------ 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 247 PTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIpvpLP 326
Cdd:PRK09407 377 PTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGY---AA 453
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 515870067 327 MFSFTGSRSSFRGDTNF---YGKQGIQFYTQLKTITSQ 361
Cdd:PRK09407 454 AWGSVDAPMGGMKDSGLgrrHGAEGLLKYTESQTIATQ 491
aldehy_Rv0768 TIGR04284
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ...
19-318 2.28e-42

aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275104  Cd Length: 480  Bit Score: 154.15  E-value: 2.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLL-QDSGAPDGTLNII-HGQHEAVNFICD 96
Cdd:TIGR04284 139 REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVtSSDHRLGALLAK 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   97 HPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQlvgAAFGA---AGQRCmALSTAVLVG 173
Cdd:TIGR04284 219 DPRVDMVSFTGSTATGRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSM---AAFTVcmhAGQGC-AITTRLVVP 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  174 EAKkwLPELVEHAK----NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTI 249
Cdd:TIGR04284 295 RAR--YDEAVAAAAatmgSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGR--PADRDRGFFVEPTV 370
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870067  250 ISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:TIGR04284 371 IAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
1-321 3.94e-42

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: 154.28  E-value: 3.94e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07125  148 FSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDV 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFE-RGSRHGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAF 156
Cdd:cd07125  227 LQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRaLAERDGPILPliAETGGKNAMIVDSTALPEQAVKDVVQSAF 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 157 GAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgrKIK 235
Cdd:cd07125  307 GSAGQRCSALRLLYLQEEiAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLI-----APA 381
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 236 VKGYENGNFVGPTIISNVKPNmtCYKEEIFGPVLVVL--ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVG 313
Cdd:cd07125  382 PLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG 459

                 ....*...
gi 515870067 314 QVGVNVPI 321
Cdd:cd07125  460 NLYINRNI 467
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
4-318 4.23e-41

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: 151.19  E-value: 4.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   4 ETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNI 83
Cdd:cd07083  138 VEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQF 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  84 IHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHG------KRVQANMGAKNHGVVMPDANKENTLNQLVGAAF 156
Cdd:cd07083  217 LPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAF 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 157 GAAGQRCMALSTAVLV-GEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIK 235
Cdd:cd07083  297 GFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 236 VKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVL--ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVG 313
Cdd:cd07083  376 GEGY----FVAPTVVEEVPPKARIAQEEIFGPVLSVIryKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVG 451

                 ....*
gi 515870067 314 QVGVN 318
Cdd:cd07083  452 NLYIN 456
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
21-358 1.95e-40

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 148.73  E-value: 1.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPamipLWMF-----PmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDG---TLNIIHGQHEAvn 92
Cdd:PRK09406 123 PLGVVLAVMPWNFP----LWQVvrfaaP-ALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGcfqTLLVGSGAVEA-- 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  93 fICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL- 171
Cdd:PRK09406 196 -ILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVh 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 172 --VGEAkkWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTI 249
Cdd:PRK09406 275 adVYDA--FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGW----FYPPTV 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 250 ISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNvPIPVPLPMFS 329
Cdd:PRK09406 349 ITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELP 427
                        330       340       350
                 ....*....|....*....|....*....|...
gi 515870067 330 FTGSRSSfrGdtnfYGKQ----GIQFYTQLKTI 358
Cdd:PRK09406 428 FGGVKRS--G----YGRElsahGIREFCNIKTV 454
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
16-362 2.03e-39

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: 146.49  E-value: 2.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFI 94
Cdd:cd07140  142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRL 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  95 CDHPDIKAISFVGSNKAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVG 173
Cdd:cd07140  222 SDHPDVRKLGFTGSTPIGKHIMKSCAVSNlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVE 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 174 EA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIIS 251
Cdd:cd07140  301 ESihDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFT 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 252 NVKPNMTCYKEEIFGPVLVV--LETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPM 327
Cdd:cd07140  377 DVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAPF 456
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 515870067 328 FSFtgSRSSFRGDtnfYGKQGIQFYTQLKTITSQW 362
Cdd:cd07140  457 GGF--KQSGFGKD---LGEEALNEYLKTKTVTIEY 486
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
2-318 2.11e-39

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 145.77  E-value: 2.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   2 MGETMPSITKDMD-LYSYRlPLGVCAGIAPFNFPamipLWMF-----PMaMVCGNTFLMKPSERVPGATMLLAKLLQDSG 75
Cdd:PRK13968 107 MLKAEPTLVENQQaVIEYR-PLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKHAPNVMGCAQLIAQVFKDAG 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  76 APDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAA 155
Cdd:PRK13968 181 IPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGR 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 156 FGAAGQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKI 234
Cdd:PRK13968 261 YQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKI 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 235 KVKGyengNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQ 314
Cdd:PRK13968 341 AGAG----NYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGG 416

                 ....
gi 515870067 315 VGVN 318
Cdd:PRK13968 417 VFIN 420
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
3-356 1.45e-38

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 143.89  E-value: 1.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PRK11241 128 GDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVF 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  82 NIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PRK11241 207 NVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAG 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCM-ALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVkgy 239
Cdd:PRK11241 287 QTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL--- 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 240 eNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV 319
Cdd:PRK11241 364 -GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINT 442
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 515870067 320 PIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:PRK11241 443 GI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
21-320 1.49e-38

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 144.21  E-value: 1.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICD 96
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAK 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  97 HPDIKAISFVGSNKAGEYIFER-GSRHGKRVqANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA 175
Cdd:PLN02315 234 DTRIPLVSFTGSSKVGLMVQQTvNARFGKCL-LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRR-LLLHES 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 176 --KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKvkgyENGNFVGPTIISnV 253
Cdd:PLN02315 312 iyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIVE-I 386
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870067 254 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKY--AHLVDVGQVGVNVP 320
Cdd:PLN02315 387 SPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIP 455
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
16-318 3.74e-37

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: 139.89  E-value: 3.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHG-QHEAVNFI 94
Cdd:cd07116  131 YHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPL 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  95 CDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPD-ANKENTL--NQLVGAAFGA--AGQRCMALSTA 169
Cdd:cd07116  210 ASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADvMDADDAFfdKALEGFVMFAlnQGEVCTCPSRA 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 170 vLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGP 247
Cdd:cd07116  290 -LIQESiyDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVP 368
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515870067 248 TIISNVKpNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07116  369 TTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
21-318 3.40e-36

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: 136.50  E-value: 3.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGtLNIIHGQHEAVNFICDHP 98
Cdd:cd07087  100 PLGVVLIIGPWNYPLQ--LALAPLigAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEA-VAVVEGGVEVATALLAEP 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  99 -DIkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKK 177
Cdd:cd07087  177 fDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY-VLVHESIK 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 178 wlPELVEHAKNlRVNA--GDQPG--ADLGPLITPQAKERVCNLIDSGTkegasILLDGRKIKVKGYengnfVGPTIISNV 253
Cdd:cd07087  254 --DELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASLLDDGK-----VVIGGQVDKEERY-----IAPTILDDV 320
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 254 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07087  321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQERVLAETSSGGVCVN 385
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
21-318 1.37e-35

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 135.93  E-value: 1.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLqDSGAPDGTLNIIHGQHEAVNFICDHP-D 99
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEVTTELLKEPfD 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 100 IkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KK 177
Cdd:PTZ00381 188 H--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY-VLVHRSikDK 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 178 WLPELVEHAKNLrvnAGDQP--GADLGPLITPQAKERVCNLIDSgtkegasillDGRKIKVKGY--ENGNFVGPTIISNV 253
Cdd:PTZ00381 265 FIEALKEAIKEF---FGEDPkkSEDYSRIVNEFHTKRLAELIKD----------HGGKVVYGGEvdIENKYVAPTIIVNP 331
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515870067 254 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
21-290 4.58e-34

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 131.62  E-value: 4.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDI 100
Cdd:PRK09457 134 PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDI 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 101 KAISFVGSNKAGeYIFER--GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKK- 177
Cdd:PRK09457 214 DGLLFTGSANTG-YLLHRqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQGAQg 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 178 --WLPELVEHAKNLRVNAGD-QPGADLGPLITPQAKERVC----NLIDSgtkeGASILLDGRKIKvkgyENGNFVGPTII 250
Cdd:PRK09457 292 daFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQGLVaaqaQLLAL----GGKSLLEMTQLQ----AGTGLLTPGII 363
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 515870067 251 snvkpNMTCYK----EEIFGPVLVVLETETLDEAIQIVNNNPYG 290
Cdd:PRK09457 364 -----DVTGVAelpdEEYFGPLLQVVRYDDFDEAIRLANNTRFG 402
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
21-318 7.08e-34

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: 130.04  E-value: 7.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHEAVNFICDHP 98
Cdd:cd07134  100 PKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDED-EVAVFEGDAEVAQALLELP 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  99 dIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKKw 178
Cdd:cd07134  177 -FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY-VFVHESVK- 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 179 lPELVEH-----AKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkikvKGYENGNFVGPTIISNV 253
Cdd:cd07134  254 -DAFVEHlkaeiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-----QFDAAQRYIAPTVLTNV 327
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515870067 254 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:cd07134  328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
18-296 2.15e-32

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: 127.32  E-value: 2.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  18 YRlPL-GVCAGIAPFNFPAM------IPLWMfpmamvcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEA 90
Cdd:cd07123  167 YR-PLeGFVYAVSPFNFTAIggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPV 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  91 V-NFICDHPDIKAISFVGSNKAGEYIFER-GSRHGK-----RVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC 163
Cdd:cd07123  239 VgDTVLASPHLAGLHFTGSTPTFKSLWKQiGENLDRyrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKC 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 164 MALSTA-VLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRKIKVKGYen 241
Cdd:cd07123  319 SAASRAyVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY-- 396
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515870067 242 gnFVGPTIISNVKPNMTCYKEEIFGPVLVVL--ETETLDEAIQIVNN-NPYGNGTAIF 296
Cdd:cd07123  397 --FVEPTVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTtSPYALTGAIF 452
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
19-349 4.62e-31

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 123.33  E-value: 4.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDH 97
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMH 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PDIKAISFVG-------SNKAGEYifergsrhgkRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAV 170
Cdd:PLN00412 236 PGVNCISFTGgdtgiaiSKKAGMV----------PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK-VV 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 171 LVGE--AKKWLPELVEHAKNLRVNAGDQpGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPT 248
Cdd:PLN00412 305 LVMEsvADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPL 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 249 IISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPiPVPLP-M 327
Cdd:PLN00412 377 LLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdH 455
                        330       340
                 ....*....|....*....|..
gi 515870067 328 FSFTGSRSSfrgdtnFYGKQGI 349
Cdd:PLN00412 456 FPFQGLKDS------GIGSQGI 471
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
21-297 3.31e-30

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: 120.02  E-value: 3.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQdSGAPDGTLNIIHGQHEAVNFICDHPDI 100
Cdd:cd07135  108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKFD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 101 KaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKkwLP 180
Cdd:cd07135  187 K-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSV--YD 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 181 ELVEHAK---NLRVNAGDQPGADLGPLITPQAKERVCNLIDSgTKegASILLDGRKIKVKgyengNFVGPTIISNVKPNM 257
Cdd:cd07135  263 EFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT-TK--GKVVIGGEMDEAT-----RFIPPTIVSDVSWDD 334
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 515870067 258 TCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFT 297
Cdd:cd07135  335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
1-351 1.28e-29

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: 118.68  E-value: 1.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   1 MMGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKL 70
Cdd:cd07148  100 LGGREIP-----MGLtpasagriaFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCPVIVKPALATPLSCLAFVDL 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  71 LQDSGAPDGTLN-IIHGQHEAVNFICDhPDIKAISFVGSNKAGEYIFERGSRhGKRVqanmgAKNHG-----VVMPDANK 144
Cdd:cd07148  174 LHEAGLPEGWCQaVPCENAVAEKLVTD-PRVAFFSFIGSARVGWMLRSKLAP-GTRC-----ALEHGgaapvIVDRSADL 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 145 ENTLNQLVGAAFGAAGQRCMALSTA-VLVGEAKKWLPELVEHAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGT 221
Cdd:cd07148  247 DAMIPPLVKGGFYHAGQVCVSVQRVfVPAEIADDFAQRLAAAAEKLVV--GDPtdPDTEVGPLIRPREVDRVEEWVNEAV 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 222 KEGASILLDGRKIKVKGYEngnfvgPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGA 301
Cdd:cd07148  325 AAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLD 398
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 515870067 302 TARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGdtnfYGKQGIQF 351
Cdd:cd07148  399 VALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
16-305 1.14e-28

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: 116.06  E-value: 1.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  16 YSYRLPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAVNF 93
Cdd:cd07136   95 YIYYEPYGVVLIIAPWNYPFQ--LALAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  94 IC----DHpdikaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTA 169
Cdd:cd07136  172 LLdqkfDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA-PDY 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 170 VLVGEAKK--WLPELVEHAKNLRvnaGDQP--GADLGPLITPQAKERVCNLIDSGTkegasILLDGrkikvKGYENGNFV 245
Cdd:cd07136  246 VLVHESVKekFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNGK-----IVFGG-----NTDRETLYI 312
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515870067 246 GPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNGATARK 305
Cdd:cd07136  313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKK 372
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
21-318 3.99e-28

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: 115.01  E-value: 3.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVN-FICDHPD 99
Cdd:TIGR01238 160 SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPR 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  100 IKAISFVGSNKAGEYI----FERGSRHGKRVqANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEA 175
Cdd:TIGR01238 240 IAGVAFTGSTEVAQLInqtlAQREDAPVPLI-AETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  176 KKWLPELVEHA-KNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKgYENGNFVGPTIISnvK 254
Cdd:TIGR01238 319 ADRVLTMIQGAmQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRA-CQHGTFVAPTLFE--L 395
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515870067  255 PNMTCYKEEIFGPVL--VVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:TIGR01238 396 DDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
21-358 2.09e-26

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: 109.42  E-value: 2.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHEAVNFICDH 97
Cdd:cd07137  101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPeylDTKA----IKVIEGGVPETTALLEQ 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PDIKaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTaVLVGEak 176
Cdd:cd07137  177 KWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY-VLVEE-- 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 177 KWLPELVEHAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSgTKEGASILLDGRKIkvkgyENGNFVGPTIISNV 253
Cdd:cd07137  253 SFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERD-----EKNLYIEPTILLDP 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 254 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN-VPIPVPLPMFSFTG 332
Cdd:cd07137  327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDTLPFGG 406
                        330       340
                 ....*....|....*....|....*.
gi 515870067 333 SRSSfrGDTNFYGKQGIQFYTQLKTI 358
Cdd:cd07137  407 VGES--GFGAYHGKFSFDAFSHKKAV 430
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
7-280 3.13e-26

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: 109.25  E-value: 3.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   7 PSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIH 85
Cdd:cd07084   86 LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLIN 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  86 GQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGsrHGKRVQANMGAKNHGVVMPDAN-KENTLNQLVGAAFGAAGQRCM 164
Cdd:cd07084  166 GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCT 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 165 ALStAVLVGEAKKWLPeLVEHAKNLRVNAGDQpGADLGPLITPQAKERvcnlIDSGTKEGASILLDGRKIkVKGYENGNF 244
Cdd:cd07084  244 AQS-MLFVPENWSKTP-LVEKLKALLARRKLE-DLLLGPVQTFTTLAM----IAHMENLLGSVLLFSGKE-LKNHSIPSI 315
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 515870067 245 VGPTIISNV----KPNMTCYK---EEIFGPVLVVLETETLDEA 280
Cdd:cd07084  316 YGACVASALfvpiDEILKTYElvtEEIFGPFAIVVEYKKDQLA 358
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
23-318 9.28e-26

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


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 109.13  E-value: 9.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   23 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIK 101
Cdd:PRK11904  686 GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIA 765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  102 AISFVGSNKAGEYIfERG--SRHGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStaVL-VGE-- 174
Cdd:PRK11904  766 GVAFTGSTETARII-NRTlaARDGPIVPliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR--VLfVQEdi 842
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  175 AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEG---ASILLDGrkikvkGYENGNFVGPTI 249
Cdd:PRK11904  843 ADRVIEMLKGAMAELKV--GDprLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPA------GTENGHFVAPTA 914
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515870067  250 ISnvKPNMTCYKEEIFGPVLVVL--ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 318
Cdd:PRK11904  915 FE--IDSISQLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
21-318 2.45e-23

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: 100.64  E-value: 2.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFP---AMIPLwmfPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHE------AV 91
Cdd:cd07133  101 PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADvaaafsSL 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  92 NFicDHpdikaISFVGSnkageyifergSRHGKRVQAN-----------MGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07133  177 PF--DH-----LLFTGS-----------TAVGRHVMRAaaenltpvtleLGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 161 QRCMAlSTAVLVGEAKkwLPELVEHAKNL------RVNAGDqpgaDLGPLITPQAKERVCNLIDSGTKEGASI------- 227
Cdd:cd07133  239 QTCVA-PDYVLVPEDK--LEEFVAAAKAAvakmypTLADNP----DYTSIINERHYARLQGLLEDARAKGARVielnpag 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 228 --LLDGRKIkvkgyengnfvGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNG 300
Cdd:cd07133  312 edFAATRKL-----------PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDK 375
                        330
                 ....*....|....*...
gi 515870067 301 ATARKYAHLVDVGQVGVN 318
Cdd:cd07133  376 AEQDRVLRRTHSGGVTIN 393
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
14-286 2.47e-22

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: 97.68  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  14 DLYSYRLPLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEA- 90
Cdd:cd07132   93 DVYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVEETt 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  91 --VNFICDHpdikaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA--- 165
Cdd:cd07132  171 elLKQRFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdy 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 166 -LSTavlvgeaKKWLPELVEHAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSGtkegasilldgrKIKVKGY-- 239
Cdd:cd07132  246 vLCT-------PEVQEKFVEALKKtLKEFYGEDPkeSPDYGRIINDRHFQRLKKLLSGG------------KVAIGGQtd 306
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 515870067 240 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNN 286
Cdd:cd07132  307 EKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINS 353
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
21-290 4.62e-21

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


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 95.43  E-value: 4.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPD 99
Cdd:PRK11809  768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADAR 847
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  100 IKAISFVGS---------NKAGeyifeRGSRHGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALST 168
Cdd:PRK11809  848 VRGVMFTGStevarllqrNLAG-----RLDPQGRPIPliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRV 922
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  169 AVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKiKVKGYENGNFVGP 247
Cdd:PRK11809  923 LCLQDDvADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARE-NSEDWQSGTFVPP 1001
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 515870067  248 TIISnvKPNMTCYKEEIFGPVLVVL--ETETLDEAIQIVNNNPYG 290
Cdd:PRK11809 1002 TLIE--LDSFDELKREVFGPVLHVVryNRNQLDELIEQINASGYG 1044
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
21-358 3.86e-20

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 91.65  E-value: 3.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHEAVNFICDHPDI 100
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 101 KaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALStavLVGEAKKWL 179
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPD---YILTTKEYA 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 180 PELVEHAK-NLRVNAGDQP--GADLGPLITPQAKERVCNLIDSgtKEGASILLDGRKikvKGYENGNfVGPTIISNVKPN 256
Cdd:PLN02174 267 PKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGE---KDRENLK-IAPTILLDVPLD 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 257 MTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN-VPIPVPLPMFSFTGSRS 335
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGE 420
                        330       340
                 ....*....|....*....|...
gi 515870067 336 SFRGdtNFYGKQGIQFYTQLKTI 358
Cdd:PLN02174 421 SGMG--AYHGKFSFDAFSHKKAV 441
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
17-290 5.69e-18

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


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 86.07  E-value: 5.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   17 SYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHEAV- 91
Cdd:PRK11905  672 PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTP----LIAaravRLLHEAGVPKDALQLLPGDGRTVg 747
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   92 NFICDHPDIKAISFVGSNKAGEYIfER--GSRHGKRVQ--ANMGAKNHGVVMPDANKEntlnQLVGA----AFGAAGQRC 163
Cdd:PRK11905  748 AALVADPRIAGVMFTGSTEVARLI-QRtlAKRSGPPVPliAETGGQNAMIVDSSALPE----QVVADviasAFDSAGQRC 822
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  164 MALStaVL-VGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgRKIKV-KGY 239
Cdd:PRK11905  823 SALR--VLcLQEdvADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLpAET 896
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 515870067  240 ENGNFVGPTIISnvKPNMTCYKEEIFGPVLVVL--ETETLDEAIQIVNNNPYG 290
Cdd:PRK11905  897 EKGTFVAPTLIE--IDSISDLEREVFGPVLHVVrfKADELDRVIDDINATGYG 947
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
21-318 6.85e-17

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


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 82.68  E-value: 6.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   21 PLGVCAGIAPFNFP---------AmiplwmfpmAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQ 87
Cdd:COG4230   680 GRGVFVCISPWNFPlaiftgqvaA---------ALAAGNTVLAKPAEQTP----LIAaravRLLHEAGVPADVLQLLPGD 746
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067   88 HEAV-NFICDHPDIKAISFVGSNKAGeyifergsrhgKRVQANMGAKNHGVVMPDAnkEnT--LN-----------QLVG 153
Cdd:COG4230   747 GETVgAALVADPRIAGVAFTGSTETA-----------RLINRTLAARDGPIVPLIA--E-TggQNamivdssalpeQVVD 812
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  154 ----AAFGAAGQRCMALStaVL-VGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGAS 226
Cdd:COG4230   813 dvlaSAFDSAGQRCSALR--VLcVQEdiADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRL 890
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  227 IlldgRKIKV-KGYENGNFVGPTI--ISNVKPnmtcYKEEIFGPVLVVL--ETETLDEAIQIVNNNPYGNGTAIFTTNGA 301
Cdd:COG4230   891 V----HQLPLpEECANGTFVAPTLieIDSISD----LEREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDE 962
                         330
                  ....*....|....*..
gi 515870067  302 TARKYAHLVDVGQVGVN 318
Cdd:COG4230   963 TIDRVAARARVGNVYVN 979
PLN02203 PLN02203
aldehyde dehydrogenase
21-305 3.21e-16

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 79.77  E-value: 3.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHEAVNFIC 95
Cdd:PLN02203 108 PLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANIPkylDSKA----VKVIEGGPAVGEQLL 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  96 DHPDIKaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENT---LNQLVGAAFGA-AGQRCMALSTaVL 171
Cdd:PLN02203 182 QHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTkvaVNRIVGGKWGScAGQACIAIDY-VL 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 172 VGEakKWLPELVEHAKN-LRVNAGDQPG--ADLGPLITPQAKERVCNLIDSgTKEGASIL----LDGRKIkvkgyengnF 244
Cdd:PLN02203 260 VEE--RFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD-PRVAASIVhggsIDEKKL---------F 327
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515870067 245 VGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARK 305
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRR 388
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
18-284 1.23e-12

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: 69.06  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  18 YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDH 97
Cdd:cd07126  139 YRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PDIKAISFVGSNKageyIFERGSR--HGKrVQANMGAKNHGVVMPDANKENTLN-QLVGAAFGAAGQRCMALStavLVGE 174
Cdd:cd07126  219 ANPRMTLFTGSSK----VAERLALelHGK-VKLEDAGFDWKILGPDVSDVDYVAwQCDQDAYACSGQKCSAQS---ILFA 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 175 AKKWLPE-LVEHAKNLrvnAGDQPGADL--GPLITpQAKERVCNLIDSGTK-EGASILLDGRKIK------VKG-YENGN 243
Cdd:cd07126  291 HENWVQAgILDKLKAL---AEQRKLEDLtiGPVLT-WTTERILDHVDKLLAiPGAKVLFGGKPLTnhsipsIYGaYEPTA 366
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 515870067 244 FVGPTIISNVKPNMTCYKEEIFGPVLVVleTETLDEAIQIV 284
Cdd:cd07126  367 VFVPLEEIAIEENFELVTTEVFGPFQVV--TEYKDEQLPLV 405
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
13-312 3.06e-12

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: 67.57  E-value: 3.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  13 MDLYSYRLPLGVCAGIAPFNFP-AmiplwmFPM-------AMVCGNTFLMKPSERVPGATMLLAKL----LQDSGAPDGT 80
Cdd:cd07129   97 PDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGV 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  81 LNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSR--HGKRVQANMGAKNHGVVMPDANKEN--TLNQ-LVGA 154
Cdd:cd07129  171 FSLLQGgGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGALAERgeAIAQgFVGS 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 155 AFGAAGQRCmaLSTAVLVGEAKKWLPELVEHAKNLrvnAGDQPGadlGPLITPqakeRVCNLIDSGTKE-----GASILL 229
Cdd:cd07129  251 LTLGAGQFC--TNPGLVLVPAGPAGDAFIAALAEA---LAAAPA---QTMLTP----GIAEAYRQGVEAlaaapGVRVLA 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 230 DGRkikvkGYENGNFVGPTI--------ISNVKpnmtcYKEEIFGPVLVVLETETLDEAIQIVNNNPyGNGTA-IFTTNG 300
Cdd:cd07129  319 GGA-----AAEGGNQAAPTLfkvdaaafLADPA-----LQEEVFGPASLVVRYDDAAELLAVAEALE-GQLTAtIHGEED 387
                        330
                 ....*....|..
gi 515870067 301 ATArKYAHLVDV 312
Cdd:cd07129  388 DLA-LARELLPV 398
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
23-307 7.41e-09

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: 57.28  E-value: 7.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  23 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQheaVNFICDHPDIK 101
Cdd:cd07128  146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQ 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 102 -AISFVGSNKAGEYIfeRGS----RHGKRVQANMGAKNHGVVMPDAnKENT------LNQLVGAAFGAAGQRCMALSTAv 170
Cdd:cd07128  223 dVVAFTGSAATAAKL--RAHpnivARSIRFNAEADSLNAAILGPDA-TPGTpefdlfVKEVAREMTVKAGQKCTAIRRA- 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 171 LVGEAKkwLPELVE--HAKNLRVNAGD--QPGADLGPLITPQAKERVCNLIDSgTKEGASILL---DGRKIKVKGYENGN 243
Cdd:cd07128  299 FVPEAR--VDAVIEalKARLAKVVVGDprLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFggpDRFEVVGADAEKGA 375
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870067 244 FVGPTII--SNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNnpyGNG---TAIFTTNGATARKYA 307
Cdd:cd07128  376 FFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFARELV 441
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
23-284 1.61e-05

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 46.62  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  23 GVCAGIAPFNFPAMiPLW-MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQHEAvnfICDH--- 97
Cdd:PRK11903 150 GVALFINAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAG---LLDHlqp 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  98 PDIkaISFVGSNKAGEYIFERGS--RHGKRVQANMGAKNHGVVMPDANKEntlnqlvGAAFGA------------AGQRC 163
Cdd:PRK11903 226 FDV--VSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPG-------SEAFDLfvkevvremtvkSGQKC 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067 164 MALSTaVLVGEAkkwLPELVEHAKNLR---VNAGD--QPGADLGPLITPQAKERVCNLIDsGTKEGASILLDGRKIKVKG 238
Cdd:PRK11903 297 TAIRR-IFVPEA---LYDAVAEALAARlakTTVGNprNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVD 371
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 515870067 239 YEN--GNFVGPTIISNVKPN--MTCYKEEIFGPVLVVLETETLDEAIQIV 284
Cdd:PRK11903 372 ADPavAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYRDAAHALALA 421
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
21-184 4.47e-04

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: 41.82  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFpMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII----HGQHEAVNFICD 96
Cdd:cd07077  100 PIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVlyvpHPSDELAEELLS 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  97 HPDIKAISFVGSNKAGEYIfeRGSRHGKRVQAnMGAKNHGVVMPDANKENTLNQLV--GAAF-GAAgqrCMALSTAVLVG 173
Cdd:cd07077  179 HPKIDLIVATGGRDAVDAA--VKHSPHIPVIG-FGAGNSPVVVDETADEERASGSVhdSKFFdQNA---CASEQNLYVVD 252
                        170
                 ....*....|.
gi 515870067 174 EAKKWLPELVE 184
Cdd:cd07077  253 DVLDPLYEEFK 263
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
21-139 5.41e-04

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: 41.87  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870067  21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQD----SGAPDGTLNIIHGQH-EAVNFIC 95
Cdd:cd07081   95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQaavaAGAPENLIGWIDNPSiELAQRLM 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 515870067  96 DHPDIKAISFVGsnkaGEYIFERGSRHGKRVQAnMGAKNHGVVM 139
Cdd:cd07081  175 KFPGIGLLLATG----GPAVVKAAYSSGKPAIG-VGAGNTPVVI 213
 
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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