|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
53-527 |
0e+00 |
|
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: 973.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 53 GVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07130 1 GVYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 213 NVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGR 292
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPL 372
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 373 HTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLgHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 453 QGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 527
Cdd:cd07130 400 QGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
53-527 |
0e+00 |
|
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: 908.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 53 GVYNGSWGGRG-EVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07086 1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 132 VSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 212 GNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFG 291
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGP 371
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR--PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNN 449
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588810 450 EVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYS 527
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
36-538 |
0e+00 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 715.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 36 QPQYAWLKELGLREENEGVY-NGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIV 114
Cdd:PLN02315 5 RKEYEFLSEIGLSSRNLGCYvGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 115 RQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAF 194
Cdd:PLN02315 85 RQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 195 NFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTG 274
Cdd:PLN02315 165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 275 STQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAY 354
Cdd:PLN02315 245 SSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 355 AQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTgLGHDASIAHTETFAPILY 434
Cdd:PLN02315 325 KQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 435 VFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWK 514
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWK 483
|
490 500
....*....|....*....|....
gi 1812588810 515 QYMRRSTCTINYSKDLPLAQGIKF 538
Cdd:PLN02315 484 QYMRRSTCTINYGNELPLAQGINF 507
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-524 |
9.68e-171 |
|
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: 489.80 E-value: 9.68e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 89 EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPI 168
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 169 LPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAIC 248
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 249 SLTCGGAD-IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAG 327
Cdd:cd07078 157 NVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 328 QRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR-PG 406
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 407 NYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIP 486
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVA--ERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 1812588810 487 TSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
61-521 |
3.97e-169 |
|
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: 486.65 E-value: 3.97e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 61 GRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 141 VEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIeQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGA 220
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYT-RREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 221 PTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGG 299
Cdd:pfam00171 163 ELTPLTALL----LAELFEEAGLPaGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVS 379
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 380 MFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 459
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812588810 460 FTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRST 521
Cdd:pfam00171 399 FTSDLERALRVA--RRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
56-526 |
9.93e-167 |
|
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: 481.16 E-value: 9.93e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:COG1012 11 GGEWvaAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:COG1012 91 LETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 214 VCLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGR 292
Cdd:COG1012 171 TVVLKPAEQTPLSALL----LAELLEEAGLPaGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPL 372
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 373 HTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR-PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 451
Cdd:COG1012 327 ISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDT 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 452 KQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 526
Cdd:COG1012 407 EYGLAASVFTRDLARARRVA--RRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
56-527 |
4.51e-132 |
|
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: 392.87 E-value: 4.51e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSWGGR--GEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07131 4 GGEWVDSasGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:cd07131 84 TREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 213 NVCLWKGAPTTSlisvAVTKIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFG 291
Cdd:cd07131 164 NTVVFKPAEDTP----ACALKLVELFAEAGLPpGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGP 371
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDR----PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAW 447
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 448 NNEVKQGLSSSIFTKDLGRIFRWLGpkgsDC--GIVNVNIPTSGAEIGGAFGGEKHTGGG-RESGSDAWKQYMRRSTCTI 524
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARR----DLeaGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
...
gi 1812588810 525 NYS 527
Cdd:cd07131 476 DYS 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
93-524 |
1.43e-126 |
|
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: 374.64 E-value: 1.43e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 93 KKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSE 172
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 173 RSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAICSLTC 252
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 253 GGAD-IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCT 331
Cdd:cd06534 157 GGGDeVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 332 TARRLFIHESIHDEVVNRLKkayaqirvgnpwdpnvlygplhtkqavsmflgaveeakkeggtvvyggkvmdrpgnyvep 411
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 412 TIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAE 491
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA--ERLRAGTVYINDSSIGVG 334
|
410 420 430
....*....|....*....|....*....|...
gi 1812588810 492 IGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
52-512 |
8.52e-117 |
|
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: 353.48 E-value: 8.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 52 EGVYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGS 130
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 131 LVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 211 CGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQER 289
Cdd:cd07097 162 YGNTVVFKPAELTPASAWA----LVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 290 FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLY 369
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 370 GPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP--GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAW 447
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1812588810 448 NNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDA 512
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFK--RRVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEAA 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
71-517 |
4.77e-110 |
|
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: 335.17 E-value: 4.77e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVqey 150
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 151 vdicDYAVGL-------SRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPvavygwnnaIAMI---------CGNV 214
Cdd:cd07103 81 ----DYAASFlewfaeeARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFP---------AAMItrkiapalaAGCT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 215 CLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQ--ERFG 291
Cdd:cd07103 148 VVLKPAEETPLSALA----LAELAEEAGLPaGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKL--LMAQaaDTVK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGP 371
Cdd:cd07103 222 RVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 451
Cdd:cd07103 302 LINERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812588810 452 KQGLSSSIFTKDLGRIFRwLGpKGSDCGIVNVNIPT-SGAEIggAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07103 382 PYGLAAYVFTRDLARAWR-VA-EALEAGMVGINTGLiSDAEA--PFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
63-469 |
3.09e-103 |
|
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: 318.44 E-value: 3.09e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVE 142
Cdd:cd07088 12 GETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 143 GVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPT 222
Cdd:cd07088 92 ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 223 TSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 301
Cdd:cd07088 172 TPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 381
Cdd:cd07088 248 PAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 382 LGAVEEAKKEGGTVVYGGKVMD-RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 460
Cdd:cd07088 328 EEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIY 407
|
....*....
gi 1812588810 461 TKDLGRIFR 469
Cdd:cd07088 408 TENLNTAMR 416
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
71-518 |
1.36e-102 |
|
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: 316.41 E-value: 1.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 149 EYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISV 228
Cdd:cd07114 84 YLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 229 AVTKIiakVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07114 164 ELAKL---AEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 309 ADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA 388
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 389 KKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 464
Cdd:cd07114 321 REEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1812588810 465 GRIFRWlgPKGSDCGIVNVNI-----PTSgaeiggAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07114 401 ARAHRV--ARAIEAGTVWVNTyralsPSS------PFGGFKDSGIGRENGIEAIREYTQ 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-516 |
1.40e-97 |
|
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: 302.53 E-value: 1.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 87 DYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGG 166
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 167 PILPSERSGHALIEQWNPVGLVGIITAFNFPV-----AVygwnnAIAMICGNVCLWKGAPTTslisvAVTK--IIAKVLE 239
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLilamrSV-----APALALGNAVVLKPDSRT-----PVTGglLIAEIFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 240 DNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGlmvqERFGRSL----LELGGNNAIIAFEDADLSLV 314
Cdd:cd07104 151 EAGLPkGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIG----ELAGRHLkkvaLELGGNNPLIVLDDADLDLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 315 VPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGT 394
Cdd:cd07104 227 VSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 395 VVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGpK 474
Cdd:cd07104 307 LLTGGT---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA-E 381
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1812588810 475 GSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQY 516
Cdd:cd07104 382 RLETGMVHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
71-510 |
4.64e-92 |
|
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: 288.84 E-value: 4.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07150 6 PADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 151 VDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVav 230
Cdd:cd07150 86 PELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 231 tkIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIA 305
Cdd:cd07150 164 --KIAEIMEEAGLPkGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGR----EIAEKAGRHLkkitLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 306 FEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAV 385
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 386 EEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLG 465
Cdd:cd07150 318 EDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1812588810 466 RIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGS 510
Cdd:cd07150 395 RAFKL--AERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGE 437
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
71-516 |
3.67e-91 |
|
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: 286.64 E-value: 3.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG-EVQE 149
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 150 YVDICDYAVGLSRMIGGPILPSeRSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07115 84 AADTFRYYAGWADKIEGEVIPV-RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 230 VTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07115 163 IAELMAEA----GFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 309 ADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA 388
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 389 KKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIF 468
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1812588810 469 RWlgPKGSDCGIVNVNipTSGA-EIGGAFGGEKHTGGGRESGSDAWKQY 516
Cdd:cd07115 399 RV--AAALKAGTVWIN--TYNRfDPGSPFGGYKQSGFGREMGREALDEY 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
71-521 |
5.07e-91 |
|
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: 285.96 E-value: 5.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 151 VDICDYAVGLSrmiggpiLPSER----SGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLI 226
Cdd:cd07106 84 VAWLRYTASLD-------LPDEVieddDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 227 SVAVTKIIAKVLEdnklPGAICSLTcGGADIGTAMAKDERVNLLSFTGSTQVGKQVglMVQ--ERFGRSLLELGGNNAII 304
Cdd:cd07106 157 TLKLGELAQEVLP----PGVLNVVS-GGDELGPALTSHPDIRKISFTGSTATGKKV--MASaaKTLKRVTLELGGNDAAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGA 384
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 385 VEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 464
Cdd:cd07106 310 VEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1812588810 465 GRIFRwLGPKgSDCGIVNVNiptSGAEIGGA--FGGEKHTGGGRESGSDAWKQYMRRST 521
Cdd:cd07106 390 ERAEA-VARR-LEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
57-509 |
1.20e-90 |
|
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: 285.74 E-value: 1.20e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 57 GSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:cd07151 1 GEWrdGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 135 EMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNV 214
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 215 CLWKGAPTTslisvAVTK--IIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFG 291
Cdd:cd07151 161 VVLKPASDT-----PITGglLLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGP 371
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMdrpGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 451
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGGEAE---GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588810 452 KQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESG 509
Cdd:cd07151 393 EYGLSGAVFTSDLERGVQF--ARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLGRFNG 448
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
71-518 |
8.18e-90 |
|
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: 283.06 E-value: 8.18e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGV-GEVQE 149
Cdd:cd07092 4 PATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 150 YVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07092 84 AVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 230 VTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDA 309
Cdd:cd07092 164 LAELAAEVLP----PGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 310 DLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAK 389
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 390 KeGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:cd07092 320 A-HARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1812588810 470 WLGPKGSDCGIVNVNIPTSgAEIggAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLA-AEM--PHGGFKQSGYGKDLSIYALEDYTR 444
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
54-526 |
2.48e-89 |
|
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: 283.73 E-value: 2.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 133 SLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPIL---PSERSGHALIeqwnPVGLVGIITAFNFPVAVYGWNNAIAM 209
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVemvPGEDNRYVYR----PLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 210 ICGNVCLWKGAPTTSLISVAVtkiiAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGStqvgKQVGLMVQE 288
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKL----VEILEEAGLPpGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGS----REVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 289 RFG----------RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIR 358
Cdd:cd07124 264 RAAkvqpgqkwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 359 VGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRP--GNYVEPTIVTGLGHDASIAHTETFAPILYVF 436
Cdd:cd07124 344 VGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSE-GRLLLGGEVLELAaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 437 KFKNEEEVFAWNNEVKQGLSSSIFTKDLGRI--FRwlgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTG-GGRESGSDA 512
Cdd:cd07124 423 KAKDFDEALEIANDTEYGLTGGVFSRSPEHLerAR----REFEVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDY 498
|
490
....*....|....
gi 1812588810 513 WKQYMRRSTCTINY 526
Cdd:cd07124 499 LLQFMQPKTVTENF 512
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
68-512 |
2.18e-88 |
|
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: 279.45 E-value: 2.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 68 TYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGev 147
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 148 qeyVDI----------CDYAVGLsrmiGGPILPSERsGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLW 217
Cdd:cd07093 79 ---RDIpraaanfrffADYILQL----DGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 218 KGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLE 296
Cdd:cd07093 151 KPSEWTPLTAW----LLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 297 LGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQ 376
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 377 AVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:cd07093 307 HLEKVLGYVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTP 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1812588810 453 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN------IPTsgaeiggAFGGEKHTGGGRESGSDA 512
Cdd:cd07093 387 YGLAAYVWTRDLGRAHRV--ARRLEAGTVWVNcwlvrdLRT-------PFGGVKASGIGREGGDYS 443
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
52-517 |
3.05e-87 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 278.11 E-value: 3.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 52 EGVYNGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLG 129
Cdd:PLN02278 26 QGLIGGKWtdAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 130 SLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAM 209
Cdd:PLN02278 106 QLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 210 ICGNVCLWKGAPTTSLISVAVTKIiakVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQ-- 287
Cdd:PLN02278 186 AAGCTVVVKPSELTPLTALAAAEL---ALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKK--LMAGaa 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 288 ERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNV 367
Cdd:PLN02278 261 ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 368 LYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAW 447
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812588810 448 NNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN---IPTSGAeiggAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRV--SEALEYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
71-526 |
3.24e-87 |
|
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: 276.56 E-value: 3.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 151 VDICDYAVGLSRMIGGPILP-SERSGHALIEQwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07107 84 AALLDYFAGLVTELKGETIPvGGRNLHYTLRE--PYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 230 VTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDA 309
Cdd:cd07107 162 LAELAREVLP----PGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 310 DLSLVVPSALFAA-VGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA 388
Cdd:cd07107 238 DPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 389 KKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 464
Cdd:cd07107 318 KREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812588810 465 GRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 526
Cdd:cd07107 398 SQAHR--TARRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
66-508 |
8.64e-87 |
|
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: 275.38 E-value: 8.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 146 EVQEYVDICDYAVGLSRMIGGPILPSE----RSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 222 TTSLISVAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN 300
Cdd:cd07145 161 NTPLTAIELAKILEEA----GLPpGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 301 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSM 380
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 381 FLGAVEEAKKEGGTVVYGGKVMDrpGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 460
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1812588810 461 TKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 508
Cdd:cd07145 395 TNDINRALKV--ARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREG 440
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
89-507 |
2.49e-86 |
|
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: 273.18 E-value: 2.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 89 EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICD-YAVGLSRMIGGP 167
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyYAENAEAFLADE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 168 ILPSErSGHALIeQWNPVGLVGIITAFNFP---VAVYGwnnAIAMICGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLP 244
Cdd:cd07100 82 PIETD-AGKAYV-RYEPLGVVLGIMPWNFPfwqVFRFA---APNLMAGNTVLLKHASNVPGCALA----IEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 245 -GAICSLTCGGADIGTAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAV 323
Cdd:cd07100 153 eGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 324 GTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMD 403
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 404 RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLG---RIFRWLgpkgsDCGI 480
Cdd:cd07100 312 GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLEraeRVARRL-----EAGM 386
|
410 420
....*....|....*....|....*...
gi 1812588810 481 VNVNIPT-SGAEIggAFGGEKHTGGGRE 507
Cdd:cd07100 387 VFINGMVkSDPRL--PFGGVKRSGYGRE 412
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
66-507 |
7.61e-86 |
|
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: 272.93 E-value: 7.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 146 EVQEYVDICDYAVGLSRMIGGPILPSE-------RSGHALIEqwnPVGLVGIITAFNFPVavygwnN--------AIAmi 210
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPFDaspggegRIGFTIRE---PIGVVAAITPFNFPL------NlvahkvgpAIA-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 211 CGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVglmvQER 289
Cdd:cd07149 150 AGNAVVLKPASQTPLSALK----LAELLLEAGLPkGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI----ARK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 290 FG--RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNV 367
Cdd:cd07149 222 AGlkKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 368 LYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAW 447
Cdd:cd07149 302 DVGPMISEAEAERIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAM 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812588810 448 NNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 507
Cdd:cd07149 379 ANDSPYGLQAGVFTNDLQKALKAA--RELEVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-518 |
1.62e-85 |
|
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: 272.26 E-value: 1.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 68 TYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEV 147
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 148 QEYVDICDYAVGL-SRMIGGPI-LPSERSGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSL 225
Cdd:cd07090 81 DSSADCLEYYAGLaPTLSGEHVpLPGGSFAYTRRE---PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 226 ISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIA 305
Cdd:cd07090 158 TAL----LLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 306 FEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAV 385
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 386 EEAKKEGGTVVYGGKVMD-----RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 460
Cdd:cd07090 314 ESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1812588810 461 TKDLGRIFRWLGP-KGSDCGIVNVNIptSGAEIggAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07090 394 TRDLQRAHRVIAQlQAGTCWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
69-517 |
4.23e-85 |
|
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: 271.04 E-value: 4.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 69 YCPANNEPIARVRQASVADYEETVKKAREAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILV-EGVGE 146
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 147 VQEYVDICDYAVGLSRM------IGGPILPSERSGHALIEQwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGA 220
Cdd:cd07089 82 VDGPIGHLRYFADLADSfpwefdLPVPALRGGPGRRVVRRE--PVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 221 PTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN 300
Cdd:cd07089 160 PDTPLSALLLGEIIA---ETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 301 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSM 380
Cdd:cd07089 237 SANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 381 FLGAVEEAKKEGGTVVYGGKvmdRP-----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGL 455
Cdd:cd07089 317 VEGYIARGRDEGARLVTGGG---RPagldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 456 SSSIFTKDLGR---IFRWLgpkgsDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07089 394 SGGVWSADVDRayrVARRI-----RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
56-508 |
5.93e-84 |
|
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: 268.55 E-value: 5.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07117 6 NGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 134 LEMGKILVEGVGevqeyVDIcDYAVGLSRMIGGPILPSERSGHALIEQW------NPVGLVGIITAFNFPVAVYGWNNAI 207
Cdd:cd07117 86 LDNGKPIRETRA-----VDI-PLAADHFRYFAGVIRAEEGSANMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 208 AMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDnklpGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQ 287
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPK----GVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 288 ERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNV 367
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 368 LYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEE 443
Cdd:cd07117 316 QMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812588810 444 VFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 508
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNtynqIPA-----GAPFGGYKKSGIGRET 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
56-517 |
7.76e-84 |
|
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: 268.41 E-value: 7.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAW--KIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07119 3 DGEWveAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 132 VSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVR-EPVGVCGLITPWNYPLLQAAWKLAPALAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 212 GNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF 290
Cdd:cd07119 162 GNTVVIKPSEVTPLTTIALFELIEEA----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 291 GRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYG 370
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 371 PLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812588810 447 WNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN---IPTSGAEiggaFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVA--RRLRAGTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
56-524 |
7.95e-82 |
|
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: 263.30 E-value: 7.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07091 9 NNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 132 VSLEMGKILVEG-VGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07091 89 ESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRR-EPIGVCGQIIPWNFPLLMLAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 211 CGNVCLWKGAPTTSLISVAVTKIIAKVLednkLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVglMV--- 286
Cdd:cd07091 168 AGNTVVLKPAEQTPLSALYLAELIKEAG----FPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTI--MEaaa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 287 QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPN 366
Cdd:cd07091 242 KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 367 VLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 447 WNNEVKQGLSSSIFTKDLGRIFR----------WLgpkgsDC-GIVNVNIPtsgaeiggaFGGEKHTGGGRESGSDAWKQ 515
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELGEEGLEE 467
|
....*....
gi 1812588810 516 YMRRSTCTI 524
Cdd:cd07091 468 YTQVKAVTI 476
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-518 |
1.03e-80 |
|
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: 259.46 E-value: 1.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 69 YCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 149 EYVDICDYAVGLSrmigGPILPSER-------SGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07099 81 LALEAIDWAARNA----PRVLAPRKvptgllmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 222 TTSLISVAVTKIIAKVLednkLPGAICSLTCGGADIGTAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 301
Cdd:cd07099 157 VTPLVGELLAEAWAAAG----PPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 381
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 382 LGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 461
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812588810 462 KDL---GRIFRWLgpkgsDCGIVNVNIPTSGAEIGGA-FGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07099 392 RDLaraEAIARRL-----EAGAVSINDVLLTAGIPALpFGGVKDSGGGRRHGAEGLREFCR 447
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
56-518 |
1.55e-80 |
|
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: 259.73 E-value: 1.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07142 9 NGQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 132 VSLEMGKILVEG-VGEVQEYVDICDYAVGLSRMIGGPILPSERSGHA--LIEqwnPVGLVGIITAFNFPVAVYGWNNAIA 208
Cdd:cd07142 89 ETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVytLHE---PIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 209 MICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQV-GLMV 286
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSAL----LAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIImQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 287 QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPN 366
Cdd:cd07142 242 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 367 VLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812588810 447 WNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLS--RALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
66-507 |
2.86e-80 |
|
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: 258.33 E-value: 2.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 146 EVQEYVDICDYAVGLSRMIGGPILP---SERS-GH-ALIEQWnPVGLVGIITAFNFPV--AVYGWNNAIAMicGNVCLWK 218
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldiSARGeGRqGLVRRF-PIGPVSAITPFNFPLnlVAHKVAPAIAA--GCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 219 GAPTTSLISVavtkIIAKVLEDNKLP-GAICSLTCGgADIGTAMAKDERVNLLSFTGStqvgKQVGLMVQERFGRS--LL 295
Cdd:cd07147 158 PASRTPLSAL----ILGEVLAETGLPkGAFSVLPCS-RDDADLLVTDERIKLLSFTGS----PAVGWDLKARAGKKkvVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 296 ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTK 375
Cdd:cd07147 229 ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 376 QAVSMFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGL 455
Cdd:cd07147 309 SEAERVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1812588810 456 SSSIFTKDLGRIFR-WlgpKGSDCGIVNVN-IPTSGAEiGGAFGGEKHTGGGRE 507
Cdd:cd07147 386 QAGVFTRDLEKALRaW---DELEVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
71-524 |
3.77e-80 |
|
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: 258.04 E-value: 3.77e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ 148
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 149 EYVDICDYAVGLSRMIGGPI---LPSERSGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSl 225
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSynnLGDDMLGLVLRE---PIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 226 isvAVTKIIAKVLEDNKLPGAICS-LTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAII 304
Cdd:cd07118 160 ---GTTLMLAELLIEAGLPAGVVNiVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGA 384
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 385 VEEAKKEGGTVVYGGKVMD-RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07118 317 VDAGRAEGATLLLGGERLAsAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812588810 464 LGRIFrwLGPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07118 397 IDTAL--TVARRIRAGTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
71-507 |
4.07e-80 |
|
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: 258.06 E-value: 4.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL-VEGVGEVQE 149
Cdd:cd07108 4 PATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 150 YVDICDYAVGLSRMIGGPILPSeRSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07108 84 LADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 230 VTKIIAKVLednklPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07108 163 LAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 309 ADLSLVVPSALFAAVGT-AGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEE 387
Cdd:cd07108 238 ADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 388 AKKE-GGTVVYGGK----VMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 462
Cdd:cd07108 318 GLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1812588810 463 DLGRIFRwlGPKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 507
Cdd:cd07108 398 DLGRALR--AAHALEAGWVQVN-QGGGQQPGQSYGGFKQSGLGRE 439
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
56-507 |
3.65e-79 |
|
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: 256.50 E-value: 3.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07559 6 NGEWvaPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 134 LEMGKILVEGVGevqeyVDIcDYAVGLSRMIGGPILPSERSGHALIEQ------WNPVGLVGIITAFNFPVAVYGWNNAI 207
Cdd:cd07559 86 LDNGKPIRETLA-----ADI-PLAIDHFRYFAGVIRAQEGSLSEIDEDtlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 208 AMICGNVCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQ 287
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDLLP----KGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 288 ERFGRSLLELGGNNAIIAFEDADLSL--VVPSALFAAVGTA---GQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNP 362
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAMDADddFDDKAEEGQLGFAfnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 363 WDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKF 438
Cdd:cd07559 316 LDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812588810 439 KNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRE 507
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIGRE 461
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
56-469 |
1.22e-78 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 254.83 E-value: 1.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:PRK13473 8 NGELvAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 135 EMGK-ILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:PRK13473 88 NCGKpLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 214 VCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRS 293
Cdd:PRK13473 168 TVVLKPSEITPLTALKLAELAADILP----PGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLH 373
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 374 TKQAVSMFLGAVEEAKKEG-GTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:PRK13473 324 SAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSD 403
|
410
....*....|....*..
gi 1812588810 453 QGLSSSIFTKDLGRIFR 469
Cdd:PRK13473 404 YGLASSVWTRDVGRAHR 420
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
68-517 |
2.82e-78 |
|
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: 253.42 E-value: 2.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 68 TYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPApKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 146 EVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSL 225
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 226 ISVAVTKIIAKVLEdnkLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAII 304
Cdd:cd07120 159 INAAIIRILAEIPS---LPaGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGA 384
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 385 VEEAKKEGGTVVY-GGKVMDR--PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 461
Cdd:cd07120 316 VERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1812588810 462 KDLGRIFRWlgPKGSDCGIVNVNipTSGAEIGGA-FGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07120 396 RDLARAMRV--ARAIRAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
71-524 |
1.34e-77 |
|
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: 251.38 E-value: 1.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07109 4 PSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 150 YVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVA 229
Cdd:cd07109 84 AARYFEYYGGAADKLHGETIPLGPGYFVYTVR-EPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 230 vtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFED 308
Cdd:cd07109 163 ----LAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 309 ADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDpNVLYGPLHTKQAVSMFLGAVEEA 388
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 389 KKEGGTVVYGG-KVMDRP--GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLG 465
Cdd:cd07109 318 RARGARIVAGGrIAEGAPagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1812588810 466 RIFRWlgPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07109 398 RALRV--ARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
56-509 |
4.28e-77 |
|
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: 250.57 E-value: 4.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAW--KIWADIPAPKRGEIVRQIGDALREKIQVLGSL 131
Cdd:cd07139 4 GGRWvaPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 132 VSLEMGK-ILVEGVGEVQEYVDICDYAVGLSRmigGPILPSERS----GHALIEQwNPVGLVGIITAFNFPVAVYGWNNA 206
Cdd:cd07139 84 WTAENGMpISWSRRAQGPGPAALLRYYAALAR---DFPFEERRPgsggGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 207 IAMICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMV 286
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 287 QERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPN 366
Cdd:cd07139 236 GERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 367 VLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRP-----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNE 441
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGG---RPagldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812588810 442 EEVFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNIPTSgaEIGGAFGGEKHTGGGRESG 509
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERglaVARRI-----RTGTVGVNGFRL--DFGAPFGGFKQSGIGREGG 456
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
56-525 |
1.00e-76 |
|
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: 249.80 E-value: 1.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWA-DIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07082 7 NGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWpTMPLEERIDCLHKFADLLKENKEEVANLLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHAL----IEQWNPVGLVGIITAFNFPVavygwNNAI-- 207
Cdd:cd07082 87 WEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPL-----NLTVsk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 208 ---AMICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvg 283
Cdd:cd07082 162 lipALIMGNTVVFKPATQGVLLGI----PLAEAFHDAGFPkGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 284 LMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPW 363
Cdd:cd07082 236 LKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 364 DPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEE 443
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 444 VFAWNNEVKQGLSSSIFTKDLGRIF---RWLgpkgsDCGIVNVNIPTS-GAEIgGAFGGEKHTGGGRESGSDAWKQYMRR 519
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARklaDAL-----EVGTVNINSKCQrGPDH-FPFLGRKDSGIGTQGIGDALRSMTRR 467
|
....*.
gi 1812588810 520 STCTIN 525
Cdd:cd07082 468 KGIVIN 473
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
66-507 |
1.46e-76 |
|
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: 248.89 E-value: 1.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 146 EVQEYVDICDYAVGLSRMIGGPILP---SERSGHALIeqW---NPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPldaTQGSDNRLA--WtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 220 APTTSLISVAVTKIIakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLLELGG 299
Cdd:cd07094 159 ASKTPLSALELAKIL---VEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEA--LRANAGGKRIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVS 379
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 380 MFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 459
Cdd:cd07094 314 RVERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1812588810 460 FTKDLGRIFRwlGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRE 507
Cdd:cd07094 391 FTRDLNVAFK--AAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
71-524 |
2.61e-76 |
|
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: 248.04 E-value: 2.61e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRqasvADYEETVKKARE-AWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07146 6 PYTGEVVGTVP----AGTEEALREALAlAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 150 YVDICDYAVGLSRMIGGPILPSERSGHA----LIEQWNPVGLVGIITAFNFPVavygwNNAIAMIC-----GNVCLWKGA 220
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCDLTANGkarkIFTLREPLGVVLAITPFNHPL-----NQVAHKIApaiaaNNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 221 PTTSLISVAvtkiIAKVLEDNKLPGAICSLTCGG-ADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERfgRSLLELGG 299
Cdd:cd07146 157 EKTPLSAIY----LADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 300 NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVS 379
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 380 MFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 459
Cdd:cd07146 311 QIENRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812588810 460 FTKDLGRIFRWLgpKGSDCGIVNVN------IPTSgaeiggAFGGEKHTG-GGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07146 388 CTNDLDTIKRLV--ERLDVGTVNVNevpgfrSELS------PFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
63-518 |
7.16e-75 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 245.18 E-value: 7.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVE 142
Cdd:PRK13252 21 GETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 143 G-VGEVQEYVDICDYAVGLSRMIGGPILPSeRSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:PRK13252 101 TsVVDIVTGADVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 222 TTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 301
Cdd:PRK13252 180 VTPLTALK----LAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 381
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 382 LGAVEEAKKEGGTVVYGGKVMDR----PGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSS 457
Cdd:PRK13252 336 LGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812588810 458 SIFTKDLGRIFRWLGpkGSDCGIVNVNipTSG---AEIggAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:PRK13252 416 GVFTADLSRAHRVIH--QLEAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLEHYTQ 473
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
63-524 |
7.51e-75 |
|
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: 244.95 E-value: 7.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI---WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK- 138
Cdd:cd07141 21 GKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 139 ILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWK 218
Cdd:cd07141 101 FSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRH-EPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 219 GAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFGRS----- 293
Cdd:cd07141 180 PAEQTPLTALYLASLIK---EAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGK----LIQQAAGKSnlkrv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLH 373
Cdd:cd07141 253 TLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 374 TKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQ 453
Cdd:cd07141 333 DEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTY 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812588810 454 GLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAeIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07141 413 GLAAAVFTKDIDKAITF--SNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
71-526 |
1.09e-74 |
|
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: 244.66 E-value: 1.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKI-WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK-ILVEGVGEVQ 148
Cdd:cd07113 22 PATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKsIHLSRAFEVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 149 EYVDICDYAVGLSRMIGG----PILPS---ERsgHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAP 221
Cdd:cd07113 102 QSANFLRYFAGWATKINGetlaPSIPSmqgER--YTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 222 TTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN 301
Cdd:cd07113 180 FTPLTLLR----VAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 302 AIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMF 381
Cdd:cd07113 256 AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 382 LGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT 461
Cdd:cd07113 336 CSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWT 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 462 KDLGRIFRWLgPKgSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 526
Cdd:cd07113 416 NNLSKALRYI-PR-IEAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
71-509 |
2.48e-74 |
|
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: 243.03 E-value: 2.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 151 VDICDYAVGLS---RMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLIS 227
Cdd:cd07110 84 AGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 228 VAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAF 306
Cdd:cd07110 164 LELAEIAAEA----GLPpGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 307 EDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVE 386
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 387 EAKKEGGTVVYGGKVMD--RPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 464
Cdd:cd07110 320 RGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1812588810 465 GRIFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKHTGGGRESG 509
Cdd:cd07110 400 ERCDRV--AEALEAGIVWINCSQP-CFPQAPWGGYKRSGIGRELG 441
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
56-517 |
8.17e-74 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 242.50 E-value: 8.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:PRK11241 16 NGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:PRK11241 96 LEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 214 VCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCGGA-DIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGR 292
Cdd:PRK11241 176 TMVLKPASQTPFSALA----LAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 293 SLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPL 372
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 373 HTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 453 QGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGAEIgGAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRV--GEALEYGIVGINTGIISNEV-APFGGIKASGLGREGSKYGIEDYL 473
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
63-526 |
1.06e-73 |
|
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: 242.40 E-value: 1.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI--WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:cd07140 20 GKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 141 VEGVG-EVQEYVDICDYAVGLSRMIGGPILP--SERSGHAL-IEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCL 216
Cdd:cd07140 100 TLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 217 WKGAPTTSLISVAVTKIIAKVledNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVglM---VQERFGRS 293
Cdd:cd07140 180 LKPAQVTPLTALKFAELTVKA---GFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHI--MkscAVSNLKKV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 294 LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLH 373
Cdd:cd07140 255 SLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 374 TKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNE--EEVFAWNNEV 451
Cdd:cd07140 335 HKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDT 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 452 KQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINY 526
Cdd:cd07140 415 EYGLASGVFTKDINKALYV--SDKLEAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIEY 486
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
77-517 |
2.00e-73 |
|
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: 240.27 E-value: 2.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 77 IARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDY 156
Cdd:cd07152 4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 157 AVGLSRMIGGPILPSERsGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTslisvAVTK--II 234
Cdd:cd07152 84 AAGLPTQPQGEILPSAP-GRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT-----PVSGgvVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 235 AKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGlmvqERFGRSL----LELGGNNAIIAFEDAD 310
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVG----EAAGRHLkkvsLELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 311 LSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKK 390
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 391 EGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRw 470
Cdd:cd07152 314 AGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1812588810 471 LGPKgSDCGIVNVNIPTSGAEIGGAFGGEKHTG-GGRESGSDAWKQYM 517
Cdd:cd07152 390 LADR-LRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
63-517 |
9.09e-72 |
|
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: 236.34 E-value: 9.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 141 VEGV-GEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITR-EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 220 APTTSLisvavTKI-IAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQvgLMvqERFGRS---- 293
Cdd:cd07112 160 AEQSPL-----TALrLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRR--FL--EYSGQSnlkr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 294 -LLELGGNNAIIAFEDA-DLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGP 371
Cdd:cd07112 231 vWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 372 LHTKQAVSMFLGAVEEAKKEGGTVVYGGKV--MDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNN 449
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALAN 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588810 450 EVKQGLSSSIFTKDLGRIFRwlGPKGSDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHR--VARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
35-525 |
1.26e-71 |
|
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: 236.54 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 35 NQPqyawlkeLGLREENEGVYNGSwggrGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK-IWADIPAPKRGEI 113
Cdd:cd07144 5 DQP-------TGLFINNEFVKSSD----GETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 114 VRQIGDALREKIQVLGSLVSLEMGKIL-VEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQwNPVGLVGIIT 192
Cdd:cd07144 74 LDKLADLVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLH-EPYGVCGQII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 193 AFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLiSVAVtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLS 271
Cdd:cd07144 153 PWNYPLAMAAWKLAPALAAGNTVVIKPAENTPL-SLLY---FANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 272 FTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLK 351
Cdd:cd07144 229 FTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 352 KAYAQI-RVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGG---KVMDRPGNYVEPTIVTGLGHDASIAHTE 427
Cdd:cd07144 309 EHVKQNyKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 428 TFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiPTSGAEIGGAFGGEKHTGGGRE 507
Cdd:cd07144 389 IFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA--RELEAGMVWIN-SSNDSDVGVPFGGFKMSGIGRE 465
|
490
....*....|....*...
gi 1812588810 508 SGSDAWKQYMRRSTCTIN 525
Cdd:cd07144 466 LGEYGLETYTQTKAVHIN 483
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
56-486 |
1.03e-69 |
|
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: 231.25 E-value: 1.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07085 6 NGEWveSKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 134 LEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGN 213
Cdd:cd07085 86 LEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 214 VCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQvglmVQER---F 290
Cdd:cd07085 166 TFVLKPSERVPGAAM----RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEY----IYERaaaN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 291 GRSLLELGG-NNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLY 369
Cdd:cd07085 238 GKRVQALGGaKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 370 GPLHTKQAVSMFLGAVEEAKKEGGTVVYGG---KVMDRP-GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVF 445
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLDGrgvKVPGYEnGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1812588810 446 AWNNEVKQGLSSSIFTKD--LGRIFRwlgpKGSDCGIVNVNIP 486
Cdd:cd07085 398 AIINANPYGNGAAIFTRSgaAARKFQ----REVDAGMVGINVP 436
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
49-525 |
4.50e-69 |
|
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: 229.72 E-value: 4.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 49 EENEGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKI-WA-DIPAPKRGEIVRQIGDALRE 123
Cdd:cd07143 4 EQPTGLFiNGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGlKVSGSKRGRCLSKLADLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 124 KIQVLGSLVSLEMGK-ILVEGVGEVQEYVDICDYAVGLSRMIGGPILP--SERSGHALIEqwnPVGLVGIITAFNFPVAV 200
Cdd:cd07143 84 NLDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIEtdIKKLTYTRHE---PIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 201 YGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGK 280
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIP---EAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 281 qvglMVQERFGRS-----LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYA 355
Cdd:cd07143 238 ----KVMEAAAKSnlkkvTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 356 QIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYV 435
Cdd:cd07143 314 KLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 436 FKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGP-KGSDCGIVNVNIPTSGAeiggAFGGEKHTGGGRESGSDAWK 514
Cdd:cd07143 394 IKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANAlKAGTVWVNCYNLLHHQV----PFGGYKQSGIGRELGEYALE 469
|
490
....*....|.
gi 1812588810 515 QYMRRSTCTIN 525
Cdd:cd07143 470 NYTQIKAVHIN 480
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
70-517 |
1.08e-68 |
|
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: 227.96 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 70 CPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKilvegvGEVQE 149
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK------ARRHA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 150 YVDICDYAVGlSRMIG---GPILPSERSGHAL------IEQWNPVGLVGIITAFNFPVAVyGWNNAI-AMICGNVCLWKG 219
Cdd:cd07101 76 FEEVLDVAIV-ARYYArraERLLKPRRRRGAIpvltrtTVNRRPKGVVGVISPWNYPLTL-AVSDAIpALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 220 APTTSLISVAVTKIiakvLEDNKLPGAICSLTCG-GADIGTAMAkdERVNLLSFTGSTQVGKQVGlmvqERFGRSL---- 294
Cdd:cd07101 154 DSQTALTALWAVEL----LIEAGLPRDLWQVVTGpGSEVGGAIV--DNADYVMFTGSTATGRVVA----ERAGRRLigcs 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 295 LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHT 374
Cdd:cd07101 224 LELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLIS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 375 KQAVSMFLGAVEEAKKEGGTVVYGGKVmdRP--GNYV-EPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEV 451
Cdd:cd07101 304 QAQLDRVTAHVDDAVAKGATVLAGGRA--RPdlGPYFyEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588810 452 KQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVN--IPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYM 517
Cdd:cd07101 382 DYGLNASVWTRDGARG-RRIAAR-LRAGTVNVNegYAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYT 447
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
56-517 |
3.10e-67 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 225.77 E-value: 3.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW-----GGRGEVITtycPANNEPIARVRQASVADYEETVKKAREAW-----KIWADIPAPKRGEIVRQIGDALREKI 125
Cdd:PLN02467 13 GGEWrepvlGKRIPVVN---PATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 126 QVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGG----PI-LPSER-SGHALieqWNPVGLVGIITAFNFPVA 199
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqkaPVsLPMETfKGYVL---KEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 200 VYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQV 278
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREV----GLPpGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 279 GKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIR 358
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 359 VGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRP-----GNYVEPTIVTGLGHDASIAHTETFAPIL 433
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK---RPehlkkGFFIEPTIITDVTTSMQIWREEVFGPVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 434 YVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN--------IPtsgaeiggaFGGEKHTGGG 505
Cdd:PLN02467 400 CVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERV--SEAFQAGIVWINcsqpcfcqAP---------WGGIKRSGFG 468
|
490
....*....|..
gi 1812588810 506 RESGSDAWKQYM 517
Cdd:PLN02467 469 RELGEWGLENYL 480
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
60-511 |
3.63e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 220.52 E-value: 3.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 60 GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKI 139
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 140 LVEGVGEVQEYVDICDY----AVGL--SRMIGG--PILPSERsghaliEQWNPVGLVGIITAFNFPVAVyGWNNAI-AMI 210
Cdd:PRK09407 108 RRHAFEEVLDVALTARYyarrAPKLlaPRRRAGalPVLTKTT------ELRQPKGVVGVISPWNYPLTL-AVSDAIpALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 211 CGNVCLWKGAPTTSLISVAVtkiiAKVLEDNKLPGAICSLTCG-GADIGTAMAkdERVNLLSFTGSTQVGKQVGlmvqER 289
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAA----VELLYEAGLPRDLWQVVTGpGPVVGTALV--DNADYLMFTGSTATGRVLA----EQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 290 FGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDP 365
Cdd:PRK09407 251 AGRRLigfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 366 NVLYGPLHTKQ---AVSMFlgaVEEAKKEGGTVVYGGKVmdRP--GNYV-EPTIVTGLGHDASIAHTETFAPILYVFKFK 439
Cdd:PRK09407 331 SADMGSLISEAqleTVSAH---VDDAVAKGATVLAGGKA--RPdlGPLFyEPTVLTGVTPDMELAREETFGPVVSVYPVA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588810 440 NEEEVFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVN---IPTSGAeIGGAFGGEKHTGGGRESGSD 511
Cdd:PRK09407 406 DVDEAVERANDTPYGLNASVWTGDTARgraIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGLGRRHGAE 477
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
56-509 |
1.01e-64 |
|
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: 217.76 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW-----GGRGEVIttyCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGS 130
Cdd:cd07138 4 DGAWvapagTETIDVI---NPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 131 LVSLEMG-------KILVE-GVGEVQEYVDIC-DYAVglsrmiggpilpSERSGHALIeQWNPVGLVGIITAFNFPVavy 201
Cdd:cd07138 81 AITLEMGapitlarAAQVGlGIGHLRAAADALkDFEF------------EERRGNSLV-VREPIGVCGLITPWNWPL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 202 gwnNAI------AMICGNVCLWKG---APTTSLIsvavtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLS 271
Cdd:cd07138 145 ---NQIvlkvapALAAGCTVVLKPsevAPLSAII-------LAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 272 FTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLK 351
Cdd:cd07138 215 FTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 352 KAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGkvMDRP-----GNYVEPTIVTGLGHDASIAHT 426
Cdd:cd07138 295 AAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIARE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 427 ETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGR---IFRWLgpkgsDCGIVNVNipTSGAEIGGAFGGEKHTG 503
Cdd:cd07138 373 EIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERaraVARRL-----RAGQVHIN--GAAFNPGAPFGGYKQSG 445
|
....*.
gi 1812588810 504 GGRESG 509
Cdd:cd07138 446 NGREWG 451
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
63-518 |
8.41e-64 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 216.61 E-value: 8.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:PLN02766 35 GKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 141 VEGvgevqEYVDI------CDYAVGLSRMIGGPILPSERS--GHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMICG 212
Cdd:PLN02766 115 ALG-----KAVDIpaaaglLRYYAGAADKIHGETLKMSRQlqGYTLKE---PIGVVGHIIPWNFPSTMFFMKVAPALAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 213 NVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKqvglMVQERFG 291
Cdd:PLN02766 187 CTMVVKPAEQTPLSAL----FYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGR----KIMQAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 292 RS-----LLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPN 366
Cdd:PLN02766 259 TSnlkqvSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 367 VLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIK 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 447 WNNEVKQGLSSSIFTKDL---GRIFRWLgpkgsDCGIVNVNIpTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:PLN02766 419 KANNTKYGLAAGIVTKDLdvaNTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
28-509 |
4.93e-63 |
|
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: 214.75 E-value: 4.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 28 FMSTLLINQPQYAWLKE-LGLREENEG----VYNGSWGGRGEVITTYCPANNE-PIARVRQASVADYEETVKKAREAWKI 101
Cdd:cd07125 5 FVNRIFDLEVPLEALADaLKAFDEKEWeaipIINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 102 WADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICD-YAVGLSRMIGGPILPSErSGHALIE 180
Cdd:cd07125 85 WSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRyYAAQARELFSDPELPGP-TGELNGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 181 QWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIiakvLEDNKLPGAICSLT-CGGADIGT 259
Cdd:cd07125 164 ELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVEL----LHEAGVPRDVLQLVpGDGEEIGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 260 AMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLL---ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRL 336
Cdd:cd07125 240 ALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPliaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 337 FIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTIVTG 416
Cdd:cd07125 320 YLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 417 lghDASIAH-TETFAPILYVFKFKNE--EEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAeIG 493
Cdd:cd07125 399 ---VGIFDLtTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWR--ERVEAGNLYINRNITGA-IV 472
|
490
....*....|....*...
gi 1812588810 494 GA--FGGEKHTGGGRESG 509
Cdd:cd07125 473 GRqpFGGWGLSGTGPKAG 490
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
37-520 |
1.68e-62 |
|
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: 212.26 E-value: 1.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 37 PQYAWLKELGLREeneGVY-NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEI 113
Cdd:cd07111 10 CALAWLDAHDRSF---GHFiNGKWvkPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 114 VRQIGDALREKIQVLGSLVSLEMGKILVEgvgevqeyvdicdyavglSRMIGGPILPSERSGHALIEQ--------WNPV 185
Cdd:cd07111 87 LYRIARHIQKHQRLFAVLESLDNGKPIRE------------------SRDCDIPLVARHFYHHAGWAQlldtelagWKPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 186 GLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCGGADIGTAMAKDE 265
Cdd:cd07111 149 GVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEA----GLPPGVLNIVTGNGSFGSALANHP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 266 RVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDE 345
Cdd:cd07111 225 GVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 346 VVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAH 425
Cdd:cd07111 305 LIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 426 TETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRwLGPkGSDCGIVNVNI-----PTSGaeiggaFGGEK 500
Cdd:cd07111 385 EEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE-VAL-SLKAGVVWINGhnlfdAAAG------FGGYR 456
|
490 500
....*....|....*....|
gi 1812588810 501 HTGGGRESGSDAWKQYMRRS 520
Cdd:cd07111 457 ESGFGREGGKEGLYEYLRPS 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
115-469 |
3.53e-62 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 209.59 E-value: 3.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 115 RQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAF 194
Cdd:PRK10090 2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 195 NFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVlednKLPGAICSLTCG-GADIGTAMAKDERVNLLSFT 273
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGrGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 274 GSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKA 353
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 354 YAQIRVGNPWD-PNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPI 432
Cdd:PRK10090 238 MQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPV 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1812588810 433 LYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMK 354
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
54-519 |
2.04e-61 |
|
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: 210.13 E-value: 2.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 133 SLEMGKILVEGVGEVQEYVDICDY-AVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMIC 211
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 212 GNVCLWKGAPTTSLISVAVTKIIAkvlEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQER-- 289
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYKVFEIFH---EAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLap 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 290 ----FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDP 365
Cdd:cd07083 259 gqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 366 NVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEE--E 443
Cdd:cd07083 339 GTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaE 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812588810 444 VFAWNNEVKQGLSSSIFTKDLGRIfRWLGPKgSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKQYMRR 519
Cdd:cd07083 418 ALEVANSTPYGLTGGVYSRKREHL-EEARRE-FHVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGG---PHYLRR 489
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
71-466 |
9.81e-61 |
|
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: 207.10 E-value: 9.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 151 VDICDYAVGLSRMIGGPILPSERSG-HALIEQwNPVGLVGIITAFNFP--VAVygwnNAI--AMICGNVCLWKGAPTTSL 225
Cdd:cd07102 83 LERARYMISIAEEALADIRVPEKDGfERYIRR-EPLGVVLIIAPWNYPylTAV----NAVipALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 226 ISVAvtkiIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIA 305
Cdd:cd07102 158 CGER----FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 306 FEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAV 385
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 386 EEAKKEGGTVVYGGK---VMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTK 462
Cdd:cd07102 314 ADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
....
gi 1812588810 463 DLGR 466
Cdd:cd07102 394 DIAR 397
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
54-469 |
1.84e-59 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 205.17 E-value: 1.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 54 VYNGSWGGRGEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLV 132
Cdd:PRK03137 40 IIGGERITTEDKIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 133 SLEMGKILVEGVGEVQEYVDICDY----AVGLSRmiGGPIL--PSERSGHALIeqwnPVGLVGIITAFNFPVAVYGWNNA 206
Cdd:PRK03137 120 VKEAGKPWAEADADTAEAIDFLEYyarqMLKLAD--GKPVEsrPGEHNRYFYI----PLGVGVVISPWNFPFAIMAGMTL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 207 IAMICGNVCLWKGAPTTSLISVAVtkiiAKVLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGStqvgKQVGLM 285
Cdd:PRK03137 194 AAIVAGNTVLLKPASDTPVIAAKF----VEVLEEAGLPaGVVNFVPGSGSEVGDYLVDHPKTRFITFTGS----REVGLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 286 VQER----------FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYA 355
Cdd:PRK03137 266 IYERaakvqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 356 QIRVGNPWDPNVLyGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYV 435
Cdd:PRK03137 346 ELTVGNPEDNAYM-GPVINQASFDKIMSYIEIGKEE-GRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAF 423
|
410 420 430
....*....|....*....|....*....|....
gi 1812588810 436 FKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:PRK03137 424 IKAKDFDHALEIANNTEYGLTGAVISNNREHLEK 457
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-524 |
4.98e-59 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 202.04 E-value: 4.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 87 DYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMG------KILVEGVGEVqeyvdICDYAVGL 160
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGataawaGFNVDLAAGM-----LREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 161 SRMIGGPIlPSERSGH-ALIEQwNPVGLVGIITAFNFPVAVYGwnNAIAM--ICGNVCLWKG---APTTSLIsvavtkiI 234
Cdd:cd07105 76 TQIIGGSI-PSDKPGTlAMVVK-EPVGVVLGIAPWNAPVILGT--RAIAYplAAGNTVVLKAselSPRTHWL-------I 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 235 AKVLEDNKLP-GAICSLTCGGAD---IGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDAD 310
Cdd:cd07105 145 GRVFHEAGLPkGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 311 LSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIrvgnPWDPNVLyGPLHTKQAVSMFLGAVEEAKK 390
Cdd:cd07105 225 LDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKL----FAGPVVL-GSLVSAAAADRVKELVDDALS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 391 EGGTVVYGGKVMDRP-GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFR 469
Cdd:cd07105 300 KGAKLVVGGLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 470 wLGpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTI 524
Cdd:cd07105 380 -VA-KRIESGAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-512 |
5.97e-59 |
|
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: 201.73 E-value: 5.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 87 DYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRmigg 166
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYH---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 167 pilpsERSG--------HALIEQWNPVGLVGIITAFNFPVAVYgwNNAI--AMICGNVCLWKGAPTTSlisvAVTKIIAK 236
Cdd:cd07095 77 -----ERTGeratpmaqGRAVLRHRPHGVMAVFGPFNFPGHLP--NGHIvpALLAGNTVVFKPSELTP----AVAELMVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 237 VLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSL-LELGGNNAIIAFEDADLSLVV 315
Cdd:cd07095 146 LWEEAGLPPGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 316 PSALFAAVGTAGQRCTTARRLFIHES-IHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGT 394
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 395 VVYGGKVMDRPGNYVEPTI--VTGLghdASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLG 472
Cdd:cd07095 306 PLLAMERLVAGTAFLSPGIidVTDA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDD-EALFERFL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1812588810 473 PKgSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDA 512
Cdd:cd07095 382 AR-IRAGIVNWNRPTTGASSTAPFGGVGLSGNHRPSAYYA 420
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
63-518 |
2.55e-58 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 202.73 E-value: 2.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKIL 140
Cdd:PLN02466 72 GKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 141 VEGVG-EVQEYVDICDYAVGLSRMIGGPILPSErSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:PLN02466 152 EQSAKaELPMFARLFRYYAGWADKIHGLTVPAD-GPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 220 APTTSLISVAVtkiiAKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQV-GLMVQERFGRSLLEL 297
Cdd:PLN02466 231 AEQTPLSALYA----AKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVlELAAKSNLKPVTLEL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 298 GGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQA 377
Cdd:PLN02466 307 GGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQ 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 378 VSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSS 457
Cdd:PLN02466 387 FEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAA 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1812588810 458 SIFTKDL---GRIFRWLgpkgsDCGIVNVN--------IPtsgaeiggaFGGEKHTGGGRESGSDAWKQYMR 518
Cdd:PLN02466 467 GVFTQNLdtaNTLSRAL-----RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
69-509 |
8.32e-53 |
|
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: 185.97 E-value: 8.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 69 YCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGV-GEV 147
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 148 qeyVDICDYAVGLSRMIGGPILPSERSGHALIE------QWNPVGLVGIITAFNFPvavygWNNAI-----AMICGNVCL 216
Cdd:cd07098 81 ---LVTCEKIRWTLKHGEKALRPESRPGGLLMFykrarvEYEPLGVVGAIVSWNYP-----FHNLLgpiiaALFAGNAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 217 WKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLE 296
Cdd:cd07098 153 VKVSEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 297 LGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQ 376
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 377 AVSMFLGAVEEAKKEGGTVVYGGKVMDRP----GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVK 452
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812588810 453 QGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNiptsgaEIGGA-------FGGEKHTGGGRESG 509
Cdd:cd07098 393 YGLGASVFGKDIKRARRIA--SQLETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
60-523 |
1.65e-51 |
|
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: 182.77 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 60 GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKI 139
Cdd:TIGR01722 12 GASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 140 LVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKG 219
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 220 APTTSLISVAVtkiiAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVgLMVQERFGRSLLELGG 299
Cdd:TIGR01722 172 SEKVPSAAVKL----AELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYI-HTTGSAHGKRVQALGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 300 -NNAIIAFEDADLSLVVPSALFAAVGTAGQRCtTARRLFIHESIHDEVVNRLKKAYAQIRVGnPW-DPNVLYGPLHTKQA 377
Cdd:TIGR01722 247 aKNHMVVMPDADKDAAADALVGAAYGAAGQRC-MAISAAVLVGAADEWVPEIRERAEKIRIG-PGdDPGAEMGPLITPQA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 378 VSMFLGAVEEAKKEGGTVVYGG---KVMDRP-GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQ 453
Cdd:TIGR01722 325 KDRVASLIAGGAAEGAEVLLDGrgyKVDGYEeGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPY 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812588810 454 GLSSSIFTKDLG--RIFRWLgpkgSDCGIVNVNIPTSGAEIGGAFGGEKHT--GGGRESGSDAWKQYMRRSTCT 523
Cdd:TIGR01722 405 GNGTAIFTRDGAaaRRFQHE----IEVGQVGVNVPIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
71-507 |
1.94e-51 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 182.37 E-value: 1.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEY 150
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 151 VDICD-YAV-GLSRMIGGPILPSERsgHALIEqWNPVGLVGIITAFNFPVavygWN---NAIAMI-CGNVCLWKGAPTTs 224
Cdd:PRK13968 94 ANLCDwYAEhGPAMLKAEPTLVENQ--QAVIE-YRPLGTILAIMPWNFPL----WQvmrGAVPILlAGNGYLLKHAPNV- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 225 lisVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAII 304
Cdd:PRK13968 166 ---MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 305 AFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGA 384
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 385 VEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDL 464
Cdd:PRK13968 323 VEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDE 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1812588810 465 GRIFRWlgPKGSDCGIVNVN-IPTSGAEIggAFGGEKHTGGGRE 507
Cdd:PRK13968 403 TQARQM--AARLECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
56-508 |
8.68e-48 |
|
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: 173.02 E-value: 8.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSWGG--RGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:cd07116 6 GGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 134 LEMGKILVEGVG-EVQEYVDICDYAVGLSRMIGGPI--LPSERSGHALIEqwnPVGLVGIITAFNFPVAVYGWNNAIAMI 210
Cdd:cd07116 86 WDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSIseIDENTVAYHFHE---PLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 211 CGNVCLWKGAPTTSLISVAVTKIIAKVLEdnklPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF 290
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDLLP----PGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 291 GRSLLELGGNNAIIAFED---ADLSLVVPS----ALFAAvgTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPW 363
Cdd:cd07116 239 IPVTLELGGKSPNIFFADvmdADDAFFDKAlegfVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 364 DPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGN----YVEPTIVTGlGHDASIAHTETFAPILYVFKFK 439
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLlgggYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812588810 440 NEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVN----IPTsgaeiGGAFGGEKHTGGGRES 508
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGREN 461
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
38-524 |
1.61e-47 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 172.39 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 38 QYAWLKELGLREENEGVYNGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKRGEI 113
Cdd:PRK09847 7 AYWQDKALSLAIENRLFINGEYtaAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 114 VRQIGDALREKIQVLGSLVSLEMGKIL-------VEGVGEVQEYvdicdYAVGLSRMIGgPILPSERSGHALIEQwNPVG 186
Cdd:PRK09847 87 LNKLADLMEAHAEELALLETLDTGKPIrhslrddIPGAARAIRW-----YAEAIDKVYG-EVATTSSHELAMIVR-EPVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 187 LVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAvtkiIAKVLEDNKLPGAICSLTCG-GADIGTAMAKDE 265
Cdd:PRK09847 160 VIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIR----LAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 266 RVNLLSFTGSTQVGKQvgLMV---QERFGRSLLELGGNNAIIAFEDA-DLSLVVPSALFAAVGTAGQRCTTARRLFIHES 341
Cdd:PRK09847 236 DIDAIAFTGSTRTGKQ--LLKdagDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 342 IHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGgTVVYGGKVMDRPGnYVEPTIVTGLGHDA 421
Cdd:PRK09847 314 IADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 422 SIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWlgPKGSDCGIVNVNIPTSGaEIGGAFGGEKH 501
Cdd:PRK09847 392 SLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM--SRRLKAGSVFVNNYNDG-DMTVPFGGYKQ 468
|
490 500
....*....|....*....|...
gi 1812588810 502 TGGGRESGSDAWKQYMRRSTCTI 524
Cdd:PRK09847 469 SGNGRDKSLHALEKFTELKTIWI 491
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
56-508 |
1.65e-46 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 169.37 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:PRK09457 6 NGDWiAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 135 EMGKILVEGVGEVQEYVDicdyAVGLSrmiggpILP-SERSGHALIE--------QWNPVGLVGIITAFNFPVAVYgwNN 205
Cdd:PRK09457 86 ETGKPLWEAATEVTAMIN----KIAIS------IQAyHERTGEKRSEmadgaavlRHRPHGVVAVFGPYNFPGHLP--NG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 206 AI--AMICGNVCLWKGAPTTSlisvAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVG 283
Cdd:PRK09457 154 HIvpALLAGNTVVFKPSELTP----WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 284 LMVQERFGRSL-LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIH-DEVVNRLKKAYAQIRVGN 361
Cdd:PRK09457 230 RQFAGQPEKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 362 PW-DPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTI--VTGLghdASIAHTETFAPILYVFKF 438
Cdd:PRK09457 310 WDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIidVTGV---AELPDEEYFGPLLQVVRY 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 439 KNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES 508
Cdd:PRK09457 387 DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFL--LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPS 454
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
66-507 |
6.09e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 167.22 E-value: 6.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 66 ITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVG 145
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 146 EVQEYVDICDY-----------------AVGLSRmiggpilpsersghALIeQWNPVGLVGIITAFNFPVavygWN---- 204
Cdd:PRK09406 83 EALKCAKGFRYyaehaealladepadaaAVGASR--------------AYV-RYQPLGVVLAVMPWNFPL----WQvvrf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 205 NAIAMICGNVCLWKGA---PTTSLIsvavtkiIAKVLEDNKLP-GAICSLTCGgADIGTAMAKDERVNLLSFTGSTQVGK 280
Cdd:PRK09406 144 AAPALMAGNVGLLKHAsnvPQTALY-------LADLFRRAGFPdGCFQTLLVG-SGAVEAILRDPRVAAATLTGSEPAGR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 281 QVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVG 360
Cdd:PRK09406 216 AVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 361 NPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKN 440
Cdd:PRK09406 296 DPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588810 441 EEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLgpKGSDCGIVNVN-IPTSGAEIGgaFGGEKHTGGGRE 507
Cdd:PRK09406 376 IDEAIEIANATTFGLGSNAWTRDEAEQERFI--DDLEAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
56-520 |
2.60e-45 |
|
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: 166.62 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSWGGRGEVITTYCPANNEPI-ARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSL 134
Cdd:TIGR01238 43 GHSYKADGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 135 EMGKILVEGVGEVQEYVDICDYAVGLSRmiggPILPSERSghalieqwNPVGLVGIITAFNFPVAVYGWNNAIAMICGNV 214
Cdd:TIGR01238 123 EAGKTIHNAIAEVREAVDFCRYYAKQVR----DVLGEFSV--------ESRGVFVCISPWNFPLAIFTGQISAALAAGNT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 215 CLWKGAPTTSLISvavTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF---G 291
Cdd:TIGR01238 191 VIAKPAEQTSLIA---YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 292 RSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGP 371
Cdd:TIGR01238 268 PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 372 LHTKQAVSMFLGAVEEAKKEGGTV---VYGGKVMDRPGNYVEPTIVTGLGHDAsiAHTETFAPILYVFKFKNEE--EVFA 446
Cdd:TIGR01238 348 VIDAEAKQNLLAHIEHMSQTQKKIaqlTLDDSRACQHGTFVAPTLFELDDIAE--LSEEVFGPVLHVVRYKAREldQIVD 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 447 WNNEVKQGLSSSIFTKDLGRIfRWLgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSDAWKQYMRRS 520
Cdd:TIGR01238 426 QINQTGYGLTMGVHSRIETTY-RWI-EKHARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGGPHYLYRLTQV 498
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
63-442 |
2.90e-45 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 171.27 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILV 141
Cdd:COG4230 569 GEARPVRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLP 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 142 EGVGEVQEYVDICD-YAVGLSRMIGGPilpsersghaliEQWNPVGLVGIITAFNFPVA-----VygwnnAIAMICGNVC 215
Cdd:COG4230 649 DAIAEVREAVDFCRyYAAQARRLFAAP------------TVLRGRGVFVCISPWNFPLAiftgqV-----AAALAAGNTV 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 216 LWKGAPTTSLI-SVAVtkiiaKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRS 293
Cdd:COG4230 712 LAKPAEQTPLIaARAV-----RLLHEAGVPADVLQLLPGdGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 294 LL---ELGGNNAIIAfedaDLS-L---VVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPN 366
Cdd:COG4230 787 VPliaETGGQNAMIV----DSSaLpeqVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLS 862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588810 367 VLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMDRP--GNYVEPTIVTgLGHDASIAHtETFAPILYVFKFKNEE 442
Cdd:COG4230 863 TDVGPVIDAEARANLEAHIERMRAE-GRLVHQLPLPEECanGTFVAPTLIE-IDSISDLER-EVFGPVLHVVRYKADE 937
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
71-505 |
4.71e-45 |
|
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: 164.90 E-value: 4.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PANNEPIARVRQASVADYEETVKKAREAWKIWAD-IPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:cd07148 6 PFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 150 YVDICDYAVGLSRMIGGPILP----SERSGHALIEQWNPVGLVGIITAFNFPV--AVYGWNNAIAMICGnvCLWKGAPTT 223
Cdd:cd07148 86 AIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLnlIVHQVAPAIAAGCP--VIVKPALAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 224 SLISVAVTKIiakvLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGkqvgLMVQERFG---RSLLELGGN 300
Cdd:cd07148 164 PLSCLAFVDL----LHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVG----WMLRSKLApgtRCALEHGGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 301 NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSM 380
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 381 FLGAVEEAKKEGGTVVYGGKVMDRpgNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIF 460
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1812588810 461 TKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGG 505
Cdd:cd07148 394 TKDLDVALKAV--RRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
60-442 |
6.21e-45 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 170.38 E-value: 6.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 60 GGRGEVITTYCPANNE-PIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK 138
Cdd:PRK11904 558 NGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 139 ILVEGVGEVQEYVDICD-YAVGLSRMIGGPI-LPSersghalieqwnPVG------LVG-----IITAFNFPVAVYGWNN 205
Cdd:PRK11904 638 TLQDAIAEVREAVDFCRyYAAQARRLFGAPEkLPG------------PTGesnelrLHGrgvfvCISPWNFPLAIFLGQV 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 206 AIAMICGNVCLWKGAPTTSLISVAVTKIiakvLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGL 284
Cdd:PRK11904 706 AAALAAGNTVIAKPAEQTPLIAAEAVKL----LHEAGIPKDVLQLLPGdGATVGAALTADPRIAGVAFTGSTETARIINR 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 285 MVQERFGRSL---LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGN 361
Cdd:PRK11904 782 TLAARDGPIVpliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGD 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 362 PWDPNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKVMD--RPGNYVEPTIVTgLGhDASIAHTETFAPILYVFKFK 439
Cdd:PRK11904 862 PRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAgtENGHFVAPTAFE-ID-SISQLEREVFGPILHVIRYK 938
|
...
gi 1812588810 440 NEE 442
Cdd:PRK11904 939 ASD 941
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
71-519 |
1.66e-43 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 166.19 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 71 PAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQE 149
Cdd:PRK11905 574 PADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVRE 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 150 YVDICD-YAVGLSRMIGGPILPsersghalieqwnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLI-S 227
Cdd:PRK11905 654 AVDFLRyYAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIaA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 228 VAVtkiiaKVLEDNKLPGAICSLTCG-GADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLL---ELGGNNAI 303
Cdd:PRK11905 721 RAV-----RLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAM 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 304 IAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLG 383
Cdd:PRK11905 796 IVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 384 AVEEAKKEGGTVvyggKVMDRP-----GNYVEPTIVTgLGHDASIAHtETFAPILYVFKFKNEE--EVFAWNNEVKQGLS 456
Cdd:PRK11905 876 HIEAMRAAGRLV----HQLPLPaetekGTFVAPTLIE-IDSISDLER-EVFGPVLHVVRFKADEldRVIDDINATGYGLT 949
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1812588810 457 SSIFTKDLGRIFRWLgpKGSDCGIVNVNIPTSGAEIG-GAFGGEKHTGGGRESGSdawKQYMRR 519
Cdd:PRK11905 950 FGLHSRIDETIAHVT--SRIRAGNIYVNRNIIGAVVGvQPFGGEGLSGTGPKAGG---PLYLGR 1008
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
56-466 |
5.95e-41 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 154.53 E-value: 5.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW--GGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVS 133
Cdd:PLN00412 21 DGEWrtSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 134 LEMGKILVEGVGEVQEYVDICDYAV--GLSRMIGGPILPS------ERSGHALIEQWnPVGLVGIITAFNFPVAVYGWNN 205
Cdd:PLN00412 101 KEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFLVSdsfpgnERNKYCLTSKI-PLGVVLAIPPFNYPVNLAVSKI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 206 AIAMICGNVCLWKgAPTTSliSVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGStqvgkQVGLM 285
Cdd:PLN00412 180 APALIAGNAVVLK-PPTQG--AVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-----DTGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 286 VQERFGRSLL--ELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPW 363
Cdd:PLN00412 252 ISKKAGMVPLqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 364 DpNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKvmdRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEE 443
Cdd:PLN00412 332 D-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEE 407
|
410 420
....*....|....*....|...
gi 1812588810 444 VFAWNNEVKQGLSSSIFTKDLGR 466
Cdd:PLN00412 408 GIHHCNASNFGLQGCVFTRDINK 430
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
17-531 |
1.94e-40 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 154.52 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 17 KLSGPWSRPA-----AFMSTLLINQPQYAWLKELGLREENegVYNGSW--GGRGEVITTYCPANNEPIARVRQASVADYE 89
Cdd:PLN02419 77 RISGNNLRPLrpqflALRSSWLSTSPEQSTQPQMPPRVPN--LIGGSFveSQSSSFIDVINPATQEVVSKVPLTTNEEFK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 90 ETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPIL 169
Cdd:PLN02419 155 AAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 170 PSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVavtkIIAKVLEDNKLPGAICS 249
Cdd:PLN02419 235 PNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASV----ILAELAMEAGLPDGVLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 250 LTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQR 329
Cdd:PLN02419 311 IVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQR 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 330 CTT-ARRLFIHE--SIHDEVVNRLKKayaqIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRP- 405
Cdd:PLN02419 391 CMAlSTVVFVGDakSWEDKLVERAKA----LKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPg 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 406 ---GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD--LGRIFRwlgpKGSDCGI 480
Cdd:PLN02419 467 yekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSgaAARKFQ----MDIEAGQ 542
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1812588810 481 VNVNIPTSGAEIGGAFGGEKHTGGGR-----ESGSDAWKQYmrrSTCTINYsKDLP 531
Cdd:PLN02419 543 IGINVPIPVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQI---KLVTQKQ-KDIH 594
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
77-442 |
9.42e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 136.64 E-value: 9.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 77 IARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDY 156
Cdd:PRK11809 673 VGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRY 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 157 AVGLSRmiggpilpsersGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIak 236
Cdd:PRK11809 753 YAGQVR------------DDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRIL-- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 237 vLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERF---GRS---LLELGGNNAIIAFEDAD 310
Cdd:PRK11809 819 -LEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqGRPiplIAETGGQNAMIVDSSAL 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 311 LSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKK 390
Cdd:PRK11809 898 TEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRA 977
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 391 EGGTV---VYGGKVMDRPGNYVEPTIVTgLGHDASIAHtETFAPILYVFKFKNEE 442
Cdd:PRK11809 978 KGRPVfqaARENSEDWQSGTFVPPTLIE-LDSFDELKR-EVFGPVLHVVRYNRNQ 1030
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
63-463 |
3.00e-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: 130.01 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 63 GEVITTYCPAN-NEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKI-QVLGSLVSLEMGKIL 140
Cdd:cd07123 45 GNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 141 VEGvgEVQEYVDICD-------YAVGLSRMigGPILPSERSGHALieQWNPV-GLVGIITAFNFpVAVYGwNNAIA-MIC 211
Cdd:cd07123 125 WQA--EIDAACELIDflrfnvkYAEELYAQ--QPLSSPAGVWNRL--EYRPLeGFVYAVSPFNF-TAIGG-NLAGApALM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 212 GNVCLWKGAPTTSLISVAVTKIiakvLEDNKLP-GAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQER- 289
Cdd:cd07123 197 GNVVLWKPSDTAVLSNYLVYKI----LEEAGLPpGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 290 -----FGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWD 364
Cdd:cd07123 273 dryrtYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 365 PNVLYGPLHTKQAVSMFLGAVEEAKKEGG-TVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPIL--YVFKFKNE 441
Cdd:cd07123 353 FSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLtvYVYPDSDF 432
|
410 420
....*....|....*....|...
gi 1812588810 442 EEVFAWNNEV-KQGLSSSIFTKD 463
Cdd:cd07123 433 EETLELVDTTsPYALTGAIFAQD 455
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
184-505 |
5.68e-32 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 128.61 E-value: 5.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPV--AVYGWNNAIAmiCGNVCLWKgaptTSLISVAVTKIIAKVLeDNKLPGAICSLTCGGADIGTAM 261
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLnlTLIPLAGAIA--AGNTVVLK----PSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 262 AKdERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHES 341
Cdd:PTZ00381 182 LK-EPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 342 IHDEVVNRLKKAYAQIRVGNPW---DPNVLYGPLHTKQAVSMFlgaveeaKKEGGTVVYGGKVmDRPGNYVEPTIVTGLG 418
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPKkseDYSRIVNEFHTKRLAELI-------KDHGGKVVYGGEV-DIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 419 HDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIV---------NVNIPtsg 489
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED-KRHKELVLENTSSGAVVindcvfhllNPNLP--- 408
|
330
....*....|....*.
gi 1812588810 490 aeiggaFGGEKHTGGG 505
Cdd:PTZ00381 409 ------FGGVGNSGMG 418
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
184-463 |
5.26e-30 |
|
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: 121.86 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPV------AVygwnNAIAmiCGNVCLWKG---APTTSlisvavtKIIAKVLEDnKLPGAICSLTCGG 254
Cdd:cd07087 100 PLGVVLIIGPWNYPLqlalapLI----GAIA--AGNTVVLKPselAPATS-------ALLAKLIPK-YFDPEAVAVVEGG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 255 ADIGTAMAKdERVNLLSFTGSTQVGKQVglMvqERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRC 330
Cdd:cd07087 166 VEVATALLA-EPFDHIFFTGSPAVGKIV--M--EAAAKHLtpvtLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 331 TTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWD-PNvlYGPL----HTKQAVSMFlgaveeakkEGGTVVYGGKVmDRP 405
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKEsPD--YGRIinerHFDRLASLL---------DDGKVVIGGQV-DKE 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588810 406 GNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07087 309 ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSED 366
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
184-463 |
2.21e-28 |
|
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: 117.32 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPV-----AVYGwnnAIAmiCGNVCLWKG---APTTSLIsvaVTKIIAKVLEdnklPGAICSLTCGGA 255
Cdd:cd07135 108 PLGVVLIIGPWNYPVllalsPLVG---AIA--AGCTVVLKPselTPHTAAL---LAELVPKYLD----PDAFQVVQGGVP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 256 DIGTAMakDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCT 331
Cdd:cd07135 176 ETTALL--EQKFDKIFYTGSGRVGR----IIAEAAAKHLtpvtLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 332 TARRLFIHESIHDEVVNRLKKAYAQiRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKkegGTVVYGGKvMDRPGNYVEP 411
Cdd:cd07135 250 APDYVLVDPSVYDEFVEELKKVLDE-FYPGGANASPDYTRIVNPRHFNRLKSLLDTTK---GKVVIGGE-MDEATRFIPP 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1812588810 412 TIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
184-463 |
5.42e-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: 116.45 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFP-----VAVYGwnnAIAmiCGNVCLWKgaPttSLISVAVTKIIAKVLEDNKLPGAICSLTcGGADIG 258
Cdd:cd07136 100 PYGVVLIIAPWNYPfqlalAPLIG---AIA--AGNTAVLK--P--SELTPNTSKVIAKIIEETFDEEYVAVVE-GGVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 259 TAMAkDERVNLLSFTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTAR 334
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVGK----IVMEAAAKHLtpvtLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 335 RLFIHESIHDEVVNRLKKayaQIRVGNPWDP--NVLYGPL----HTKQAVSMFlgaveeakkEGGTVVYGGKVmDRPGNY 408
Cdd:cd07136 245 YVLVHESVKEKFIKELKE---EIKKFYGEDPleSPDYGRIinekHFDRLAGLL---------DNGKIVFGGNT-DRETLY 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1812588810 409 VEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07136 312 IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED 366
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
184-509 |
4.47e-25 |
|
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: 107.70 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPVA------VYgwnnAIAmiCGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLpgAICSltcGGADI 257
Cdd:cd07134 100 PKGVCLIISPWNYPFNlafgplVS----AIA--AGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFE---GDAEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 258 GTAmakdervnLLS-------FTGSTQVGKqvglMVQERFGRSL----LELGGNNAIIAFEDADLSLVVPSALFAAVGTA 326
Cdd:cd07134 169 AQA--------LLElpfdhifFTGSPAVGK----IVMAAAAKHLasvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 327 GQRCTTARRLFIHESIHDEVVNRLKKAYAQIrvgnpwdpnvlYGPLHTKQAVSMF------------LGAVEEAKKEGGT 394
Cdd:cd07134 237 GQTCIAPDYVFVHESVKDAFVEHLKAEIEKF-----------YGKDAARKASPDLarivndrhfdrlKGLLDDAVAKGAK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 395 VVYGGKVmDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPK 474
Cdd:cd07134 306 VEFGGQF-DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1812588810 475 GS-DCGI-------VNVNIPtsgaeiggaFGGEKHTGGGRESG 509
Cdd:cd07134 385 SSgGVVVndvvlhfLNPNLP---------FGGVNNSGIGSYHG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
95-520 |
2.51e-24 |
|
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: 105.78 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 95 AREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGK--ILVEGVGEVQEYVDICDYAVGLSRMIGGPI--LP 170
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwMFAENICGDQVQLRARAFVIYSYRIPHEPGnhLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 171 SERSGHALIEQWnPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLednKLPGAICSL 250
Cdd:cd07084 88 QGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG---LLPPEDVTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 251 TCGGADIGTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLLELGGNNAIIAFEDAD-LSLVVPSALFAAVGTAGQR 329
Cdd:cd07084 164 INGDGKTMQALLLHPNPKMVLFTGSSRVAEK--LALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 330 CTTARRLFIHESIHDE-VVNRLKKAYAQIRVGnpwdpNVLYGPLHTKQAVSMflgaVEEAKKEGGTVV-YGGKVM---DR 404
Cdd:cd07084 242 CTAQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQTFTTLAM----IAHMENLLGSVLlFSGKELknhSI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 405 PGNY----VEPTIVTGLGHDAS-IAHT-ETFAPILYVFKFKNEEEVFAWN-NEVKQG-LSSSIFTKD---LGRifrwLGP 473
Cdd:cd07084 313 PSIYgacvASALFVPIDEILKTyELVTeEIFGPFAIVVEYKKDQLALVLElLERMHGsLTAAIYSNDpifLQE----LIG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1812588810 474 KGSDCGIVNVNIPTSgaeiGGAFGGEKHTGGGRES-------GSDAWKQYMRRS 520
Cdd:cd07084 389 NLWVAGRTYAILRGR----TGVAPNQNHGGGPAADprgagigGPEAIKLVWRCH 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
56-520 |
1.01e-23 |
|
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: 104.66 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSW-GGRGEVITTYCPANNEPIARVRQASVaDYEETVKKAREawkiwadIPAPK--------RGEIVRQIGDALREK-- 124
Cdd:cd07128 6 AGQWhAGTGDGRTLHDAVTGEVVARVSSEGL-DFAAAVAYARE-------KGGPAlraltfheRAAMLKALAKYLMERke 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 125 -----------------------IQVL---GSLVSLEM--GKILVEGVGEVqeyvdicdyavgLSR---MIGGPILpSER 173
Cdd:cd07128 78 dlyalsaatgatrrdswididggIGTLfayASLGRRELpnAHFLVEGDVEP------------LSKdgtFVGQHIL-TPR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 174 SGHALIeqwnpvglvgiITAFNFPVavygW----NNAIAMICGNVCLWKGAPTTSLISVAVTKIIakvLEDNKLP-GAIc 248
Cdd:cd07128 145 RGVAVH-----------INAFNFPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDI---VESGLLPeGAL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 249 SLTCGGAdiGTAMAKDERVNLLSFTGSTQVGKQVGLM--VQERFGRSLLELGGNNAIIAFEDA-----DLSLVVPSALFA 321
Cdd:cd07128 206 QLICGSV--GDLLDHLGEQDVVAFTGSAATAAKLRAHpnIVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVARE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 322 AVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEgGTVVYGGKV 401
Cdd:cd07128 284 MTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 402 MDRP-------GNYVEPTIVTGLG-HDASIAH-TETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD---LGRIFR 469
Cdd:cd07128 363 RFEVvgadaekGAFFPPTLLLCDDpDAATAVHdVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafARELVL 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 470 WLGPKGsdcGIVNVNIPTSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYMRRS 520
Cdd:cd07128 443 GAAPYH---GRLLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRT 499
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
181-463 |
1.32e-19 |
|
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: 91.51 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 181 QWNPVGLVGIITAFNFPVA-----VYGwnnAIAmiCGNVCLWKgaPttSLISVAVTKIIAKVLE---DNKLPGAIcsltC 252
Cdd:cd07132 97 YKEPLGVVLIIGAWNYPLQltlvpLVG---AIA--AGNCVVIK--P--SEVSPATAKLLAELIPkylDKECYPVV----L 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 253 GGADIGTAMAKdERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTT 332
Cdd:cd07132 164 GGVEETTELLK-QRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 333 ARRLFIHESIHDEVVNRLKKAYAQIRVGNPWD-PNvlYGPL----HTKQAVSMFlgaveeakkEGGTVVYGGKVmDRPGN 407
Cdd:cd07132 243 PDYVLCTPEVQEKFVEALKKTLKEFYGEDPKEsPD--YGRIindrHFQRLKKLL---------SGGKVAIGGQT-DEKER 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1812588810 408 YVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD 463
Cdd:cd07132 311 YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
184-446 |
5.91e-19 |
|
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: 89.47 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPVAVygwnnAIA-MIC----GNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLpgaicSLTCGGADIG 258
Cdd:cd07133 101 PLGVVGIIVPWNYPLYL-----ALGpLIAalaaGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-----AVVTGGADVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 259 TAMAK---DervNLLsFTGSTQVGKQVglM---------VQerfgrslLELGGNN-AIIAfEDADLSLVVPSALFAAVGT 325
Cdd:cd07133 171 AAFSSlpfD---HLL-FTGSTAVGRHV--MraaaenltpVT-------LELGGKSpAIIA-PDADLAKAAERIAFGKLLN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 326 AGQRCTTARRLFIHESIHDEVVNRLKKAYAQI---RVGNPwDpnvlYGPLHTKQAVSMFLGAVEEAKKEGGTVVyggKVM 402
Cdd:cd07133 237 AGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-D----YTSIINERHYARLQGLLEDARAKGARVI---ELN 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1812588810 403 DRPGNYVE-----PTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFA 446
Cdd:cd07133 309 PAGEDFAAtrklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAID 357
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
191-520 |
2.64e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 87.84 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 191 ITAFNFPVavYG-WNNA-IAMICGNVCLWKGAPTTSLISvavTKIIAKVLEDNKLPGAICSLTCGGAdiGTAMAKDERVN 268
Cdd:PRK11903 155 INAFNFPA--WGlWEKAaPALLAGVPVIVKPATATAWLT---QRMVKDVVAAGILPAGALSVVCGSS--AGLLDHLQPFD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 269 LLSFTGSTQVGKQVGLM--VQERFGRSLLELGGNNAIIAFEDADLSlvvpSALFAAVG---------TAGQRCTTARRLF 337
Cdd:PRK11903 228 VVSFTGSAETAAVLRSHpaVVQRSVRVNVEADSLNSALLGPDAAPG----SEAFDLFVkevvremtvKSGQKCTAIRRIF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 338 IHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTK-QAVSMFLGAveEAKKEGGTVVYGGKV---MDRP---GNYVE 410
Cdd:PRK11903 304 VPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRaQLAAVRAGL--AALRAQAEVLFDGGGfalVDADpavAACVG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 411 PTI-VTGLGHDASIAH-TETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKD---LGRIFRWLGPKGsdcGIVNVNI 485
Cdd:PRK11903 382 PTLlGASDPDAATAVHdVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDaafLAAAALELADSH---GRVHVIS 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1812588810 486 PTSGAEIGG--------AFGGEKHTGGGRE-SGSDAWKQYMRRS 520
Cdd:PRK11903 459 PDVAALHTGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRS 502
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
184-509 |
4.25e-16 |
|
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: 80.53 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPVA-----VYGwnnAIAmiCGNVCLWKgaptTSLISVAVTKIIAKVLEDNKLPGAIcSLTCGGADIG 258
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG---AIA--AGNAVVLK----PSELAPATSALLAKLIPEYLDTKAI-KVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 259 TAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGT-AGQRCTTARRLF 337
Cdd:cd07137 171 TALL-EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 338 IHESIHDEVV----NRLKKAYAQirvgNPWDPNVLYGPLHTK--QAVSMFLGAVEEAKKeggtVVYGGKVmDRPGNYVEP 411
Cdd:cd07137 250 VEESFAPTLIdalkNTLEKFFGE----NPKESKDLSRIVNSHhfQRLSRLLDDPSVADK----IVHGGER-DEKNLYIEP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 412 TIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFT--KDLGRIFRWLGPKGS----DCgIVNVNI 485
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTknKELKRRIVAETSSGGvtfnDT-VVQYAI 399
|
330 340
....*....|....*....|....
gi 1812588810 486 PTSgaeiggAFGGEKHTGGGRESG 509
Cdd:cd07137 400 DTL------PFGGVGESGFGAYHG 417
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
184-509 |
6.41e-14 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 73.93 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKgaptTSLISVAVTKIIAKVLEDNKLPGAICSLTcgGADIGTAMAK 263
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLK----PSELAPASSALLAKLLEQYLDSSAVRVVE--GAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 264 DERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVG-TAGQRCTTARRLFIHESI 342
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 343 HDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSmfLGAVEEAKKEGGTVVYGGKvMDRPGNYVEPTIVTGLGHDAS 422
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDR--LSKLLDEKEVSDKIVYGGE-KDRENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 423 IAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDlGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHT 502
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHN-KKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGES 421
|
....*..
gi 1812588810 503 GGGRESG 509
Cdd:PLN02174 422 GMGAYHG 428
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
184-520 |
1.55e-12 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 69.76 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPV--AVYGWNNAIAmiCGNVCLWKG---APTTSLIsvaVTKIIAKVLeDNKlpgAIcSLTCGGADIG 258
Cdd:PLN02203 108 PLGVVLIFSSWNFPIglSLEPLIGAIA--AGNAVVLKPselAPATSAF---LAANIPKYL-DSK---AV-KVIEGGPAVG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 259 TAMAkDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNN-AIIAFEDA--DLSLVVPSALFAAVGT-AGQRCTTAR 334
Cdd:PLN02203 178 EQLL-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCpCIVDSLSSsrDTKVAVNRIVGGKWGScAGQACIAID 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 335 RLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTK--QAVSMFLgaveEAKKEGGTVVYGGKvMDRPGNYVEPT 412
Cdd:PLN02203 257 YVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKhfQRLSNLL----KDPRVAASIVHGGS-IDEKKLFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 413 IVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEi 492
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACD- 410
|
330 340 350
....*....|....*....|....*....|....
gi 1812588810 493 GGAFGGEKHTGGGRESGSDAW------KQYMRRS 520
Cdd:PLN02203 411 SLPFGGVGESGFGRYHGKYSFdtfsheKAVLRRS 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
56-443 |
9.27e-11 |
|
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: 64.05 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 56 NGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWK--IWADIPAPKR----GEIVRQIGDALReKIQV-- 127
Cdd:cd07126 4 AGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKsgLHNPLKNPERyllyGDVSHRVAHELR-KPEVed 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 128 -LGSLVSLEMGKILVEGVGEV---QEYV-----DICDYavgLSR--MIGGPILPSERSGHalieQWnPVGLVGIITAFNF 196
Cdd:cd07126 83 fFARLIQRVAPKSDAQALGEVvvtRKFLenfagDQVRF---LARsfNVPGDHQGQQSSGY----RW-PYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 197 PVAVYGWNNAIAMICGNVCLWKGaptTSLISVAVTKIIaKVLEDNKLPGAICSLT-CGGADIGTAMaKDERVNLLSFTGS 275
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKV---DSKVSVVMEQFL-RLLHLCGMPATDVDLIhSDGPTMNKIL-LEANPRMTLFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 276 TQVGKQVGLMVQerfGRSLLELGGNNAIIAFED-ADLSLVVPSALFAAVGTAGQRCTTARRLFIHES-IHDEVVNRLKKA 353
Cdd:cd07126 230 SKVAERLALELH---GKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 354 YAQIRVgnpwdPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVM---DRPGNY--VEPTIV------TGLGHDAS 422
Cdd:cd07126 307 AEQRKL-----EDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPLtnhSIPSIYgaYEPTAVfvpleeIAIEENFE 381
|
410 420
....*....|....*....|.
gi 1812588810 423 IAHTETFAPILYVFKFKNEEE 443
Cdd:cd07126 382 LVTTEVFGPFQVVTEYKDEQL 402
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
184-459 |
6.40e-07 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 51.77 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPVA--VYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSL-TCGGADIGTA 260
Cdd:cd07129 105 PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLlQGGGREVGVA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 261 MAKDERVNLLSFTGSTQVGKQVGLMVQER------FGrsllELGGNNAIIafedadlslVVPSAL----------FAA-- 322
Cdd:cd07129 185 LVKHPAIKAVGFTGSRRGGRALFDAAAARpepipfYA----ELGSVNPVF---------ILPGALaergeaiaqgFVGsl 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 323 VGTAGQRCTTARRLFIHESIH-DEVVNRLKKAYAQirvgnpWDPnvlyGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKV 401
Cdd:cd07129 252 TLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAA------APA----QTMLTPGIAEAYRQGVEALAAAPGVRVLAGGA 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812588810 402 MDRPGNYVEPTI--VTG---LGHDAsiAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSI 459
Cdd:cd07129 322 AAEGGNQAAPTLfkVDAaafLADPA--LQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATI 382
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
89-493 |
3.34e-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: 43.02 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 89 EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGvgEVQEYVDICDYAVGLSRMIGGPI 168
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVED--KVIKNHFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 169 LPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAIC 248
Cdd:cd07081 80 VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 249 SlTCGGADIGTAMA--KDERVNLLSFTGSTQVGKQVglmvqERFGRSLLELG-GNNAIIAFEDADLSLVVPSALFAAVGT 325
Cdd:cd07081 160 G-WIDNPSIELAQRlmKFPGIGLLLATGGPAVVKAA-----YSSGKPAIGVGaGNTPVVIDETADIKRAVQSIVKSKTFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 326 AGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNpwdpnvlygPLHTKQAVSMFLGAVEEA--KKEGGTV--VYGGKV 401
Cdd:cd07081 234 NGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAE---------ELQQVQPVILKNGDVNRDivGQDAYKIaaAAGLKV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 402 mdrPGN----YVEptiVTGLGHDASIAHtETFAPILYVFKFKNEEEVFAWNNEVKQ----GLSSSIFTKDLGRIFR--WL 471
Cdd:cd07081 305 ---PQEtrilIGE---VTSLAEHEPFAH-EKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIKAIENmnQF 377
|
410 420
....*....|....*....|..
gi 1812588810 472 GPKgSDCGIVNVNIPTSGAEIG 493
Cdd:cd07081 378 ANA-MKTSRFVKNGPCSQGGLG 398
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
184-437 |
3.64e-04 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 43.24 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 184 PVGLVGIITAFNFPVavygWNNAIAMIC----GNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCG--GADI 257
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGYPGLFAslatGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAADtpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 258 GTAMAKDERVNLLSFTGSTQVGKQvgLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLF 337
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDW--LEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588810 338 I----------HESiHDEVVNRLKKAYAQIrVGNPWDPNVLYGPLHTkQAVsmfLGAVEEAKKEGGTVVYGGKVM--DRP 405
Cdd:cd07127 347 VprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQS-PDT---LARIAEARQLGEVLLASEAVAhpEFP 420
|
250 260 270
....*....|....*....|....*....|...
gi 1812588810 406 GNYVE-PTIVTGLGHDASIAHTETFAPILYVFK 437
Cdd:cd07127 421 DARVRtPLLLKLDASDEAAYAEERFGPIAFVVA 453
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