|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
1-426 |
0e+00 |
|
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: 634.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 1 MNHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKP 80
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 81 QHIKTKWTESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP--IYKN 158
Cdd:cd07100 81 EPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELF--REAGFPegVFQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 159 LSLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSC 238
Cdd:cd07100 159 LLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 239 IAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGAFYK 315
Cdd:cd07100 239 IAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRpdgPGAFYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 316 PTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPH 395
Cdd:cd07100 319 PTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPR 398
|
410 420 430
....*....|....*....|....*....|.
gi 1242547020 396 LPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07100 399 LPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
4-426 |
2.74e-142 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 413.75 E-value: 2.74e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 4 IIENIQQSYLLWKEY---SVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKP 80
Cdd:PRK09406 25 VDAAIARAHARFRDYrttTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALLAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 81 QHI---KTKWTESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP--I 155
Cdd:PRK09406 105 EPAdaaAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLF--RRAGFPdgC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 156 YKNLSLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAG 235
Cdd:PRK09406 183 FQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 236 QSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGA 312
Cdd:PRK09406 263 QSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRpdgPGW 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 313 FYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQTYRF----EEGAVYINE 388
Cdd:PRK09406 343 FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE----AEQERFiddlEAGQVFING 418
|
410 420 430
....*....|....*....|....*....|....*...
gi 1242547020 389 MLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:PRK09406 419 MTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
15-424 |
4.42e-132 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 388.07 E-value: 4.42e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWTESYITF 94
Cdd:PRK13968 45 WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVADIIAHKH 174
Cdd:PRK13968 125 RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 175 IKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKF 254
Cdd:PRK13968 205 IAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 255 LSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGAFYKPTILSEVTPQMPVFRE 331
Cdd:PRK13968 285 TERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKiagAGNYYAPTVLANVTPEMTAFRE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 332 ETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSGYGRELS 411
Cdd:PRK13968 365 ELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELS 444
|
410
....*....|...
gi 1242547020 412 QFGMYEFANIKTV 424
Cdd:PRK13968 445 HFGLHEFCNIQTV 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
15-426 |
4.09e-129 |
|
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: 379.24 E-value: 4.09e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQH-IKTKWTESYIT 93
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIpSPDPGELAIVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 94 FEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP--IYKNLSLESKFVAD-II 170
Cdd:cd07078 94 REPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELL--AEAGLPpgVLNVVTGDGDEVGAaLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 171 AHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSL 250
Cdd:cd07078 172 SHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 251 KEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKRE----GAFYKPTILSEVTPQM 326
Cdd:cd07078 252 YDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeggkGYFVPPTVLTDVDPDM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 327 PVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLIS-DPHLPFGGVKNSG 405
Cdd:cd07078 332 PIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEPSAPFGGVKQSG 411
|
410 420
....*....|....*....|.
gi 1242547020 406 YGRELSQFGMYEFANIKTVVI 426
Cdd:cd07078 412 IGREGGPYGLEEYTEPKTVTI 432
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
15-427 |
2.07e-125 |
|
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: 371.38 E-value: 2.07e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQ-HIKTKWTESYIT 93
Cdd:COG1012 59 WAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETiPSDAPGTRAYVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 94 FEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP---IykNL--SLESKFVAD 168
Cdd:COG1012 139 REPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELL--EEAGLPagvL--NVvtGDGSEVGAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHK 248
Cdd:COG1012 215 LVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHE 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 249 SLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR----EGAFYKPTILSEVTP 324
Cdd:COG1012 295 SIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRpdgeGGYFVEPTVLADVTP 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 325 QMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLIS-DPHLPFGGVKN 403
Cdd:COG1012 375 DMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQ 454
|
410 420
....*....|....*....|....
gi 1242547020 404 SGYGRELSQFGMYEFANIKTVVIK 427
Cdd:COG1012 455 SGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
2-424 |
2.86e-123 |
|
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: 365.32 E-value: 2.86e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 2 NHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENfLKPQ 81
Cdd:pfam00171 32 DAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARR-LDGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 82 HIKTKWTE-SYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFPiyKNL- 159
Cdd:pfam00171 111 TLPSDPGRlAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELF--EEAGLP--AGVl 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 160 ----SLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAG 235
Cdd:pfam00171 187 nvvtGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 236 QSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGK---REGA 312
Cdd:pfam00171 267 QVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEaglDNGY 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 313 FYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVE----FIKsqtyRFEEGAVYINE 388
Cdd:pfam00171 347 FVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLEralrVAR----RLEAGMVWIND 422
|
410 420 430
....*....|....*....|....*....|....*..
gi 1242547020 389 MLISDP-HLPFGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:pfam00171 423 YTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
5-426 |
2.18e-116 |
|
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: 347.50 E-value: 2.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENF---LKPQ 81
Cdd:cd07103 25 IDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARRIygrTIPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 82 HIKTKWTesYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNskKLKFP------I 155
Cdd:cd07103 105 PAPGKRI--LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAE--EAGLPagvlnvV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 156 YknlSLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAG 235
Cdd:cd07103 181 T---GSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 236 QSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGA 312
Cdd:cd07103 258 QTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRlglGGY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 313 FYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLIS 392
Cdd:cd07103 338 FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLIS 417
|
410 420 430
....*....|....*....|....*....|....
gi 1242547020 393 DPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07103 418 DAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
15-426 |
2.86e-98 |
|
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: 298.37 E-value: 2.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHI-KTKWTESYIT 93
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPsPDPGGEAYVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 94 FEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFPiyKNL-----SLESKFVAD 168
Cdd:cd06534 90 REPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELL--QEAGLP--PGVvnvvpGGGDEVGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHK 248
Cdd:cd06534 166 LLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 249 SLKEKFlstfkskvealkrgdkfnaeteiaemaredlaieLEKLVnesislgakvicggkregafykpTILSEVTPQMPV 328
Cdd:cd06534 246 SIYDEF----------------------------------VEKLV-----------------------TVLVDVDPDMPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 329 FREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLI-SDPHLPFGGVKNSGYG 407
Cdd:cd06534 269 AQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKNSGIG 348
|
410
....*....|....*....
gi 1242547020 408 RELSQFGMYEFANIKTVVI 426
Cdd:cd06534 349 REGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
19-426 |
2.96e-98 |
|
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: 301.05 E-value: 2.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 19 SVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENfLKPQHIKTKWTES------YI 92
Cdd:cd07149 41 PAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKR-LAGETIPFDASPGgegrigFT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 93 TFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLkfpIYKNLSL---ESKFVAD- 168
Cdd:cd07149 120 IREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGL---PKGALNVvtgSGETVGDa 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 IIAHKHIKGVSLTGSEKAGKAVAQCAGqhLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHK 248
Cdd:cd07149 197 LVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 249 SLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGAFYKPTILSEVTPQMPV 328
Cdd:cd07149 275 DIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKRDGAILEPTVLTDVPPDMKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 329 FREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEmlISD---PHLPFGGVKNSG 405
Cdd:cd07149 355 VCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIND--SSTfrvDHMPYGGVKESG 432
|
410 420
....*....|....*....|.
gi 1242547020 406 YGRELSQFGMYEFANIKTVVI 426
Cdd:cd07149 433 TGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
5-426 |
2.89e-97 |
|
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: 299.18 E-value: 2.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENA--------EN 76
Cdd:cd07088 41 VDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWArriegeiiPS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 77 FLKPQHIktkwtesYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIY 156
Cdd:cd07088 121 DRPNENI-------FIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 157 KNLSLESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAG 235
Cdd:cd07088 194 NIVTGRGSVVGDaLVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 236 QSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETE----IAEMAREdlaiELEKLVNESISLGAKVICGGKR-- 309
Cdd:cd07088 274 QVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDmgplVNEAALD----KVEEMVERAVEAGATLLTGGKRpe 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 --EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYIN 387
Cdd:cd07088 350 geKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1242547020 388 eMLISDPHLPF-GGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07088 430 -RENFEAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
3-426 |
2.21e-95 |
|
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: 293.87 E-value: 2.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 3 HIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENA-----ENF 77
Cdd:cd07145 25 EAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAkvlrgETI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 78 LKPQHIKTKWTESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYK 157
Cdd:cd07145 105 PVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVIN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 158 NLSLESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:cd07145 185 VVTGYGSEVGDeIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR-EGAFYK 315
Cdd:cd07145 265 VCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKRdEGSFFP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 316 PTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINE--MLISD 393
Cdd:cd07145 345 PTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDstRFRWD 424
|
410 420 430
....*....|....*....|....*....|...
gi 1242547020 394 pHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07145 425 -NLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
15-426 |
9.79e-94 |
|
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: 289.51 E-value: 9.79e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIKT----KWTES 90
Cdd:cd07099 34 WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVLAPRKVPTgllmPNKKA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 91 YITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVADII 170
Cdd:cd07099 114 TVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 171 AHKHIKgVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSL 250
Cdd:cd07099 194 DAGVDK-VAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 251 KEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKRE---GAFYKPTILSEVTPQMP 327
Cdd:cd07099 273 YDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSnggGPFYEPTVLTDVPHDMD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 328 VFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEML--ISDPHLPFGGVKNSG 405
Cdd:cd07099 353 VMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLltAGIPALPFGGVKDSG 432
|
410 420
....*....|....*....|.
gi 1242547020 406 YGRELSQFGMYEFANIKTVVI 426
Cdd:cd07099 433 GGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
88-418 |
1.85e-93 |
|
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: 287.89 E-value: 1.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 88 TESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLL-ESIFNSKKLKFPIYKNLSLESKFV 166
Cdd:cd07104 90 KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEAGLPKGVLNVVPGGGSEI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 167 AD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFL 245
Cdd:cd07104 170 GDaLVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRIL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 246 VHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGAFYKPTILSEVTPQ 325
Cdd:cd07104 250 VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEGLFYQPTVLSDVTPD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 326 MPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISD-PHLPFGGVKNS 404
Cdd:cd07104 330 MPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDePHVPFGGVKAS 409
|
330
....*....|....
gi 1242547020 405 GYGRELSQFGMYEF 418
Cdd:cd07104 410 GGGRFGGPASLEEF 423
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
5-426 |
1.13e-91 |
|
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: 284.22 E-value: 1.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKcaylcdyyienAENFLK----- 79
Cdd:cd07150 27 IAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF-----------TPELLRaaage 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 80 PQHIK-------TKWTESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLK 152
Cdd:cd07150 96 CRRVRgetlpsdSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 153 FPIYKNLSLESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARM 231
Cdd:cd07150 176 KGVFNVVTGGGAEVGDeLVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 232 QNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREG 311
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGGKYDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 312 AFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLI 391
Cdd:cd07150 336 NFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTI 415
|
410 420 430
....*....|....*....|....*....|....*.
gi 1242547020 392 SD-PHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07150 416 LDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-424 |
3.41e-91 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 284.28 E-value: 3.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAEN---FLKPQ 81
Cdd:PLN02278 68 IASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRvygDIIPS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 82 HIKTKwtESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSA----NL-LESIFNSKKLKFPIY 156
Cdd:PLN02278 148 PFPDR--RLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTAlaaaELaLQAGIPPGVLNVVMG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 157 KNLSLESKFVADIIAHKhikgVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:PLN02278 226 DAPEIGDALLASPKVRK----ITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQ 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKRE---GAF 313
Cdd:PLN02278 302 TCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHslgGTF 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 314 YKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQTYRFEE----GAVYINEM 389
Cdd:PLN02278 382 YEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDL----QRAWRVSEaleyGIVGVNEG 457
|
410 420 430
....*....|....*....|....*....|....*
gi 1242547020 390 LISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:PLN02278 458 LISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
22-426 |
4.57e-91 |
|
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: 282.71 E-value: 4.57e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 22 QRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENF------------LKPQHIKTKWte 89
Cdd:cd07146 41 QRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDdgesfscdltanGKARKIFTLR-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 90 syitfEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVAD- 168
Cdd:cd07146 119 -----EPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDe 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 IIAHKHIKGVSLTGSEKAGKAVAQCAGqhLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHK 248
Cdd:cd07146 194 LITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 249 SLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGAFYKPTILSEVTPQMPV 328
Cdd:cd07146 272 SVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQRQGALYAPTVLDHVPPDAEL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 329 FREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEML-ISDPHLPFGGVKNSGYG 407
Cdd:cd07146 352 VTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPgFRSELSPFGGVKDSGLG 431
|
410 420
....*....|....*....|
gi 1242547020 408 -RELSQFGMYEFANIKTVVI 426
Cdd:cd07146 432 gKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
15-426 |
1.13e-90 |
|
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: 281.63 E-value: 1.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCA---YLCDYYIENAENFLKPQHIKTKWTESY 91
Cdd:cd07094 37 RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIdtlRLAAEEAERIRGEEIPLDATQGSDNRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 92 ITF--EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVAD- 168
Cdd:cd07094 117 AWTirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDa 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 IIAHKHIKGVSLTGSEKAGKAVAQCAGqhLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHK 248
Cdd:cd07094 197 FAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 249 SLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGAFYKPTILSEVTPQMPV 328
Cdd:cd07094 275 ELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGERDGALFKPTVLEDVPRDTKL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 329 FREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISD-PHLPFGGVKNSGYG 407
Cdd:cd07094 355 STEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRtDWMPFGGVKESGVG 434
|
410
....*....|....*....
gi 1242547020 408 RELSQFGMYEFANIKTVVI 426
Cdd:cd07094 435 REGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
15-426 |
1.50e-90 |
|
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: 281.53 E-value: 1.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFlkpqHiktkwTESYITF 94
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTL----H-----GDSYNNL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 ----------EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESK 164
Cdd:cd07118 108 gddmlglvlrEPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 165 FVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKR 243
Cdd:cd07118 188 TVGQaMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 244 FLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR----EGAFYKPTIL 319
Cdd:cd07118 268 LLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERlasaAGLFYQPTIF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 320 SEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFG 399
Cdd:cd07118 348 TDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFG 427
|
410 420
....*....|....*....|....*..
gi 1242547020 400 GVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07118 428 GFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
15-414 |
1.73e-90 |
|
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: 281.06 E-value: 1.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQ-HIKTKWTESYIT 93
Cdd:cd07102 34 WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIrVPEKDGFERYIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 94 FEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVADIIAHK 173
Cdd:cd07102 114 REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 174 HIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEK 253
Cdd:cd07102 194 RIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 254 FLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKRE------GAFYKPTILSEVTPQMP 327
Cdd:cd07102 274 FVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFpedkagGAYLAPTVLTNVDHSMR 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 328 VFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSGYG 407
Cdd:cd07102 354 VMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRG 433
|
....*..
gi 1242547020 408 RELSQFG 414
Cdd:cd07102 434 VTLSRLG 440
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
22-426 |
1.10e-87 |
|
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: 273.74 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 22 QRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFlKPQHIKTKWTESYITFE------ 95
Cdd:cd07147 44 RRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRI-YGEVLPLDISARGEGRQglvrrf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 96 PIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKL---KFPIyknLSLESKFVADIIAH 172
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLpkgAFSV---LPCSRDDADLLVTD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 173 KHIKGVSLTGSEKAGKAVAQCAGQhlKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKE 252
Cdd:cd07147 200 ERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 253 KFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGAFYKPTILSEVTPQMPVFREE 332
Cdd:cd07147 278 EFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKRDGALLEPTILEDVPPDMEVNCEE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 333 TFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMlisdP-----HLPFGGVKNSGYG 407
Cdd:cd07147 358 VFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDV----PtfrvdHMPYGGVKDSGIG 433
|
410
....*....|....*....
gi 1242547020 408 RELSQFGMYEFANIKTVVI 426
Cdd:cd07147 434 REGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
15-425 |
8.18e-86 |
|
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: 269.55 E-value: 8.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKP-ISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWTESY-- 91
Cdd:cd07098 34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYkr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 92 --ITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSkklkfpIYKNLSLESKFV--- 166
Cdd:cd07098 114 arVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRE------CLAACGHDPDLVqlv 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 167 ------AD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCI 239
Cdd:cd07098 188 tclpetAEaLTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 240 AAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR-------EGA 312
Cdd:cd07098 268 GIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRyphpeypQGH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 313 FYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEM--- 389
Cdd:cd07098 348 YFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvn 427
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1242547020 390 -LISDphLPFGGVKNSGYGRelsqFGMYE----FANIKTVV 425
Cdd:cd07098 428 yYVQQ--LPFGGVKGSGFGR----FAGEEglrgLCNPKSVT 462
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
95-426 |
6.16e-84 |
|
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: 263.67 E-value: 6.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNskKLKFP----IYKNLSLES--KFVAD 168
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFH--EAGLPkgvlNVVTHSPEDapEVVEA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHK 248
Cdd:cd07105 175 LIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 249 SLKEKFLSTFKSKVEALKRGDkfnaeTEIAEMAREDLAIELEKLVNESISLGAKVICGGKRE----GAFYKPTILSEVTP 324
Cdd:cd07105 255 SIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADespsGTSMPPTILDNVTP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 325 QMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISD-PHLPFGGVKN 403
Cdd:cd07105 330 DMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDePTLPHGGVKS 409
|
330 340
....*....|....*....|...
gi 1242547020 404 SGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07105 410 SGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
15-426 |
7.42e-83 |
|
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: 261.72 E-value: 7.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVqkcAYLCDYYIENA------ENFLKPqhIKTKWT 88
Cdd:cd07114 37 WRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV---RYLAEWYRYYAgladkiEGAVIP--VDKGDY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 89 ESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFPiyknlslesKFVAD 168
Cdd:cd07114 112 LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLA--EEAGFP---------PGVVN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 II------------AHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:cd07114 181 VVtgfgpetgealvEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR------- 309
Cdd:cd07114 261 TCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERpsgadlg 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQTYRF----EEGAVY 385
Cdd:cd07114 341 AGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL----ARAHRVaraiEAGTVW 416
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1242547020 386 INEMLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07114 417 VNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
15-424 |
1.06e-82 |
|
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: 260.92 E-value: 1.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYienAENFLKPQHIK---TKWTEsy 91
Cdd:cd07106 35 WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYT---ASLDLPDEVIEdddTRRVE-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 92 ITFEPIGVLLGVMPWNFPF----WQVfrfvIPNLILGNLFIVKHASNVPKSANLLESIFNSKklkFP--IYKNLSLESKF 165
Cdd:cd07106 110 LRRKPLGVVAAIVPWNFPLllaaWKI----APALLAGNTVVLKPSPFTPLCTLKLGELAQEV---LPpgVLNVVSGGDEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 166 VADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANL-ELATSIAVNArMQNAGQSCIAAKRF 244
Cdd:cd07106 183 GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIdAVAPKLFWGA-FINSGQVCAAIKRL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 245 LVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIA----EMAREdlaiELEKLVNESISLGAKVICGGKRE---GAFYKPT 317
Cdd:cd07106 262 YVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGpvqnKMQYD----KVKELVEDAKAKGAKVLAGGEPLdgpGYFIPPT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 318 ILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLP 397
Cdd:cd07106 338 IVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAP 417
|
410 420
....*....|....*....|....*..
gi 1242547020 398 FGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:cd07106 418 FGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
15-424 |
3.16e-82 |
|
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: 260.26 E-value: 3.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENflkpQHIKT-----KWTE 89
Cdd:cd07097 53 WRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALR----LSGETlpstrPGVE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 90 SYITFEPIGVLLGVMPWNFPF----WQvfrfVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYkNLSLES-K 164
Cdd:cd07097 129 VETTREPLGVVGLITPWNFPIaipaWK----IAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVF-NLVMGSgS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 165 FVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKR 243
Cdd:cd07097 204 EVGQaLVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 244 FLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDlaiELEKlVNESISL----GAKVICGGKR-----EGAFY 314
Cdd:cd07097 284 LIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSER---QLEK-DLRYIEIarseGAKLVYGGERlkrpdEGYYL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 315 KPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLIS-D 393
Cdd:cd07097 360 APALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvD 439
|
410 420 430
....*....|....*....|....*....|..
gi 1242547020 394 PHLPFGGVKNSGYG-RELSQFGMYEFANIKTV 424
Cdd:cd07097 440 YHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
15-409 |
8.94e-82 |
|
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: 259.43 E-value: 8.94e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAEN----FLK-PQHIKTKWTE 89
Cdd:cd07082 55 WPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRldgdSLPgDWFPGTKGKI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 90 SYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP--IYKNLSLESKFVA 167
Cdd:cd07082 135 AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAF--HDAGFPkgVVNVVTGRGREIG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 168 D-IIAHKHIKGVSLTGSEKAGKAVAQCAGqhLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLV 246
Cdd:cd07082 213 DpLVTHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 247 HKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKRE-GAFYKPTILSEVTPQ 325
Cdd:cd07082 291 HESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREgGNLIYPTLLDPVTPD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 326 MPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDP-HLPFGGVKNS 404
Cdd:cd07082 371 MRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPdHFPFLGRKDS 450
|
....*
gi 1242547020 405 GYGRE 409
Cdd:cd07082 451 GIGTQ 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-425 |
9.91e-81 |
|
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: 256.28 E-value: 9.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSiAEVQkcAYLC----DYYIENAENFlkpqhiktKWTE- 89
Cdd:cd07138 52 WSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLA-RAAQ--VGLGighlRAAADALKDF--------EFEEr 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 90 ---SYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNskKLKFP--IYkNLSLESK 164
Cdd:cd07138 121 rgnSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILD--EAGLPagVF-NLVNGDG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 165 FV--ADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAK 242
Cdd:cd07138 198 PVvgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 243 RFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMARedlAIELEK---LVNESISLGAKVICGGK------REGAF 313
Cdd:cd07138 278 RMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLAS---AAQFDRvqgYIQKGIEEGARLVAGGPgrpeglERGYF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 314 YKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINeMLISD 393
Cdd:cd07138 355 VKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFN 433
|
410 420 430
....*....|....*....|....*....|..
gi 1242547020 394 PHLPFGGVKNSGYGRELSQFGMYEFANIKTVV 425
Cdd:cd07138 434 PGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-425 |
8.61e-80 |
|
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: 254.19 E-value: 8.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 2 NHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENF---L 78
Cdd:cd07131 40 DAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLfgeT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 79 KPQHIKTKwtESYITFEPIGVLLGVMPWNFPF----WQVFrfviPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKfP 154
Cdd:cd07131 120 VPSELPNK--DAMTRRQPIGVVALITPWNFPVaipsWKIF----PALVCGNTVVFKPAEDTPACALKLVELFAEAGLP-P 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 155 IYKNLSL---ESKFVAdIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARM 231
Cdd:cd07131 193 GVVNVVHgrgEEVGEA-LVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 232 QNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR-- 309
Cdd:cd07131 272 GTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERlt 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 -----EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAV 384
Cdd:cd07131 352 gggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGIT 431
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1242547020 385 YINEMLI-SDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVV 425
Cdd:cd07131 432 YVNAPTIgAEVHLPFGGVKKSGNGHREAGTTALDAFTEWKAV 473
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
79-427 |
1.68e-79 |
|
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: 253.00 E-value: 1.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 79 KPQHIKTKwtESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLL-ESIFNSKKLKFPIYK 157
Cdd:cd07151 115 LPSDVPGK--ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLlAKIFEEAGLPKGVLN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 158 NLSLESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:cd07151 193 VVVGAGSEIGDaFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQ 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGAFYKP 316
Cdd:cd07151 273 ICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGNVLEP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 317 TILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISD-PH 395
Cdd:cd07151 353 TVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePH 432
|
330 340 350
....*....|....*....|....*....|..
gi 1242547020 396 LPFGGVKNSGYGRELSQFGMYEFANIKTVVIK 427
Cdd:cd07151 433 VPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-426 |
7.93e-79 |
|
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: 251.73 E-value: 7.93e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQS-IAEVQKCAYLCDYYIENAENFLKPQHIKTKWT-ESYI 92
Cdd:cd07139 54 WPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSrRAQGPGPAALLRYYAALARDFPFEERRPGSGGgHVLV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 93 TFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLL----------ESIFN--------SKKLkfp 154
Cdd:cd07139 134 RREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLaeaaeeaglpPGVVNvvpadrevGEYL--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 155 iyknlsleskfvadiIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNA 234
Cdd:cd07139 211 ---------------VRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 235 GQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR----- 309
Cdd:cd07139 276 GQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpagld 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINeM 389
Cdd:cd07139 356 RGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-G 434
|
410 420 430
....*....|....*....|....*....|....*..
gi 1242547020 390 LISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07139 435 FRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
15-426 |
4.51e-78 |
|
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: 249.07 E-value: 4.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENF------LKPQHIktkwt 88
Cdd:cd07109 36 WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKLhgetipLGPGYF----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 89 eSYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP-----IYKNLSLES 163
Cdd:cd07109 111 -VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELA--EEAGLPagalnVVTGLGAEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 164 KfvADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKR 243
Cdd:cd07109 188 G--AALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 244 FLVHKSLKEKFLSTFKSKVEALKRGdkfnaeteiAEMAREDL-----AIELEK---LVNESISLGAKVICGGKR------ 309
Cdd:cd07109 266 LLVHRSIYDEVLERLVERFRALRVG---------PGLEDPDLgplisAKQLDRvegFVARARARGARIVAGGRIaegapa 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQTYRFEE----GAVY 385
Cdd:cd07109 337 GGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG----DRALRVARrlraGQVF 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1242547020 386 INEML----ISdphLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07109 413 VNNYGagggIE---LPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
2-409 |
4.72e-78 |
|
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: 249.79 E-value: 4.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 2 NHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDY----------YI 71
Cdd:cd07086 38 EAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYavglsrmlygLT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 72 ENAEnflKPQH-IKTKWtesyitfEPIGVLLGVMPWNFPF----WQVFrfviPNLILGNLFIVKHASNVPKSANLLESIF 146
Cdd:cd07086 118 IPSE---RPGHrLMEQW-------NPLGVVGVITAFNFPVavpgWNAA----IALVCGNTVVWKPSETTPLTAIAVTKIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 147 NS--KKLKFP--IYkNLSLESKFVADIIAH-KHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLEL 221
Cdd:cd07086 184 AEvlEKNGLPpgVV-NLVTGGGDGGELLVHdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 222 ATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDlAIEL-EKLVNESISLG 300
Cdd:cd07086 263 AVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQA-AVEKyLNAIEIAKSQG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 301 AKVICGGKR-----EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQ 375
Cdd:cd07086 342 GTVLTGGKRidggePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDL----RE 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1242547020 376 TYRF------EEGAVYIN------EMlisdpHLPFGGVKNSGYGRE 409
Cdd:cd07086 418 AFRWlgpkgsDCGIVNVNiptsgaEI-----GGAFGGEKETGGGRE 458
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
15-426 |
3.30e-77 |
|
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: 247.61 E-value: 3.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWTESYITF 94
Cdd:cd07119 53 WPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFPI-YKNLSLESKFV--ADIIA 171
Cdd:cd07119 133 EPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELI--EEAGLPAgVVNLVTGSGATvgAELAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 172 HKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLK 251
Cdd:cd07119 211 SPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIH 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 252 EKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR-------EGAFYKPTILSEVTP 324
Cdd:cd07119 291 DKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRptgdelaKGYFVEPTIFDDVDR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 325 QMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNS 404
Cdd:cd07119 371 TMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQS 450
|
410 420
....*....|....*....|..
gi 1242547020 405 GYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07119 451 GIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
15-426 |
1.15e-76 |
|
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: 245.97 E-value: 1.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQS----IAEVQKC----AYLCDYY----IENAENFLkpqh 82
Cdd:cd07091 59 WRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESakgdVALSIKClryyAGWADKIqgktIPIDGNFL---- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 83 iktkwteSYITFEPIGVLLGVMPWNFPFwQVFRFVI-PNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP--IYKNL 159
Cdd:cd07091 135 -------AYTRREPIGVCGQIIPWNFPL-LMLAWKLaPALAAGNTVVLKPAEQTPLSALYLAELI--KEAGFPpgVVNIV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 160 SLESKFVADIIA-HKHIKGVSLTGSEKAGKAVAQCAGQ-HLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQS 237
Cdd:cd07091 205 PGFGPTAGAAISsHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQC 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 238 CIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETE----IAEMAREDLAIELEKLVNEsislGAKVICGGKR---E 310
Cdd:cd07091 285 CCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFqgpqVSKAQFDKILSYIESGKKE----GATLLTGGERhgsK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 311 GAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEfiKSQTY--RFEEGAVYINE 388
Cdd:cd07091 361 GYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDIN--KALRVsrALKAGTVWVNT 438
|
410 420 430
....*....|....*....|....*....|....*...
gi 1242547020 389 MLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07091 439 YNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
15-425 |
5.48e-75 |
|
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: 241.63 E-value: 5.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQS-IAEVQKCAYLCDYYIENAENFlkpqHIKTKWTE---- 89
Cdd:cd07142 59 WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKI----HGMTLPADgphh 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 90 SYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIyknLSLESKFV--- 166
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGV---LNIVTGFGpta 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 167 -ADIIAHKHIKGVSLTGSEKAGKAVAQCAGQ-HLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRF 244
Cdd:cd07142 212 gAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 245 LVHKSLKEKFLStfKSKVEALKR--GDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGAFYKPTIL 319
Cdd:cd07142 292 FVHESIYDEFVE--KAKARALKRvvGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRigsKGYYIQPTIF 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 320 SEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFG 399
Cdd:cd07142 370 SDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFG 449
|
410 420
....*....|....*....|....*.
gi 1242547020 400 GVKNSGYGRELSQFGMYEFANIKTVV 425
Cdd:cd07142 450 GYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
5-424 |
2.80e-74 |
|
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: 239.51 E-value: 2.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENfLKPQHIK 84
Cdd:cd07090 25 VKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPT-LSGEHVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 85 TKWTE-SYITFEPIGVLLGVMPWNFPF----WQVfrfvIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNL 159
Cdd:cd07090 104 LPGGSfAYTRREPLGVCAGIGAWNYPIqiasWKS----APALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 160 SLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCI 239
Cdd:cd07090 180 QGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 240 AAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR-------EGA 312
Cdd:cd07090 260 NGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERvvpedglENG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 313 FY-KPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLI 391
Cdd:cd07090 340 FYvSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNI 419
|
410 420 430
....*....|....*....|....*....|...
gi 1242547020 392 SDPHLPFGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:cd07090 420 SPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
22-426 |
4.34e-74 |
|
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: 239.07 E-value: 4.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 22 QRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISqsIAEVQKCAYLCD---YYIENAENFLKPQHI-----KTKWTESYIT 93
Cdd:cd07089 43 ERARCLRQLHEALEARKEELRALLVAEVGAPVM--TARAMQVDGPIGhlrYFADLADSFPWEFDLpvpalRGGPGRRVVR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 94 FEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVAD-IIAH 172
Cdd:cd07089 121 REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEaLTTD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 173 KHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKE 252
Cdd:cd07089 201 PRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 253 KFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR-----EGAFYKPTILSEVTPQMP 327
Cdd:cd07089 281 EVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGRpagldKGFYVEPTLFADVDNDMR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 328 VFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSGYG 407
Cdd:cd07089 361 IAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLG 440
|
410
....*....|....*....
gi 1242547020 408 RELSQFGMYEFANIKTVVI 426
Cdd:cd07089 441 RENGIEGLEEFLETKSIAY 459
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
15-426 |
1.61e-72 |
|
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: 235.38 E-value: 1.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQ-SIAEVQKCAYLCDYYIENAENFlKPQHIKTKWTE-SYI 92
Cdd:cd07144 62 WSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKI-QGKTIPTSPNKlAYT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 93 TFEPIGVLLGVMPWNFPF----WQVFrfviPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFPiyknlslesKFVAD 168
Cdd:cd07144 141 LHEPYGVCGQIIPWNYPLamaaWKLA----PALAAGNTVVIKPAENTPLSLLYFANLV--KEAGFP---------PGVVN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 II------------AHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:cd07144 206 IIpgygavagsalaEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKV-EALKRGDKFNAET----EIAEMAREDLA--IELEKLVNESISLGAKVICGGKR 309
Cdd:cd07144 286 NCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTvvgpQVSKTQYDRVLsyIEKGKKEGAKLVYGGEKAPEGLG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEM 389
Cdd:cd07144 366 KGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS 445
|
410 420 430
....*....|....*....|....*....|....*..
gi 1242547020 390 LISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07144 446 NDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
96-414 |
2.87e-72 |
|
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: 233.72 E-value: 2.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 96 PIGVLlGVM-PWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSAN-LLESIFNSKKLKFPIYKNLSLESKFVADIIAHK 173
Cdd:cd07152 110 PLGVV-GVIsPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGvVIARLFEEAGLPAGVLHVLPGGADAGEALVEDP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 174 HIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEK 253
Cdd:cd07152 189 NVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 254 FLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGAFYKPTILSEVTPQMPVFREET 333
Cdd:cd07152 269 YTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTYDGLFYRPTVLSGVKPGMPAFDEEI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 334 FGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISD-PHLPFGGVKNSGYGrelSQ 412
Cdd:cd07152 349 FGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDePHNPFGGMGASGNG---SR 425
|
..
gi 1242547020 413 FG 414
Cdd:cd07152 426 FG 427
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
15-426 |
8.41e-72 |
|
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: 232.84 E-value: 8.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIA-EVQKCAYLCDYY---IENAENFLKPQHIKTKwteS 90
Cdd:cd07093 35 WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFadyILQLDGESYPQDGGAL---N 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 91 YITFEPIGVLLGVMPWNFPF----WQVfrfvIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYkNLsleskfV 166
Cdd:cd07093 112 YVLRQPVGVAGLITPWNLPLmlltWKI----APALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVV-NV------V 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 167 --------ADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSC 238
Cdd:cd07093 181 hgfgpeagAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 239 IAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDlaiELEKlVNESISL----GAKVICGGKRE---- 310
Cdd:cd07093 261 LAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE---HLEK-VLGYVELaraeGATILTGGGRPelpd 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 311 ---GAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQTYRF----EEGA 383
Cdd:cd07093 337 legGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL----GRAHRVarrlEAGT 412
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1242547020 384 VYINEMLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07093 413 VWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
15-426 |
9.81e-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: 232.88 E-value: 9.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIA-EVQKCAYLCDYYIE-----------NAENFLkpqh 82
Cdd:cd07112 42 WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAvDVPSAANTFRWYAEaidkvygevapTGPDAL---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 83 iktkwteSYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKS----------ANLLESIFNSkklk 152
Cdd:cd07112 118 -------ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTalrlaelaleAGLPAGVLNV---- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 153 FPIY-----KNLSLeskfvadiiaHKHIKGVSLTGSEKAGKAVAQCAGQ-HLKKSVLELGGSAAFIICEDA-NLELATSI 225
Cdd:cd07112 187 VPGFghtagEALGL----------HMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 226 AVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVIC 305
Cdd:cd07112 257 AAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 306 GGKRE-----GAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFE 380
Cdd:cd07112 337 GGKRVltetgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLR 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1242547020 381 EGAVYINEMLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07112 417 AGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
15-424 |
1.38e-70 |
|
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: 229.50 E-value: 1.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQH------IKTKWT 88
Cdd:cd07101 34 WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERLLKPRRrrgaipVLTRTT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 89 ESYitfEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVAD 168
Cdd:cd07101 114 VNR---RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 169 IIAhKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHK 248
Cdd:cd07101 191 AIV-DNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 249 SLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKRE---G-AFYKPTILSEVTP 324
Cdd:cd07101 270 SVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARpdlGpYFYEPTVLTGVTE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 325 QMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLIS-----DPhlPFG 399
Cdd:cd07101 350 DMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAawasiDA--PMG 427
|
410 420
....*....|....*....|....*
gi 1242547020 400 GVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:cd07101 428 GMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
9-424 |
1.95e-70 |
|
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: 229.25 E-value: 1.95e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 9 QQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQS-IAEVQKCAYLCDYYIENAENF------LKPQ 81
Cdd:cd07115 29 RAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPRAADTFRYYAGWADKIegevipVRGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 82 HIktkwteSYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP--IYKNL 159
Cdd:cd07115 109 FL------NYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELM--AEAGFPagVLNVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 160 SLESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSC 238
Cdd:cd07115 181 TGFGEVAGAaLVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 239 IAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGA---FYK 315
Cdd:cd07115 261 TAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGArgfFVE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 316 PTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPH 395
Cdd:cd07115 341 PTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINTYNRFDPG 420
|
410 420
....*....|....*....|....*....
gi 1242547020 396 LPFGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:cd07115 421 SPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
5-426 |
2.92e-69 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 227.10 E-value: 2.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLK---PQ 81
Cdd:PRK11241 54 IDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGdtiPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 82 HIKTKwtESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSL 161
Cdd:PRK11241 134 HQADK--RLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 162 ESKFVA-DIIAHKHIKGVSLTGSEKAGKAV-AQCAgQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCI 239
Cdd:PRK11241 212 SAGAVGgELTSNPLVRKLSFTGSTEIGRQLmEQCA-KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 240 AAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGK---REGAFYKP 316
Cdd:PRK11241 291 CANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKaheLGGNFFQP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 317 TILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHL 396
Cdd:PRK11241 371 TILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA 450
|
410 420 430
....*....|....*....|....*....|
gi 1242547020 397 PFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:PRK11241 451 PFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-427 |
2.93e-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: 227.03 E-value: 2.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 22 QRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIA-EVQKCAYLCDYYIENAENfLKPQHIKTKWTE-SYITFEPIGV 99
Cdd:cd07143 69 KRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADK-IHGQVIETDIKKlTYTRHEPIGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 100 LLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVADIIA-HKHIKGV 178
Cdd:cd07143 148 CGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISsHMDIDKV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 179 SLTGSEKAGKAVAQCAGQ-HLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLST 257
Cdd:cd07143 228 AFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 258 FKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGAFYKPTILSEVTPQMPVFREETF 334
Cdd:cd07143 308 FKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRhgnEGYFIEPTIFTDVTEDMKIVKEEIF 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 335 GPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSGYGRELSQFG 414
Cdd:cd07143 388 GPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYA 467
|
410
....*....|...
gi 1242547020 415 MYEFANIKTVVIK 427
Cdd:cd07143 468 LENYTQIKAVHIN 480
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
42-425 |
1.98e-68 |
|
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: 224.15 E-value: 1.98e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 42 AKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENF--LKPQHIKTKWTE--SYITFEPIGVLLGVMPWNFPF----WQV 113
Cdd:cd07110 62 AELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQLdaKAERAVPLPSEDfkARVRREPVGVVGLITPWNFPLlmaaWKV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 114 frfvIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLK---FPIYKNLSLESKfvADIIAHKHIKGVSLTGSEKAGKAV 190
Cdd:cd07110 142 ----APALAAGCTVVLKPSELTSLTELELAEIAAEAGLPpgvLNVVTGTGDEAG--APLAAHPGIDKISFTGSTATGSQV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 191 AQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDK 270
Cdd:cd07110 216 MQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDP 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 271 FNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR-----EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFET 345
Cdd:cd07110 296 LEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRRpahleKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFAT 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 346 FDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVV 425
Cdd:cd07110 376 EDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
88-424 |
4.01e-68 |
|
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: 222.97 E-value: 4.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 88 TESYITFEPIGVLLGVMPWNFPF----WQVFrfviPNLILGNLFIVKHASNVPKSANLLESIFNSKklkFP--IYKNLSL 161
Cdd:cd07092 110 HTSMIRREPIGVVAQIAPWNYPLmmaaWKIA----PALAAGNTVVLKPSETTPLTTLLLAELAAEV---LPpgVVNVVCG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 162 ESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIA 240
Cdd:cd07092 183 GGASAGDaLVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 241 AKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMA----REDLAIELEKLvnesiSLGAKVICGGKR---EGAF 313
Cdd:cd07092 263 ACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNsaaqRERVAGFVERA-----PAHARVLTGGRRaegPGYF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 314 YKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISD 393
Cdd:cd07092 338 YEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLA 417
|
330 340 350
....*....|....*....|....*....|.
gi 1242547020 394 PHLPFGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:cd07092 418 AEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
27-387 |
1.13e-67 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 220.76 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 27 IKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWTESYITFE-PIGVLLGVMP 105
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKrALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 106 WNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVADIIA-HKHIKGVSLTGSE 184
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAgNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 185 KAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEA 264
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 265 LKRGDKFNAET-EIAEMAREDLAIELEKLVNESISLGAKVICGGKRE---GAFYKPTILSEVTPQMPVFREETFGPVAVV 340
Cdd:PRK10090 241 VQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVegkGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1242547020 341 TFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYIN 387
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
1-426 |
2.68e-67 |
|
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: 221.56 E-value: 2.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 1 MNHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIA-EVQKCAYLCDYY---IENAEN 76
Cdd:cd07117 40 VDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYFagvIRAEEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 77 FLKpqhIKTKWTESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIY 156
Cdd:cd07117 120 SAN---MIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 157 KNLSLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:cd07117 197 IVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR------- 309
Cdd:cd07117 277 VCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltengld 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEM 389
Cdd:cd07117 357 KGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTY 436
|
410 420 430
....*....|....*....|....*....|....*..
gi 1242547020 390 LISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07117 437 NQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
9-426 |
5.03e-67 |
|
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: 220.31 E-value: 5.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 9 QQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPI-SQSIAEVQKCAYLCDYY-----------IENAEN 76
Cdd:cd07108 29 KAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFgglagelkgetLPFGPD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 77 FLkpqhiktkwteSYITFEPIGVLLGVMPWNFPFwQVFRFVI-PNLILGNLFIVKHASNVPKSANLLESIFNsKKLKFPI 155
Cdd:cd07108 109 VL-----------TYTVREPLGVVGAILPWNAPL-MLAALKIaPALVAGNTVVLKAAEDAPLAVLLLAEILA-QVLPAGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 156 YKNLS-LESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNA-RMQN 233
Cdd:cd07108 176 LNVITgYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 234 AGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISL-GAKVICGGK---- 308
Cdd:cd07108 256 QGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPlpge 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 309 ---REGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVY 385
Cdd:cd07108 336 gplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQ 415
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1242547020 386 INEMLISDPHLPFGGVKNSGYGRELSQFGMYE-FANIKTVVI 426
Cdd:cd07108 416 VNQGGGQQPGQSYGGFKQSGLGREASLEGMLEhFTQKKTVNI 457
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
15-409 |
1.20e-66 |
|
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: 219.91 E-value: 1.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSI-AEVQKCAYLCDYY---IENAENFLKpqHIKTKwTES 90
Cdd:cd07559 54 WGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLaADIPLAIDHFRYFagvIRAQEGSLS--EIDED-TLS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 91 YITFEPIGVLLGVMPWNFPF----WQVfrfvIPNLILGNLFIVKHASNVPKSANLLESIFNSkklkfpiyknlsLESKFV 166
Cdd:cd07559 131 YHFHEPLGVVGQIIPWNFPLlmaaWKL----APALAAGNTVVLKPASQTPLSILVLMELIGD------------LLPKGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 167 ADII------------AHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDA-----NLELATSIAVNA 229
Cdd:cd07559 195 VNVVtgfgseagkplaSHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 230 RMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDlaiELEKLVNeSISL----GAKVIC 305
Cdd:cd07559 275 FAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKD---QLEKILS-YVDIgkeeGAEVLT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 306 GGKR-------EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQTYR 378
Cdd:cd07559 351 GGERltlggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDI----NRALR 426
|
410 420 430
....*....|....*....|....*....|....*
gi 1242547020 379 F----EEGAVYINEMLISDPHLPFGGVKNSGYGRE 409
Cdd:cd07559 427 VargiQTGRVWVNCYHQYPAHAPFGGYKKSGIGRE 461
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
23-425 |
1.88e-66 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 220.37 E-value: 1.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 23 RIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWT----ESYITFEPIG 98
Cdd:PLN02467 74 RAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPmetfKGYVLKEPLG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 99 VLLGVMPWNFPF----WQVfrfvIPNLILGNLFIVKH---AS-------NVPKSANLLESIFNskklkfpIYKNLSLESK 164
Cdd:PLN02467 154 VVGLITPWNYPLlmatWKV----APALAAGCTAVLKPselASvtclelaDICREVGLPPGVLN-------VVTGLGTEAG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 165 fvADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRF 244
Cdd:PLN02467 223 --APLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 245 LVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR-----EGAFYKPTIL 319
Cdd:PLN02467 301 LVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpehlkKGFFIEPTII 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 320 SEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINemlISDP---HL 396
Cdd:PLN02467 381 TDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN---CSQPcfcQA 457
|
410 420
....*....|....*....|....*....
gi 1242547020 397 PFGGVKNSGYGRELSQFGMYEFANIKTVV 425
Cdd:PLN02467 458 PWGGIKRSGFGRELGEWGLENYLSVKQVT 486
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
15-425 |
2.88e-63 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 212.43 E-value: 2.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIK------TKWT 88
Cdd:PRK09407 70 WAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAPRRRAgalpvlTKTT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 89 ESYItfePIGVLlGVM-PWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVA 167
Cdd:PRK09407 150 ELRQ---PKGVV-GVIsPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 168 DIIAhKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVH 247
Cdd:PRK09407 226 TALV-DNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVH 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 248 KSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKRE---G-AFYKPTILSEVT 323
Cdd:PRK09407 305 ESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARpdlGpLFYEPTVLTGVT 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 324 PQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLIS-----DPhlPF 398
Cdd:PRK09407 385 PDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgsvDA--PM 462
|
410 420
....*....|....*....|....*..
gi 1242547020 399 GGVKNSGYGRELSQFGMYEFANIKTVV 425
Cdd:PRK09407 463 GGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
15-425 |
7.94e-63 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 211.59 E-value: 7.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSI-AEVQKCAYLCDYYIENAENFL-------KPQHIKTk 86
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMFARLFRYYAGWADKIHgltvpadGPHHVQT- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 87 wtesyiTFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIyknLSLESKFV 166
Cdd:PLN02466 192 ------LHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGV---LNVVSGFG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 167 ----ADIIAHKHIKGVSLTGSEKAGKAVAQCAGQ-HLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAA 241
Cdd:PLN02466 263 ptagAALASHMDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 242 KRFLVHKSLKEKFLStfKSKVEALKR--GDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGAFYKP 316
Cdd:PLN02466 343 SRTFVHERVYDEFVE--KAKARALKRvvGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRfgsKGYYIQP 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 317 TILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHL 396
Cdd:PLN02466 421 TVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAI 500
|
410 420
....*....|....*....|....*....
gi 1242547020 397 PFGGVKNSGYGRELSQFGMYEFANIKTVV 425
Cdd:PLN02466 501 PFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
46-427 |
9.49e-63 |
|
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: 209.90 E-value: 9.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 46 TSDMGKPIS-QSIAEVQKCAYLCDYYIENAENFlkpqHIKTKWTE----SYITFEPIGVLLGVMPWNFPF----WQVfrf 116
Cdd:cd07141 94 TLDNGKPFSkSYLVDLPGAIKVLRYYAGWADKI----HGKTIPMDgdffTYTRHEPVGVCGQIIPWNFPLlmaaWKL--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 117 vIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFP-----IYKNLSLESKfvADIIAHKHIKGVSLTGSEKAGKAVA 191
Cdd:cd07141 167 -APALACGNTVVLKPAEQTPLTALYLASLI--KEAGFPpgvvnVVPGYGPTAG--AAISSHPDIDKVAFTGSTEVGKLIQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 192 QCAGQ-HLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDK 270
Cdd:cd07141 242 QAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 271 FNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFD 347
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRhgdKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 348 EAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVIK 427
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
5-426 |
1.28e-62 |
|
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: 208.77 E-value: 1.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENfLKPQHIK 84
Cdd:cd07107 25 VAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTE-LKGETIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 85 TKWTE-SYITFEPIGVLLGVMPWNFPF-WQVFRFVIPnLILGNLFIVKHASNVPKSANLLESIFNSKklkFP--IYKNLS 160
Cdd:cd07107 104 VGGRNlHYTLREPYGVVARIVAFNHPLmFAAAKIAAP-LAAGNTVVVKPPEQAPLSALRLAELAREV---LPpgVFNILP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 161 LESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLE-LATSIAVNARMQNAGQSC 238
Cdd:cd07107 180 GDGATAGAaLVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEaAADAAVAGMNFTWCGQSC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 239 IAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR------EGA 312
Cdd:cd07107 260 GSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRpegpalEGG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 313 FY-KPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEmli 391
Cdd:cd07107 340 FYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWING--- 416
|
410 420 430
....*....|....*....|....*....|....*...
gi 1242547020 392 SDPH---LPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07107 417 SSRHflgAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
23-426 |
1.24e-61 |
|
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: 205.45 E-value: 1.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 23 RIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQS-IAEVQKCAYLCDYYIENAENFLKPQHIKTKWT----ESYITFEPI 97
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAyLTEIAVVLGEIDHALKHLKKWMKPRRVSVPLLlqpaKAYVIPEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 98 GVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSkklkfpiYknlsLESKFVA---------- 167
Cdd:cd07087 102 GVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPK-------Y----FDPEAVAvveggvevat 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 168 DIIAHK--HIkgvSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFL 245
Cdd:cd07087 171 ALLAEPfdHI---FFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 246 VHKSLKEKFLSTFKSKVEALkRGDKFNAETEIAEMAREDLAIELEKLVNesislGAKVICGGKREGA--FYKPTILSEVT 323
Cdd:cd07087 248 VHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLD-----DGKVVIGGQVDKEerYIAPTILDDVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 324 PQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKD---VEFIKSQTyrfEEGAVYINEMLI--SDPHLPF 398
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDkavQERVLAET---SSGGVCVNDVLLhaAIPNLPF 398
|
410 420
....*....|....*....|....*...
gi 1242547020 399 GGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07087 399 GGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
9-426 |
1.40e-61 |
|
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: 205.54 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 9 QQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKP--------ISQSIAEVQkcaylcdYYIENAENFLKP 80
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPaaevdlteILPVLSEIN-------HAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 81 QHIKTKW----TESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVK------HASNVpkSANLLESIFNSKK 150
Cdd:cd07134 81 KRVRTPLllfgTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKpseltpHTSAV--IAKIIREAFDEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 151 LKF-----PIYKNLsLESKFvadiiahKHIkgvSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSI 225
Cdd:cd07134 159 VAVfegdaEVAQAL-LELPF-------DHI---FFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 226 AVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEalkrgdKFNAETEiAEMAREDLA--------IELEKLVNESI 297
Cdd:cd07134 228 IAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIE------KFYGKDA-ARKASPDLArivndrhfDRLKGLLDDAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 298 SLGAKVICGGKREGA--FYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQ 375
Cdd:cd07134 301 AKGAKVEFGGQFDAAqrYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1242547020 376 TYRFEEGAVYINEMLI--SDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07134 381 LARTSSGGVVVNDVVLhfLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
90-427 |
2.58e-61 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 205.91 E-value: 2.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 90 SYITFEPIGVLLGVMPWNFPF----WQVfrfvIPNLILGNLFIVKHASNVPKSANLLESIfnSKKLkFP--IYKNLSLES 163
Cdd:PRK13473 132 SMIRRDPVGVVASIAPWNYPLmmaaWKL----APALAAGNTVVLKPSEITPLTALKLAEL--AADI-LPpgVLNVVTGRG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 164 KFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAK 242
Cdd:PRK13473 205 ATVGDaLVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAAC 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 243 RFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEI------AEMARedlaieLEKLVNESISLG-AKVICGGKR---EGA 312
Cdd:PRK13473 285 RIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELgplisaAHRDR------VAGFVERAKALGhIRVVTGGEApdgKGY 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 313 FYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINE--ML 390
Cdd:PRK13473 359 YYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNThfML 438
|
330 340 350
....*....|....*....|....*....|....*...
gi 1242547020 391 ISD-PHlpfGGVKNSGYGRELSQFGMYEFANIKTVVIK 427
Cdd:PRK13473 439 VSEmPH---GGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
22-425 |
2.16e-60 |
|
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: 202.96 E-value: 2.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 22 QRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENF------LKPQHIktkwteSYITFE 95
Cdd:cd07120 43 LRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEagrmiePEPGSF------SLVLRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 96 PIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPK-SANLLESIFNSKKLKFPIYkNLSLES--KFVADIIAH 172
Cdd:cd07120 117 PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQiNAAIIRILAEIPSLPAGVV-NLFTESgsEGAAHLVAS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 173 KHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKE 252
Cdd:cd07120 196 PDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIAD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 253 KFLSTFKSKVEALKRGDKFNAETEIAEMA-REDLAIeLEKLVNESISLGAKVICGGKR------EGAFYKPTILSEVTPQ 325
Cdd:cd07120 276 EVRDRLAARLAAVKVGPGLDPASDMGPLIdRANVDR-VDRMVERAIAAGAEVVLRGGPvteglaKGAFLRPTLLEVDDPD 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 326 MPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSG 405
Cdd:cd07120 355 ADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSG 434
|
410 420
....*....|....*....|
gi 1242547020 406 YGRELSQFGMYEFANIKTVV 425
Cdd:cd07120 435 LGRLHGVAALEDFIEYKHIY 454
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
4-427 |
3.23e-58 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 198.33 E-value: 3.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 4 IIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGK-PISQSIAEVQKCAYLCDYYIENAENFLKP-- 80
Cdd:PTZ00381 12 IVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRhPFETKMTEVLLTVAEIEHLLKHLDEYLKPek 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 81 --QHIKTKWTESYITFEPIGVLLGVMPWNFPFwqvFRFVIP---NLILGNLFIVKHASNVPKSANLLESIFNsKKLKFPI 155
Cdd:PTZ00381 92 vdTVGVFGPGKSYIIPEPLGVVLVIGAWNYPL---NLTLIPlagAIAAGNTVVLKPSELSPHTSKLMAKLLT-KYLDPSY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 156 YKNLSLESKFVADIIAHK--HIkgvSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQN 233
Cdd:PTZ00381 168 VRVIEGGVEVTTELLKEPfdHI---FFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 234 AGQSCIAAKRFLVHKSLKEKFLSTFKskvEALKR--GDKFNAETEIAEMAREDLAIELEKLVNESislGAKVICGGK--R 309
Cdd:PTZ00381 245 AGQTCVAPDYVLVHRSIKDKFIEALK---EAIKEffGEDPKKSEDYSRIVNEFHTKRLAELIKDH---GGKVVYGGEvdI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKsqtyRFEE----GAVY 385
Cdd:PTZ00381 319 ENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKE----LVLEntssGAVV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1242547020 386 INEML--ISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVIK 427
Cdd:PTZ00381 395 INDCVfhLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
5-424 |
5.65e-58 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 197.41 E-value: 5.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQ-SIAEVQKCAYLCDYY------IENaenf 77
Cdd:PRK13252 50 VASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQEtSVVDIVTGADVLEYYaglapaLEG---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 78 lkpQHIKTKWTESYITF-EPIGVLLGVMPWNFPF----WQVfrfvIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLK 152
Cdd:PRK13252 126 ---EQIPLRGGSFVYTRrEPLGVCAGIGAWNYPIqiacWKS----APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 153 FPIYKNLSLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQ 232
Cdd:PRK13252 199 DGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 233 NAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDlaiELEKL---VNESISLGAKVICGGKR 309
Cdd:PRK13252 279 SSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFA---HRDKVlgyIEKGKAEGARLLCGGER 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 -------EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEG 382
Cdd:PRK13252 356 lteggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAG 435
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1242547020 383 AVYINEMLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:PRK13252 436 ICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
1-424 |
8.16e-58 |
|
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: 196.58 E-value: 8.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 1 MNHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCaylcdyyIENAE----- 75
Cdd:cd07085 40 VDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLRG-------LEVVEfacsi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 76 -NFLKPQHIK--TKWTESYITFEPIGVLLGVMPWNFP----FWqvfrfVIPNLI-LGNLFIVKHASNVPKSANLLESIFN 147
Cdd:cd07085 113 pHLLKGEYLEnvARGIDTYSYRQPLGVVAGITPFNFPamipLW-----MFPMAIaCGNTFVLKPSERVPGAAMRLAELLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 148 SKKLKFPIYkNLSLESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKsVLELGGSAAF-IICEDANLELATSI 225
Cdd:cd07085 188 EAGLPDGVL-NVVHGGKEAVNaLLDHPDIKAVSFVGSTPVGEYIYERAAANGKR-VQALGGAKNHaVVMPDADLEQTANA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 226 AVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVIC 305
Cdd:cd07085 266 LVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 306 GGKR-------EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYR 378
Cdd:cd07085 346 DGRGvkvpgyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQRE 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1242547020 379 FEEGAVYINeMLISDP--HLPFGGVKNS------GYGRELSQFgmyeFANIKTV 424
Cdd:cd07085 426 VDAGMVGIN-VPIPVPlaFFSFGGWKGSffgdlhFYGKDGVRF----YTQTKTV 474
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
95-418 |
1.79e-57 |
|
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: 196.08 E-value: 1.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVADIIAHKH 174
Cdd:cd07111 146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 175 IKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKF 254
Cdd:cd07111 226 VDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEEL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 255 LSTFKSKVEALKRGDKFNAETEIAEM--AREDLAIEleKLVNESISLGAKVI---CGGKREGAFYKPTILSEVTPQMPVF 329
Cdd:cd07111 306 IRKLKERMSHLRVGDPLDKAIDMGAIvdPAQLKRIR--ELVEEGRAEGADVFqpgADLPSKGPFYPPTLFTNVPPASRIA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 330 REETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSGYGRE 409
Cdd:cd07111 384 QEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGRE 463
|
....*....
gi 1242547020 410 LSQFGMYEF 418
Cdd:cd07111 464 GGKEGLYEY 472
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-425 |
3.87e-54 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 187.72 E-value: 3.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQS-IAEVQKCAYLCDYYIENAENFLKPQHIKTKWTESYIT 93
Cdd:PLN02766 76 WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGkAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 94 FEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIfnSKKLKFP---IYKNLSLESKFVADII 170
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHL--AKLAGVPdgvINVVTGFGPTAGAAIA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 171 AHKHIKGVSLTGSEKAGKAVAQCAGQ-HLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKS 249
Cdd:PLN02766 234 SHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 250 LKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGK---REGAFYKPTILSEVTPQM 326
Cdd:PLN02766 314 IYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKpcgDKGYYIEPTIFTDVTEDM 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 327 PVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSGY 406
Cdd:PLN02766 394 KIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGF 473
|
410
....*....|....*....
gi 1242547020 407 GRELSQFGMYEFANIKTVV 425
Cdd:PLN02766 474 GRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
15-427 |
4.72e-54 |
|
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: 186.88 E-value: 4.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIA-EVQKCAYLCDYYIE-----NAENfLKPQhIKTKWT 88
Cdd:cd07113 54 WAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQSANFLRYFAGwatkiNGET-LAPS-IPSMQG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 89 ESYITF---EPIGVLLGVMPWNFPF----WQVfrfvIPNLILGNLFIVKHASNVPKSanLLESIFNSKKLKFP--IYKNL 159
Cdd:cd07113 132 ERYTAFtrrEPVGVVAGIVPWNFSVmiavWKI----GAALATGCTIVIKPSEFTPLT--LLRVAELAKEAGIPdgVLNVV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 160 SLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCI 239
Cdd:cd07113 206 NGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 240 AAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGK---REGAFYKP 316
Cdd:cd07113 286 APERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEalaGEGYFVQP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 317 TILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQTYRF----EEGAVYINEMLIS 392
Cdd:cd07113 366 TLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNL----SKALRYipriEAGTVWVNMHTFL 441
|
410 420 430
....*....|....*....|....*....|....*
gi 1242547020 393 DPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVIK 427
Cdd:cd07113 442 DPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-426 |
3.05e-53 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 185.10 E-value: 3.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAE-VQKCAYLCDYYIENAENFLKPQHIKTKWTESYIT 93
Cdd:PRK09847 75 WSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDdIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 94 FEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIyknLSLESKFVAD----I 169
Cdd:PRK09847 155 REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGV---LNVVTGFGHEagqaL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 170 IAHKHIKGVSLTGSEKAGKAVAQCAGQ-HLKKSVLELGGSAAFIICEDA-NLELATSIAVNARMQNAGQSCIAAKRFLVH 247
Cdd:PRK09847 232 SRHNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 248 KSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGaKVICGGKREG--AFYKPTILSEVTPQ 325
Cdd:PRK09847 312 ESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGlaAAIGPTIFVDVDPN 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 326 MPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPHLPFGGVKNSG 405
Cdd:PRK09847 391 ASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSG 470
|
410 420
....*....|....*....|.
gi 1242547020 406 YGRELSQFGMYEFANIKTVVI 426
Cdd:PRK09847 471 NGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
19-427 |
3.83e-53 |
|
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: 183.47 E-value: 3.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 19 SVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKP--------ISQSIAEVqkcaylcDYYIENAENFLKPQHIKTKWT-- 88
Cdd:cd07136 18 DVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSefeaymteIGFVLSEI-------NYAIKHLKKWMKPKRVKTPLLnf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 89 --ESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKklkFP------------ 154
Cdd:cd07136 91 psKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET---FDeeyvavveggve 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 155 IYKNLsLESKFvaDIIAhkhikgvsLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNA 234
Cdd:cd07136 168 ENQEL-LDQKF--DYIF--------FTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 235 GQSCIAAKRFLVHKSLKEKFLstfkskvEALKRgdkfnaetEIAEMARED--LAIELEKLVNES-----ISL--GAKVIC 305
Cdd:cd07136 237 GQTCVAPDYVLVHESVKEKFI-------KELKE--------EIKKFYGEDplESPDYGRIINEKhfdrlAGLldNGKIVF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 306 GGK--REGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGA 383
Cdd:cd07136 302 GGNtdRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGG 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1242547020 384 VYINE--MLISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVIK 427
Cdd:cd07136 382 GCINDtiMHLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSILKK 427
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
30-425 |
9.03e-53 |
|
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: 182.42 E-value: 9.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 30 IKDNllknTDLHAKAITSDMGKPISQSI-AEVQKCAYLCDYYIENAENFLKPQHIKT-----KWTESYITFEPIGVLLGV 103
Cdd:cd07135 40 VKDN----EEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLKKWAKDEKVKDgplafMFGKPRIRKEPLGVVLII 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 104 MPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNsKKLKFPIYKNLS---------LESKFvaDIIAHkh 174
Cdd:cd07135 116 GPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQggvpettalLEQKF--DKIFY-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 175 ikgvslTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKF 254
Cdd:cd07135 191 ------TGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 255 lstfkskVEALKR------GDKFNAETEIAEMAREDLAIELEKLVNESislGAKVICGGKREGA--FYKPTILSEVTPQM 326
Cdd:cd07135 265 -------VEELKKvldefyPGGANASPDYTRIVNPRHFNRLKSLLDTT---KGKVVIGGEMDEAtrFIPPTIVSDVSWDD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 327 PVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKD---VEFIKSQTyrfEEGAVYINEMLI--SDPHLPFGGV 401
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDkseIDHILTRT---RSGGVVINDTLIhvGVDNAPFGGV 411
|
410 420
....*....|....*....|....
gi 1242547020 402 KNSGYGRELSQFGMYEFANIKTVV 425
Cdd:cd07135 412 GDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
2-409 |
1.73e-52 |
|
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: 182.41 E-value: 1.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 2 NHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDY----------YI 71
Cdd:cd07130 37 ESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFavglsrqlygLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 72 ENAEnflKPQHIKtkwtesYITFEPIGVLLGVMPWNFPF----WqvfrfvipN----LILGNLFIVKHASNVPKSA---- 139
Cdd:cd07130 117 IPSE---RPGHRM------MEQWNPLGVVGVITAFNFPVavwgW--------NaaiaLVCGNVVVWKPSPTTPLTAiavt 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 140 NLLESIFNSKKLKFPIYKNLSLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANL 219
Cdd:cd07130 180 KIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 220 ELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDlAIEL-EKLVNESIS 298
Cdd:cd07130 260 DLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKA-AVDNyLAAIEEAKS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 299 LGAKVICGGKR---EGAFYKPTILsEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQ 375
Cdd:cd07130 339 QGGTVLFGGKVidgPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDL----RN 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1242547020 376 TYRF------EEGAVYINemlisdphLP---------FGGVKNSGYGRE 409
Cdd:cd07130 414 AFRWlgpkgsDCGIVNVN--------IGtsgaeiggaFGGEKETGGGRE 454
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
15-407 |
6.84e-52 |
|
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: 181.65 E-value: 6.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNT-DLHAkAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWTESYIT 93
Cdd:cd07124 85 WRRTPPEERARLLLRAAALLRRRRfELAA-WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 94 FEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVAD-IIAH 172
Cdd:cd07124 164 YRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDyLVEH 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 173 KHIKGVSLTGSEKAGKAVAQCAGQ------HLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLV 246
Cdd:cd07124 244 PDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 247 HKSLKEKFLSTFKSKVEALKRGDKFNAETE----IAEMAREDLAIELEKLVNEsislgAKVICGGKR-----EGAFYKPT 317
Cdd:cd07124 324 HESVYDEFLERLVERTKALKVGDPEDPEVYmgpvIDKGARDRIRRYIEIGKSE-----GRLLLGGEVlelaaEGYFVQPT 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 318 ILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEML---ISDP 394
Cdd:cd07124 399 IFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKItgaLVGR 478
|
410
....*....|...
gi 1242547020 395 HlPFGGVKNSGYG 407
Cdd:cd07124 479 Q-PFGGFKMSGTG 490
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
95-427 |
2.07e-51 |
|
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: 180.00 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSAnllesifnskkLKFpiyKNLSLESKFVADII---- 170
Cdd:cd07140 146 EPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTA-----------LKF---AELTVKAGFPKGVInilp 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 171 -----------AHKHIKGVSLTGSEKAGKAVAQ-CAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSC 238
Cdd:cd07140 212 gsgslvgqrlsDHPDVRKLGFTGSTPIGKHIMKsCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENC 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 239 IAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGK---REGAFYK 315
Cdd:cd07140 292 IAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKqvdRPGFFFE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 316 PTILSEVTPQMPVFREETFGPVAVVTFFET--FDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISD 393
Cdd:cd07140 372 PTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTD 451
|
330 340 350
....*....|....*....|....*....|....
gi 1242547020 394 PHLPFGGVKNSGYGRELSQFGMYEFANIKTVVIK 427
Cdd:cd07140 452 VAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
22-424 |
1.44e-49 |
|
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: 173.83 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 22 QRIEIIKDIKDNLLKNTDLHAKAITSDMG-KPISQS-IAEVQKCAYLCDYYIENAENFLKPQHIKTKWT----ESYITFE 95
Cdd:cd07133 21 ERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETlLAEILPSIAGIKHARKHLKKWMKPSRRHVGLLflpaKAEVEYQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 96 PIGVLlGVM-PWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKklkFPiyknlslESKFV-----ADI 169
Cdd:cd07133 101 PLGVV-GIIvPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY---FD-------EDEVAvvtggADV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 170 IAH------KHIkgvsL-TGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELA-TSIAVnARMQNAGQSCIAA 241
Cdd:cd07133 170 AAAfsslpfDHL----LfTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAaERIAF-GKLLNAGQTCVAP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 242 KRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAE-TEI---AEMARedlaieLEKLVNESISLGAKVI-CGGKREGAFYK- 315
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDyTSIineRHYAR------LQGLLEDARAKGARVIeLNPAGEDFAATr 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 316 ---PTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKD---VEFIKSQTYrfeEGAVYINEM 389
Cdd:cd07133 319 klpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDkaeQDRVLRRTH---SGGVTINDT 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1242547020 390 L--ISDPHLPFGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:cd07133 396 LlhVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
15-409 |
3.61e-47 |
|
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: 168.40 E-value: 3.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAylCDYY------IENAENFLkpQHIKTKwT 88
Cdd:cd07116 54 WGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADIPLA--IDHFryfagcIRAQEGSI--SEIDEN-T 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 89 ESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNS--KKLKFPIYKNLSLES-KF 165
Cdd:cd07116 129 VAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDllPPGVVNVVNGFGLEAgKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 166 VAdiiAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICE----------DANLELATSIAVNArmqnaG 235
Cdd:cd07116 209 LA---SSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFAdvmdaddaffDKALEGFVMFALNQ-----G 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 236 QSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDlaiELEKLVNeSISLG----AKVICGGKR-- 309
Cdd:cd07116 281 EVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLE---QLEKILS-YIDIGkeegAEVLTGGERne 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 -----EGAFYKPTILSEvTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVefikSQTYRF----E 380
Cdd:cd07116 357 lggllGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDG----NTAYRMgrgiQ 431
|
410 420
....*....|....*....|....*....
gi 1242547020 381 EGAVYINEMLISDPHLPFGGVKNSGYGRE 409
Cdd:cd07116 432 AGRVWTNCYHLYPAHAAFGGYKQSGIGRE 460
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
15-408 |
1.15e-43 |
|
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: 157.82 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWTESYITF 94
Cdd:cd07095 16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGERATPMAQGRAVLRH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKfPIYKNLSLESKFV-ADIIAHK 173
Cdd:cd07095 96 RPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLP-PGVLNLVQGGRETgEALAAHE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 174 HIKGVSLTGSEKAGKAVA-QCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLK- 251
Cdd:cd07095 175 GIDGLLFTGSAATGLLLHrQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGAVg 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 252 EKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGAFYKPTILsEVTPQMPV 328
Cdd:cd07095 255 DAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERlvaGTAFLSPGII-DVTDAADV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 329 FREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDPH-LPFGGVKNSGYG 407
Cdd:cd07095 334 PDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGASStAPFGGVGLSGNH 413
|
.
gi 1242547020 408 R 408
Cdd:cd07095 414 R 414
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
22-426 |
7.33e-43 |
|
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: 156.42 E-value: 7.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 22 QRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKC---AYLCDYYIENAENFLKPQHIkTKWTESYITF---E 95
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAidgVELAADELGQLGGREIPMGL-TPASAGRIAFttrE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 96 PIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKL-----KFPIYKNLSLEsKFVADii 170
Cdd:cd07148 124 PIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLpegwcQAVPCENAVAE-KLVTD-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 171 ahKHIKGVSLTGSEKAG-----KAV--AQCAgqhlkksvLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKR 243
Cdd:cd07148 201 --PRVAFFSFIGSARVGwmlrsKLApgTRCA--------LEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 244 FLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREG-AFYKPTILSEV 322
Cdd:cd07148 271 VFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSdTTYAPTVLLDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 323 TPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEmlisdpH------- 395
Cdd:cd07148 351 PRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND------Htafrvdw 424
|
410 420 430
....*....|....*....|....*....|.
gi 1242547020 396 LPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:cd07148 425 MPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
15-409 |
1.20e-41 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 154.22 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENF-------LKPQHIKTKw 87
Cdd:PLN02315 72 WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLngsiipsERPNHMMME- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 88 tesyiTFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVP----KSANLLESIFNSKKLKFPIYKNLSLES 163
Cdd:PLN02315 151 -----VWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCGGA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 164 KFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKR 243
Cdd:PLN02315 226 EIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 244 FLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGK---REGAFYKPTILs 320
Cdd:PLN02315 306 LLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSaieSEGNFVQPTIV- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 321 EVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIksqtyrFEEGAVYINEMLISDPHLP--- 397
Cdd:PLN02315 385 EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETI------FKWIGPLGSDCGIVNVNIPtng 458
|
410
....*....|....*...
gi 1242547020 398 ------FGGVKNSGYGRE 409
Cdd:PLN02315 459 aeiggaFGGEKATGGGRE 476
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
50-405 |
2.24e-40 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 150.47 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 50 GKPISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWTESYITF-EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFI 128
Cdd:PRK03137 124 GKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 129 VKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFVAD-IIAHKHIKGVSLTGSEKAG------KAVAQCAGQHLKKS 201
Cdd:PRK03137 204 LKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDyLVDHPKTRFITFTGSREVGlriyerAAKVQPGQIWLKRV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 202 VLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAE---TEIA 278
Cdd:PRK03137 284 IAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAymgPVIN 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 279 EMAredlaielEKLVNESISLG---AKVICGGKR---EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNL 352
Cdd:PRK03137 364 QAS--------FDKIMSYIEIGkeeGRLVLGGEGddsKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEI 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1242547020 353 SNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEML---ISDPHlPFGGVKNSG 405
Cdd:PRK03137 436 ANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCtgaIVGYH-PFGGFNMSG 490
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
33-427 |
1.12e-38 |
|
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: 144.67 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 33 NLLKNTDLHAKAIT----SDMGKPISQS-IAEVQKCAYLCDYYIENAENFLKPQHIKTKWT----ESYITFEPIGVLLGV 103
Cdd:cd07132 28 ALLRMLEENEDEIVealaKDLRKPKFEAvLSEILLVKNEIKYAISNLPEWMKPEPVKKNLAtlldDVYIYKEPLGVVLII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 104 MPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnSKKLK---FPIYK------NLSLESKFvaDIIAHkh 174
Cdd:cd07132 108 GAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-PKYLDkecYPVVLggveetTELLKQRF--DYIFY-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 175 ikgvslTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKF 254
Cdd:cd07132 183 ------TGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 255 LSTFKskvEALKR--GDKFNAETEIAEMAREDLAIELEKLVNesislGAKVICGGKREGA--FYKPTILSEVTPQMPVFR 330
Cdd:cd07132 257 VEALK---KTLKEfyGEDPKESPDYGRIINDRHFQRLKKLLS-----GGKVAIGGQTDEKerYIAPTVLTDVKPSDPVMQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 331 EETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINE--MLISDPHLPFGGVKNSGYGR 408
Cdd:cd07132 329 EEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDtiMHYTLDSLPFGGVGNSGMGA 408
|
410
....*....|....*....
gi 1242547020 409 ELSQFGMYEFANIKTVVIK 427
Cdd:cd07132 409 YHGKYSFDTFSHKRSCLVK 427
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
14-426 |
1.78e-36 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 139.51 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 14 LWKEYSVIQRI-EIIKDIKDNLlkntdlhAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLK----------PQH 82
Cdd:PLN00412 74 LWKRAELLHKAaAILKEHKAPI-------AECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGegkflvsdsfPGN 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 83 IKTKWT-ESYItfePIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnsKKLKFPiyKNL-S 160
Cdd:PLN00412 147 ERNKYClTSKI---PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCF--HLAGFP--KGLiS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 161 LESKFVADI----IAHKHIKGVSLTGSEkAGKAVAQCAGqhLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:PLN00412 220 CVTGKGSEIgdflTMHPGVNCISFTGGD-TGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKfNAETEIAEMAREDLAIELEKLVNESISLGAKVICGGKREGAFYKP 316
Cdd:PLN00412 297 RCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNLIWP 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 317 TILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLISDP-H 395
Cdd:PLN00412 376 LLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPdH 455
|
410 420 430
....*....|....*....|....*....|.
gi 1242547020 396 LPFGGVKNSGYGRELSQFGMYEFANIKTVVI 426
Cdd:PLN00412 456 FPFQGLKDSGIGSQGITNSINMMTKVKSTVI 486
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-407 |
4.03e-36 |
|
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: 138.48 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 1 MNHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKP 80
Cdd:cd07083 57 AEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 81 QHIKTKWTESY--ITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKN 158
Cdd:cd07083 137 AVEVVPYPGEDneSFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 159 LSLESKFVAD-IIAHKHIKGVSLTGSEKAGKAVAQCAGQHL------KKSVLELGGSAAFIICEDANLELATSIAVNARM 231
Cdd:cd07083 217 LPGVGEEVGAyLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAF 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 232 QNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNESISLGaKVICGGKR-- 309
Cdd:cd07083 297 GFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRle 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 -EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFET--FDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYI 386
Cdd:cd07083 376 gEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDddFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYI 455
|
410 420
....*....|....*....|...
gi 1242547020 387 NEMLISD--PHLPFGGVKNSGYG 407
Cdd:cd07083 456 NRKITGAlvGVQPFGGFKLSGTN 478
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-407 |
1.47e-35 |
|
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: 137.33 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 2 NHIIENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNT-DLHAkAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKP 80
Cdd:cd07125 72 DAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRgELIA-LAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 81 QHIKTKWTES-YITFEPIGVLLGVMPWNFPfwqvfrFVIP------NLILGNLFIVKHASNVPKSANLLESIF-----NS 148
Cdd:cd07125 151 PELPGPTGELnGLELHGRGVFVCISPWNFP------LAIFtgqiaaALAAGNTVIAKPAEQTPLIAARAVELLheagvPR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 149 KKLKFPIYKNLSLESKFVadiiAHKHIKGVSLTGSEKAGKAVAQC-AGQHLKKSVL--ELGGSAAFIICEDANLELATSI 225
Cdd:cd07125 225 DVLQLVPGDGEEIGEALV----AHPRIDGVIFTGSTETAKLINRAlAERDGPILPLiaETGGKNAMIVDSTALPEQAVKD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 226 AVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMAREDLAIELEKLVNEsISLGAKVIC 305
Cdd:cd07125 301 VVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTEL-MRGEAWLIA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 306 GGK---REGAFYKPTILSEVTPqmPVFREETFGPVA-VVTF-FETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFE 380
Cdd:cd07125 380 PAPlddGNGYFVAPGIIEIVGI--FDLTTEVFGPILhVIRFkAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVE 457
|
410 420 430
....*....|....*....|....*....|..
gi 1242547020 381 EGAVYINEMLI-----SDphlPFGGVKNSGYG 407
Cdd:cd07125 458 AGNLYINRNITgaivgRQ---PFGGWGLSGTG 486
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
9-424 |
1.82e-33 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 132.56 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 9 QQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDY-----------YIENAENF 77
Cdd:PLN02419 161 KQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHacgmatlqmgeYLPNVSNG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 78 LkpqhiktkwtESYITFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYK 157
Cdd:PLN02419 241 V----------DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLN 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 158 NLSLESKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQS 237
Cdd:PLN02419 311 IVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQR 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 238 CIAAKRFLV---HKSLKEKFLStfKSKVEALKRGDKFNAETE--IAEMAREDLAIELEKLVNESISL---GAKVICGGKR 309
Cdd:PLN02419 391 CMALSTVVFvgdAKSWEDKLVE--RAKALKVTCGSEPDADLGpvISKQAKERICRLIQSGVDDGAKLlldGRDIVVPGYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYIN-E 388
Cdd:PLN02419 469 KGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINvP 548
|
410 420 430
....*....|....*....|....*....|....*....
gi 1242547020 389 MLISDPHLPFGGVKNSgYGRELSQFGMYE---FANIKTV 424
Cdd:PLN02419 549 IPVPLPFFSFTGNKAS-FAGDLNFYGKAGvdfFTQIKLV 586
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
23-424 |
4.04e-33 |
|
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: 129.07 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 23 RIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQS-IAEVQKCAYLCDYYIENAENFLKPQHIKTkwteSYITF------- 94
Cdd:cd07137 23 RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKWMAPEKVKT----PLTTFpakaeiv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 -EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFnskklkfPIYknlsLESKFVADI---- 169
Cdd:cd07137 99 sEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-------PEY----LDTKAIKVIeggv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 170 ------IAHKHIKgVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFIICEDANLELATS-IAVNARMQNAGQSCIAAK 242
Cdd:cd07137 168 pettalLEQKWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRrIAGGKWGCNNGQACIAPD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 243 RFLVHKSLKEKFLSTFKSKVEalkrgdKFNAET--EIAEMAR---EDLAIELEKLVNESiSLGAKVICGGKR--EGAFYK 315
Cdd:cd07137 247 YVLVEESFAPTLIDALKNTLE------KFFGENpkESKDLSRivnSHHFQRLSRLLDDP-SVADKIVHGGERdeKNLYIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 316 PTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLI--SD 393
Cdd:cd07137 320 PTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVqyAI 399
|
410 420 430
....*....|....*....|....*....|.
gi 1242547020 394 PHLPFGGVKNSGYGRELSQFGMYEFANIKTV 424
Cdd:cd07137 400 DTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
44-427 |
6.00e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 109.37 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 44 AITSDMGKP-ISQSIAEVQKCAYLCDYYIENAENFLKPQHIKTKWT----ESYITFEPIGVLLGVMPWNFPFWQVFRFVI 118
Cdd:PLN02174 55 ALRDDLGKPeLESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTtfpaSAEIVSEPLGVVLVISAWNYPFLLSIDPVI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 119 PNLILGNLFIVKHASNVPKSANLLESIFnSKKLKFPIYKNLSLESKFVADIIAHKHIKgVSLTGSEKAGKAVAQCAGQHL 198
Cdd:PLN02174 135 GAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKWDK-IFYTGSSKIGRVIMAAAAKHL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 199 KKSVLELGGSAAFIICEDANLELAT-SIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAEtEI 277
Cdd:PLN02174 213 TPVVLELGGKSPVVVDSDTDLKVTVrRIIAGKWGCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 278 AEMAREDLAIELEKLVNESiSLGAKVICGGK--REGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQ 355
Cdd:PLN02174 292 SRIVNSTHFDRLSKLLDEK-EVSDKIVYGGEkdRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRS 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1242547020 356 SDFGLGVSIFSKDVEFIKSQTYRFEEGAVYINEMLI--SDPHLPFGGVKNSGYGRELSQFGMYEFANIKTVVIK 427
Cdd:PLN02174 371 RPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVhlALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYR 444
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
15-405 |
9.89e-24 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 103.11 E-value: 9.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIenaenflKPQHIKTkWTESYITF 94
Cdd:PRK09457 53 WARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINKIAISI-------QAYHERT-GEKRSEMA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 EPIGVL----LGVM----PWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIYKNLSLESKFV 166
Cdd:PRK09457 125 DGAAVLrhrpHGVVavfgPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 167 ADIIAHKHIKGVSLTGSEKAGKAV-AQCAGQHLKKSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQSCIAAKRFL 245
Cdd:PRK09457 205 KALAAHPDIDGLLFTGSANTGYLLhRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 246 VHKSLK-EKFLSTFKSKVEALKRGDkFNAETE--IAEMAREDLAIELEKLVNESISLGAKVICGGKR---EGAFYKPTIL 319
Cdd:PRK09457 285 VPQGAQgDAFLARLVAVAKRLTVGR-WDAEPQpfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQlqaGTGLLTPGII 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 320 sEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDvefiKSQTYRFEE----GAVYINEMLISDPH 395
Cdd:PRK09457 364 -DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDD----REDYDQFLLeiraGIVNWNKPLTGASS 438
|
410
....*....|.
gi 1242547020 396 -LPFGGVKNSG 405
Cdd:PRK09457 439 aAPFGGVGASG 449
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
5-407 |
6.20e-22 |
|
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: 97.67 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 5 IENIQQSYLLWKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLkPQHik 84
Cdd:TIGR01238 80 IDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVL-GEF-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 85 tkwtesyiTFEPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSAN-----LLESIFNSKKLKFPIYKNL 159
Cdd:TIGR01238 157 --------SVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYravelMQEAGFPAGTIQLLPGRGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 160 SLEskfvADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVL---ELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:TIGR01238 229 DVG----AALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPliaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIA----EMAREDLAIELEKL--VNESI---SLGAKVICgg 307
Cdd:TIGR01238 305 RCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGpvidAEAKQNLLAHIEHMsqTQKKIaqlTLDDSRAC-- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 308 kREGAFYKPTILSevTPQMPVFREETFGPVAVVTFFET--FDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFEEGAVY 385
Cdd:TIGR01238 383 -QHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCY 459
|
410 420
....*....|....*....|....
gi 1242547020 386 INEMLISD--PHLPFGGVKNSGYG 407
Cdd:TIGR01238 460 VNRNQVGAvvGVQPFGGQGLSGTG 483
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
13-425 |
2.62e-17 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 83.62 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 13 LLWKEYSVIQRIEIIKDIKDNLLKntdlhakAITSDMGKPISQSIA-EVQKCAYLCDYYIENAENFLKPQHIKTkwteSY 91
Cdd:PLN02203 27 LEWRKSQLKGLLRLLKDNEEAIFK-------ALHQDLGKHRVEAYRdEVGVLTKSANLALSNLKKWMAPKKAKL----PL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 92 ITF--------EPIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESifnskklKFPIYknlsLES 163
Cdd:PLN02203 96 VAFpataevvpEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAA-------NIPKY----LDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 164 KFVADI----------IAHKHIKgVSLTGSEKAGKAVAQCAGQHLKKSVLELGGSAAFI---ICEDANLELATSIAVNAR 230
Cdd:PLN02203 165 KAVKVIeggpavgeqlLQHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 231 MQN-AGQSCIAAKRFLVhkslKEKFLSTFkskVEALKRG-DKFNAET--EIAEMAREDLAIELEKLVN--ESISLGAKVI 304
Cdd:PLN02203 244 WGScAGQACIAIDYVLV----EERFAPIL---IELLKSTiKKFFGENprESKSMARILNKKHFQRLSNllKDPRVAASIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 305 CGG--KREGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEF---IKSQTyrf 379
Cdd:PLN02203 317 HGGsiDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLkrrILSET--- 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1242547020 380 EEGAVYINEMLIS---DPhLPFGGVKNSGYGRELSQFGMYEFANIKTVV 425
Cdd:PLN02203 394 SSGSVTFNDAIIQyacDS-LPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
96-387 |
1.93e-16 |
|
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: 80.74 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 96 PIGVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVP-KSANLLESIFNSKKLKFPIYKNLSLESKFVADIIAHKH 174
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSiVMQIMVRLLHYAGLLPPEDVTLINGDGKTMQALLLHPN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 175 IKGVSLTGSEKAGKAVAQCAgqHLKKSVLELGGSAAFIICEDANL--ELATSIAVNARMQnAGQSCIAAKRFLVHKSL-K 251
Cdd:cd07084 180 PKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAvdYVAWQCVQDMTAC-SGQKCTAQSMLFVPENWsK 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 252 EKFLSTFKSKVE-------ALKRGDKFNAETEIAEMaREDLAIELEKLVNESISLGAKVICGGKREGAFYKPTilSEVTP 324
Cdd:cd07084 257 TPLVEKLKALLArrkledlLLGPVQTFTTLAMIAHM-ENLLGSVLLFSGKELKNHSIPSIYGACVASALFVPI--DEILK 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242547020 325 QMPVFREETFGPVAVVTFFETFDEA--VNLSNQSDFGLGVSIFSKDVEFIKSQTYRFE-EGAVYIN 387
Cdd:cd07084 334 TYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGRTYAI 399
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
163-405 |
1.96e-16 |
|
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: 81.09 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 163 SKFVADIIAHKHIKGVSLTGSEKAGKAVAQCAGQHLK------KSVLELGGSAAFIICEDANLELATSIAVNARMQNAGQ 236
Cdd:cd07123 237 PVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQ 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 237 SCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGD--KFNAETE--IAEMAREDLAIELEKLVNESislGAKVICGGK---R 309
Cdd:cd07123 317 KCSAASRAYVPESLWPEVKERLLEELKEIKMGDpdDFSNFMGavIDEKAFDRIKGYIDHAKSDP---EAEIIAGGKcddS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 310 EGAFYKPTILSEVTPQMPVFREETFGPVAVVTFFE--TFDEAVNLSNQ-SDFGLGVSIFSKDVEFIK--SQTYRFEEGAV 384
Cdd:cd07123 394 VGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPdsDFEETLELVDTtSPYALTGAIFAQDRKAIReaTDALRNAAGNF 473
|
250 260
....*....|....*....|....*..
gi 1242547020 385 YINEmlisDP------HLPFGGVKNSG 405
Cdd:cd07123 474 YIND----KPtgavvgQQPFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
15-407 |
6.66e-11 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 64.45 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTD-----LHAKAitsdmGKPISQSIAEVQKCAYLCDYYIENAEN-FLKPQHIKTKWT 88
Cdd:PRK11904 601 WSRTPVEERAAILERAADLLEANRAelialCVREA-----GKTLQDAIAEVREAVDFCRYYAAQARRlFGAPEKLPGPTG 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 89 ES-YITFEPIGVLLGVMPWNFP---FW-QvfrfVIPNLILGNLFIVK----------------HASNVPKSAnllesifn 147
Cdd:PRK11904 676 ESnELRLHGRGVFVCISPWNFPlaiFLgQ----VAAALAAGNTVIAKpaeqtpliaaeavkllHEAGIPKDV-------- 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 148 skkLKFpiyknLSLESKFV-ADIIAHKHIKGVSLTGS------------EKAGKAVAQCAgqhlkksvlELGGSAAFIIC 214
Cdd:PRK11904 744 ---LQL-----LPGDGATVgAALTADPRIAGVAFTGStetariinrtlaARDGPIVPLIA---------ETGGQNAMIVD 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 215 EDANLELATSIAVNARMQNAGQSCIAAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETE----IAEMAREDLAIELE 290
Cdd:PRK11904 807 STALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDvgpvIDAEAKANLDAHIE 886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 291 KLVNEsislgAKVIC-----GGKREGAFYKPTILsEVtPQMPVFREETFGPVA-VVTF-FETFDEAVNLSNQSDFGLGVS 363
Cdd:PRK11904 887 RMKRE-----ARLLAqlplpAGTENGHFVAPTAF-EI-DSISQLEREVFGPILhVIRYkASDLDKVIDAINATGYGLTLG 959
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1242547020 364 IFSKDVEFIKSQTYRFEEGAVYINEMLI-----SDphlPFGGVKNSGYG 407
Cdd:PRK11904 960 IHSRIEETADRIADRVRVGNVYVNRNQIgavvgVQ---PFGGQGLSGTG 1005
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
15-407 |
1.58e-10 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 63.35 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 15 WKEYSVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLCDYYIENAENFLKPQhiktkwtesyiTF 94
Cdd:PRK11905 606 WSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGP-----------GH 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 95 EPIGVLLGVMPWNFP---FW-QVfrfvIPNLILGNLFIVK----------------HASNVPKSAnllesifnskkLKFP 154
Cdd:PRK11905 675 KPLGPVVCISPWNFPlaiFTgQI----AAALVAGNTVLAKpaeqtpliaaravrllHEAGVPKDA-----------LQLL 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 155 IYKNLSLESKFVADiiahKHIKGVSLTGSEKAGKAVAQCAGQHLKKSVL---ELGGSAAFIICEDANLELATSIAVNARM 231
Cdd:PRK11905 740 PGDGRTVGAALVAD----PRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPEQVVADVIASAF 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 232 QNAGQSCiAAKRFL-VHKSLKEKFLSTFKSKVEALKRGDKFNAETE----IAEMAREdlaiELEKLVNESISLGAKV--- 303
Cdd:PRK11905 816 DSAGQRC-SALRVLcLQEDVADRVLTMLKGAMDELRIGDPWRLSTDvgpvIDAEAQA----NIEAHIEAMRAAGRLVhql 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 304 -ICGGKREGAFYKPTILsEVtPQMPVFREETFGPVA-VVTF-FETFDEAVNLSNQSDFGLGVSIFSKDVEFIKSQTYRFE 380
Cdd:PRK11905 891 pLPAETEKGTFVAPTLI-EI-DSISDLEREVFGPVLhVVRFkADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIR 968
|
410 420 430
....*....|....*....|....*....|..
gi 1242547020 381 EGAVYINEMLI-----SDphlPFGGVKNSGYG 407
Cdd:PRK11905 969 AGNIYVNRNIIgavvgVQ---PFGGEGLSGTG 997
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
98-372 |
5.37e-08 |
|
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: 54.97 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 98 GVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNvpkSANLLE----SIFNSKKLkfPiYKNLSLESKFVADIIAH- 172
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATA---TAYLTEavvkDIVESGLL--P-EGALQLICGSVGDLLDHl 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 173 KHIKGVSLTGSekagKAVAQCAGQH---LKKSV---LELGGSAAFIICEDANL---ELATSIAVNAR-M-QNAGQSCIAA 241
Cdd:cd07128 220 GEQDVVAFTGS----AATAAKLRAHpniVARSIrfnAEADSLNAAILGPDATPgtpEFDLFVKEVAReMtVKAGQKCTAI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 242 KRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMA----REDLAIELEKLVNES-ISLGAKV---ICGGKRE-GA 312
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVsreqREDVRAAVATLLAEAeVVFGGPDrfeVVGADAEkGA 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1242547020 313 FYKPTILSEVTP-QMPVFRE-ETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFI 372
Cdd:cd07128 376 FFPPTLLLCDDPdAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFA 437
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
98-372 |
1.88e-04 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 43.54 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 98 GVLLGVMPWNFPFWQVFRFVIPNLILGNLFIVKHASNVPKSANLLESIFNSKKLkFPiYKNLSLESKFVADIIAHkhIKG 177
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGI-LP-AGALSVVCGSSAGLLDH--LQP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 178 ---VSLTGSE------KAGKAVAQCA------GQHLKKSVL---ELGGSAAFiicedanlELATSIAVNARMQNAGQSCI 239
Cdd:PRK11903 226 fdvVSFTGSAetaavlRSHPAVVQRSvrvnveADSLNSALLgpdAAPGSEAF--------DLFVKEVVREMTVKSGQKCT 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 240 AAKRFLVHKSLKEKFLSTFKSKVEALKRGDKFNAETEIAEMA-REDLAIELEKLvnESISLGAKVICGGKRE-------- 310
Cdd:PRK11903 298 AIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVsRAQLAAVRAGL--AALRAQAEVLFDGGGFalvdadpa 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242547020 311 -GAFYKPTIL--SEVTPQMPVFREETFGPVAVVTFFETFDEAVNLSNQSDFGLGVSIFSKDVEFI 372
Cdd:PRK11903 376 vAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFL 440
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
19-266 |
2.53e-04 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 42.98 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 19 SVIQRIEIIKDIKDNLLKNTDLHAKAITSDMGKPISQSIAEVQKCAYLC-DYYIENAENFL----KPQHIKTKWT----E 89
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSeSKLYKNIDTERgitaSVGHIQDVLLpdngE 93
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 90 SYITFEPIGVLLGVMPWNFPFWQVFRFVIpNLILGNLFIVKHASNVPKSANLLESIFNSKKLKFPIyKNLSL-----ESK 164
Cdd:cd07077 94 TYVRAFPIGVTMHILPSTNPLSGITSALR-GIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGP-KILVLyvphpSDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242547020 165 FVADIIAHKHIKGVSLTGSEKAGKAvAQCAGQHlkKSVLELG-GSAAFIICEDANLELATSIAVNARMQNaGQSCIAAKR 243
Cdd:cd07077 172 LAEELLSHPKIDLIVATGGRDAVDA-AVKHSPH--IPVIGFGaGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQN 247
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250 260
....*....|....*....|....*
gi 1242547020 244 FLVHKSLKEKFLSTFKSK--VEALK 266
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLKlvVEGLK 272
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|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
213-255 |
7.71e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 38.51 E-value: 7.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1242547020 213 IC-----EDANLELATSIAVNARMQNAGqSCIAAKRFLVHKSLKEKFL 255
Cdd:PRK00197 228 IChiyvdESADLDKALKIVLNAKTQRPS-VCNALETLLVHEAIAEEFL 274
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