|
Name |
Accession |
Description |
Interval |
E-value |
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
1-487 |
0e+00 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 935.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 1 MTLWINGDWITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELT 80
Cdd:PRK09457 1 MTLWINGDWIAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 81 AIIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALL 160
Cdd:PRK09457 81 EVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 161 AGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKIL 240
Cdd:PRK09457 161 AGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 241 ALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQGDAFLARLVAVSQRLTPGNWDDEPQPFIGG 320
Cdd:PRK09457 241 ALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPFMGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 321 LISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTR 400
Cdd:PRK09457 321 VISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 401 FGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYAADYCAWPMASLESDSLTLPATL 480
Cdd:PRK09457 401 FGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGASGNHRPSAYYAADYCAYPMASLESDSLTLPATL 480
|
....*..
gi 16129700 481 NPGLDFS 487
Cdd:PRK09457 481 SPGLDFS 487
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
3-486 |
0e+00 |
|
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 274486 Cd Length: 484 Bit Score: 929.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAI 82
Cdd:TIGR03240 1 LFIDGKWRAGQGESFASRNPATQEVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 83 IARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAG 162
Cdd:TIGR03240 81 IARETGKPLWETRTEVASMIGKVAISIKAYHERTGESENPMPDGRAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 163 NTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKILAL 242
Cdd:TIGR03240 161 NTVVFKPSELTPWVAEETVKLWEKAGLPAGVLNLVQGARETGVALAAHPQIDGLLFTGSSNTGTLLHRQFGGRPEKILAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 243 EMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQGDAFLARLVAVSQRLTPGNWDDEPQPFIGGLI 322
Cdd:TIGR03240 241 EMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRLLVPDGAQGDAFLARLVEVAERLTVGAWDAEPQPFMGAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 323 SEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFG 402
Cdd:TIGR03240 321 SLRAAQRLLAAQAKLLALGGKSLLEMRQLDPGAAFLTPGIIDVTGVAELPDEEHFGPLLQVIRYTDFDEAIAIANNTRFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 403 LSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYAADYCAWPMASLESDSLTLPATLNP 482
Cdd:TIGR03240 401 LSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGASSAAPFGGIGASGNHRPSAYYAADYCAYPVASLEADSLTLPATLSP 480
|
....
gi 16129700 483 GLDF 486
Cdd:TIGR03240 481 GLKF 484
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
38-469 |
0e+00 |
|
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: 765.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 38 QVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAMINKIAISIKAYHVRTG 117
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 118 EQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLV 197
Cdd:cd07095 81 ERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 198 QGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRC 277
Cdd:cd07095 161 QGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 278 TCARRLLLKSGAQGDAFLARLVAVSQRLTPGNWDDEPQPFiGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSL 357
Cdd:cd07095 241 TCARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFM-GPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 358 LTPGIIEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAA 437
Cdd:cd07095 320 LSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGAS 399
|
410 420 430
....*....|....*....|....*....|..
gi 16129700 438 STAPFGGIGASGNHRPSAWYAADYCAWPMASL 469
Cdd:cd07095 400 STAPFGGVGLSGNHRPSAYYAADYCAYPVASL 431
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
3-460 |
1.21e-153 |
|
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: 446.11 E-value: 1.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:COG1012 8 LFIGGEWVAAASGETFDvINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQR-SEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALL 160
Cdd:COG1012 88 LLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIpSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 161 AGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQlSGQPEKI 239
Cdd:COG1012 168 AGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA-AAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 240 LALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIG 319
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIY-DEFVERLVAAAKALKVGDPLD-PGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 320 GLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQ-AGTSLLTPGIIemTGV---AGVPDEEVFGPLLRVWRYDTFDEAIRM 395
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTGGRRPDgEGGYFVEPTVL--ADVtpdMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129700 396 ANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYAAD 460
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLE 467
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
9-452 |
1.80e-145 |
|
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: 424.64 E-value: 1.80e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 9 WITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETG 88
Cdd:pfam00171 1 WVDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 89 KPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFK 168
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 169 PSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQlSGQPEKILALEMGGN 247
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEA-AAQNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 248 NPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNwDDEPQPFIGGLISEQAA 327
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIY-DEFVEKLVEAAKKLKVGD-PLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 328 QQVVTAWQQLEAMGGrpllapRLLQAGTSLLTPG-IIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTR 400
Cdd:pfam00171 318 ERVLKYVEDAKEEGA------KLLTGGEAGLDNGyFVEPTVLANVTPdmriaqEEIFGPVLSVIRFKDEEEAIEIANDTE 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16129700 401 FGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHR 452
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGR 443
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
40-464 |
3.67e-143 |
|
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: 417.76 E-value: 3.67e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 40 EQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQ 119
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 120 R-SEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQ 198
Cdd:cd07078 81 IpSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 199 G-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPeKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRC 277
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL-KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 278 TCARRLLLKSGaQGDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLL-APRLLQAGTS 356
Cdd:cd07078 240 TAASRLLVHES-IYDEFVERLVERVKALKVGNPLD-PDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCgGKRLEGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 357 LLTPGIIEMTGVA-GVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTG 435
Cdd:cd07078 318 FVPPTVLTDVDPDmPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|
gi 16129700 436 AASTAPFGGIGASGNHRP-SAWYAADYCAW 464
Cdd:cd07078 398 AEPSAPFGGVKQSGIGREgGPYGLEEYTEP 427
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
44-460 |
2.06e-116 |
|
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: 346.91 E-value: 2.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 44 RAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAMINKIAISIK-AYHVRTGEQRSE 122
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGlADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 123 MPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GR 201
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 202 ETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPeKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCAR 281
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL-KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 282 RLLLKSGaQGDAFLARLVAVsqrLTPGNWDDEpqpfiggliseqaaqqvvtawqqleamggrpllaprllqagtslltpg 361
Cdd:cd06534 240 RLLVHES-IYDEFVEKLVTV---LVDVDPDMP------------------------------------------------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 362 iiemtgvagVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAP 441
Cdd:cd06534 268 ---------IAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAP 338
|
410
....*....|....*....
gi 16129700 442 FGGIGASGNHRPSAWYAAD 460
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLE 357
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
5-459 |
6.18e-107 |
|
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: 326.61 E-value: 6.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDWITGQGASRV-KRNPVSG-EVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAI 82
Cdd:cd07131 3 IGGEWVDSASGETFdSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 83 IARETGKPRWEAATEVTAMINKiaisikAYHVrTGEQR--------SEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGH 154
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDM------AQYA-AGEGRrlfgetvpSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 155 IVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLhRQLS 233
Cdd:cd07131 156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERI-GETC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 234 GQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDe 313
Cdd:cd07131 235 ARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVY-DEFLKRFVERAKRLRVGDGLD- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 314 PQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSL----LTPGIIEM-TGVAGVPDEEVFGPLLRVWRYDT 388
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEkgyfVEPTVFTDvTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129700 389 FDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYAA 459
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNGHREAGTTA 463
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
5-464 |
1.40e-103 |
|
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: 317.97 E-value: 1.40e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDWITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIA 84
Cdd:cd07086 3 IGGEWVGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 85 RETGKPRWEAATEVTAMINkiaisIKAYHVrtGEQR--------SEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIV 156
Cdd:cd07086 83 LEMGKILPEGLGEVQEMID-----ICDYAV--GLSRmlygltipSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 157 PALLAGNTIIFKPSELTPWSGEAVMRLWQQA----GLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLhRQL 232
Cdd:cd07086 156 IALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRV-GET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 233 SGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGN-WD 311
Cdd:cd07086 235 VARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVY-DEFLERLVKAYKQVRIGDpLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 312 DEpqPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTS--LLTPGIIEM-TGVAGVPDEEVFGPLLRVWRYDT 388
Cdd:cd07086 314 EG--TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPgnYVEPTIVTGvTDDARIVQEETFAPILYVIKFDS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 389 FDEAIRMANNTRFGLSCGLVSP---EREKF-DQLLLEarAGIVNWNKPLTGAASTAPFGGIGASGNHRPS---AWYAadY 461
Cdd:cd07086 392 LEEAIAINNDVPQGLSSSIFTEdlrEAFRWlGPKGSD--CGIVNVNIPTSGAEIGGAFGGEKETGGGRESgsdAWKQ--Y 467
|
...
gi 16129700 462 CAW 464
Cdd:cd07086 468 MRR 470
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
4-461 |
7.30e-100 |
|
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: 308.41 E-value: 7.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 4 WINGDWITGqGASRVKRNPVS-GEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAI 82
Cdd:cd07097 4 YIDGEWVAG-GDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 83 IARETGKPRWEAATEVTAminkiAISIKAYHV-----RTGE-QRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIV 156
Cdd:cd07097 83 LTREEGKTLPEARGEVTR-----AGQIFRYYAgealrLSGEtLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 157 PALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQ 235
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 236 PEKIlALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPQ 315
Cdd:cd07097 238 GARV-QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIH-DRFVEALVERTKALKVGDALDEGV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 316 PfIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTS--LLTPGII-----EMTgvagVPDEEVFGPLLRVWRYDT 388
Cdd:cd07097 316 D-IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEgyYLAPALFagvtnDMR----IAREEIFGPVAAVIRVRD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129700 389 FDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNH-RPSAWYAADY 461
Cdd:cd07097 391 YDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHVPFGGRKGSSYGpREQGEAALEF 464
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
3-449 |
2.32e-97 |
|
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: 302.99 E-value: 2.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVkRNPV-SGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:cd07124 35 LVIGGKEVRTEEKIES-RNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPRWEAATEVTAminkiAISIKAYHVR-----TGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIV 156
Cdd:cd07124 114 WMVLEVGKNWAEADADVAE-----AIDFLEYYARemlrlRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 157 PALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLS-- 233
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGpGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 234 --GQPE-KILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNw 310
Cdd:cd07124 269 qpGQKWlKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVY-DEFLERLVERTKALKVGD- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 311 DDEPQPFIGGLISEQAAQQVVTAWQQLEAMGgrpllapRLLQAG--TSLLTPG-IIEMTGVAGVP------DEEVFGPLL 381
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-------RLLLGGevLELAAEGyFVQPTIFADVPpdhrlaQEEIFGPVL 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129700 382 RVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTA-PFGGIGASG 449
Cdd:cd07124 420 AVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRqPFGGFKMSG 488
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
20-449 |
2.46e-92 |
|
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: 287.97 E-value: 2.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 20 RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVT 99
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMIN------KIAISIKAYHVRTGeqRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELT 173
Cdd:cd07099 81 LALEaidwaaRNAPRVLAPRKVPT--GLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 174 PWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSAlEDLDGLLFTGSANTGyqlhRQLSGQPEKIL---ALEMGGNNPL 250
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALID-AGVDKVAFTGSVATG----RKVMAAAAERLipvVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 251 IIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGnWDDEPQPFIGGLISeqaAQQV 330
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVY-DEFVARLVAKARALRPG-ADDIGDADIGPMTT---ARQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 331 VTAWQQLE---AMGGRPLLAPRLLQAGTSLLTPgiiemTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRF 401
Cdd:cd07099 309 DIVRRHVDdavAKGAKALTGGARSNGGGPFYEP-----TVLTDVPHdmdvmrEETFGPVLPVMPVADEDEAIALANDSRY 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16129700 402 GLSCGLVSPEREKFDQLLLEARAGIVNWNKPL-TGAASTAPFGGIGASG 449
Cdd:cd07099 384 GLSASVFSRDLARAEAIARRLEAGAVSINDVLlTAGIPALPFGGVKDSG 432
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
17-449 |
5.03e-87 |
|
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: 274.21 E-value: 5.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 17 RVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAAT 96
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 97 EVTAMINKI-AISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPW 175
Cdd:cd07150 81 ETTFTPELLrAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 176 SGEAVMRLWQQAGLPPGVLNLVQGGR-ETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKIlALEMGGNNPLIIDE 254
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGaEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKI-TLELGGKNPLIVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 255 VADIDAAVHLTIQSAFVTAGQRCTCARRLLLkSGAQGDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQVVTAW 334
Cdd:cd07150 240 DADLDYAVRAAAFGAFMHQGQICMSASRIIV-EEPVYDEFVKKFVARASKLKVGDPRD-PDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 335 QQLEAMGGrpllapRLLQAGTSllTPGIIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLV 408
Cdd:cd07150 318 EDAVAKGA------KLLTGGKY--DGNFYQPTVLTDVTPdmrifrEETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16129700 409 SPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASG 449
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASG 430
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
16-449 |
3.09e-85 |
|
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: 271.76 E-value: 3.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 16 SRVKRNPVSGEVLwqgnDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAA 95
Cdd:cd07125 52 DPADHERTIGEVS----LADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 96 TEVtaminKIAISIKAYHVRTGEQRSEMPDGAAS------LRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKP 169
Cdd:cd07125 128 AEV-----REAIDFCRYYAAQARELFSDPELPGPtgelngLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 170 SELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKILAL--EMGG 246
Cdd:cd07125 203 AEQTPLIAARAVELLHEAGVPRDVLQLVPGdGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLiaETGG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 247 NNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLksgaQGD---AFLARLVAVSQRLTPGN-WDdePQPFIGGLI 322
Cdd:cd07125 283 KNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYL----QEEiaeRFIEMLKGAMASLKVGDpWD--LSTDVGPLI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 323 sEQAAQQVVTAWQQLEAMGGRpLLAPRLLQAGT-SLLTPGIIEMTGVaGVPDEEVFGPLLRVWRYD--TFDEAIRMANNT 399
Cdd:cd07125 357 -DKPAGKLLRAHTELMRGEAW-LIAPAPLDDGNgYFVAPGIIEIVGI-FDLTTEVFGPILHVIRFKaeDLDEAIEDINAT 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16129700 400 RFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTA-PFGGIGASG 449
Cdd:cd07125 434 GYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRqPFGGWGLSG 484
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
21-461 |
1.21e-84 |
|
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: 268.28 E-value: 1.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATevta 100
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 minkIAISIKAYHVR--------TGEQRSEMPDGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSE 171
Cdd:cd07093 79 ----RDIPRAAANFRffadyilqLDGESYPQDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 172 LTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKiLALEMGGNNPL 250
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKP-VSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 251 IIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQV 330
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIY-DEFLERFVERAKALKVGDPLD-PDTEVGPLISKEHLEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 331 VTAWQQLEAMGGRPLL----APRLLQAGTSLLTPGIIemtgvAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTR 400
Cdd:cd07093 312 LGYVELARAEGATILTgggrPELPDLEGGYFVEPTVI-----TGLDNdsrvaqEEIFGPVVTVIPFDDEEEAIELANDTP 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129700 401 FGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTaPFGGIGASGNHRPSAWYAADY 461
Cdd:cd07093 387 YGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRT-PFGGVKASGIGREGGDYSLEF 446
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
21-449 |
1.43e-84 |
|
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: 267.76 E-value: 1.43e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTA 100
Cdd:cd07103 3 NPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 MINKI---AISIKAYHVRTGEqrSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSG 177
Cdd:cd07103 83 AASFLewfAEEARRIYGRTIP--SPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 178 EAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQlSGQPEKILALEMGGNNPLIIDEVA 256
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMAQ-AADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 257 DIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGN-WDDEPQpfIGGLISEQAAQQVVTAWQ 335
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIY-DEFVEKLVERVKKLKVGNgLDEGTD--MGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 336 QLEAMGGRPLLAPRLLQAGTSLLTPgiiemTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVS 409
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGYFYEP-----TVLTDVTDdmlimnEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16129700 410 PEREKFDQLLLEARAGIVNWNKPLTGAAStAPFGGIGASG 449
Cdd:cd07103 392 RDLARAWRVAEALEAGMVGINTGLISDAE-APFGGVKESG 430
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
39-449 |
1.31e-83 |
|
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: 264.78 E-value: 1.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 39 VEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAMINKI--AISIkAYHVRT 116
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILreAAGL-PRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 117 GEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVM-RLWQQAGLPPGVLN 195
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 196 LVQGGR-ETGQALSALEDLDGLLFTGSANTGYQLHRqLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAG 274
Cdd:cd07104 161 VVPGGGsEIGDALVEHPRVRMISFTGSTAVGRHIGE-LAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 275 QRCTCARRLLL-KSGAqgDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQVVTAWQQLEAMGGrpllapRLLQA 353
Cdd:cd07104 240 QICMAAGRILVhESVY--DEFVEKLVAKAKALPVGDPRD-PDTVIGPLINERQVDRVHAIVEDAVAAGA------RLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 354 GTS---LLTPGIIemTGV-AGVP--DEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIV 427
Cdd:cd07104 311 GTYeglFYQPTVL--SDVtPDMPifREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMV 388
|
410 420
....*....|....*....|..
gi 16129700 428 NWNKPLTGAASTAPFGGIGASG 449
Cdd:cd07104 389 HINDQTVNDEPHVPFGGVKASG 410
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
14-464 |
9.21e-83 |
|
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: 263.69 E-value: 9.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 14 GASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFP--RWARLSFAERHAVVERFAALLESNKAELTAIIARETGKP- 90
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 91 RWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPS 170
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 171 ELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRqLSGQPE-KILALEMGGNN 248
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLE-YSGQSNlKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 249 PLII-DEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAA 327
Cdd:cd07112 240 PNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIK-DEFLEKVVAAAREWKPGDPLD-PATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 328 QQVVTAWQQLEAMGGrpllapRLLQAGTSLLTPG---IIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANN 398
Cdd:cd07112 318 DKVLGYIESGKAEGA------RLVAGGKRVLTETggfFVEPTVFDGVTPdmriarEEIFGPVLSVITFDSEEEAVALAND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129700 399 TRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTaPFGGIGASGNHRPSAWYAAD-YCAW 464
Cdd:cd07112 392 SVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITT-PFGGFKQSGNGRDKSLHALDkYTEL 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
21-449 |
2.34e-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: 262.08 E-value: 2.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTA 100
Cdd:cd07106 3 NPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 MIN------KIAISIKAYHvrtgeqrsEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTP 174
Cdd:cd07106 83 AVAwlrytaSLDLPDEVIE--------DDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 175 WSGEAVMRLWQQAgLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQpEKILALEMGGNNPLIIDE 254
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKT-LKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 255 VADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSgAQGDAFLARLVAVSQRLTPGNwDDEPQPFIGGLiseQAAQQ---VV 331
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHE-SIYDEFCEALVALAKAAVVGD-GLDPGTTLGPV---QNKMQydkVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 332 TAWQQLEAMGGRPLLaprllqAGTSLLTPG-IIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLS 404
Cdd:cd07106 308 ELVEDAKAKGAKVLA------GGEPLDGPGyFIPPTIVDDPPEgsrivdEEQFGPVLPVLKYSDEDEVIARANDSEYGLG 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 16129700 405 CGLVSPEREKFDQLLLEARAGIVNWNKPlTGAASTAPFGGIGASG 449
Cdd:cd07106 382 ASVWSSDLERAEAVARRLEAGTVWINTH-GALDPDAPFGGHKQSG 425
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
21-459 |
1.54e-80 |
|
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: 257.75 E-value: 1.54e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTA 100
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 MINKIAISiKAYHVRTGEQRSEMPDGAAS------LRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTP 174
Cdd:cd07094 85 AIDTLRLA-AEEAERIRGEEIPLDATQGSdnrlawTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 175 WSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGqpeKILALEMGGNNPLIID 253
Cdd:cd07094 164 LSALELAKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG---KRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 254 EVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEpQPFIGGLISEQAAQQVVTA 333
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELY-DEFIEAFVAAVKKLKVGDPLDE-DTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 334 WQQLEAMGGRPLLAPRLLQAgtsLLTPGIIEMTGV-AGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPER 412
Cdd:cd07094 319 VEEAVEAGARLLCGGERDGA---LFKPTVLEDVPRdTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16129700 413 EKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYAA 459
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAM 442
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
4-452 |
1.09e-79 |
|
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: 256.47 E-value: 1.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 4 WINGDWITG-QGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAF--PRWARLSFAERHAVVERFAALLESNKAELT 80
Cdd:cd07119 1 YIDGEWVEAaSGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 81 AIIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALL 160
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 161 AGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKI 239
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 240 lALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIG 319
Cdd:cd07119 241 -ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIH-DKFVAALAERAKKIKLGNGLD-ADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 320 GLISEQAAQQVVTAWQ-------QLEAMGGRPllAPRLLQAGtSLLTPGII-EMTGVAGVPDEEVFGPLLRVWRYDTFDE 391
Cdd:cd07119 318 PLVSAEHREKVLSYIQlgkeegaRLVCGGKRP--TGDELAKG-YFVEPTIFdDVDRTMRIVQEEIFGPVLTVERFDTEEE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129700 392 AIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASGNHR 452
Cdd:cd07119 395 AIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTV-WINDYHPYFAEAPWGGYKQSGIGR 454
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
20-458 |
1.47e-79 |
|
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: 255.21 E-value: 1.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 20 RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVT 99
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINKIAISIKAYHVRTGEQrseMP-DGAASLRHR-------PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSE 171
Cdd:cd07149 84 RAIETLRLSAEEAKRLAGET---IPfDASPGGEGRigftirePIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 172 LTPWSGEAVMRLWQQAGLPPGVLNLVQGGRET-GQALSALEDLDGLLFTGSANTGYQLHRQlsgQPEKILALEMGGNNPL 250
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETvGDALVTDPRVRMISFTGSPAVGEAIARK---AGLKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 251 IIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEpQPFIGGLISEQAAQQV 330
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIY-DEFLERFVAATKKLVVGDPLDE-DTDVGPMISEAEAERI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 331 VtAWQQlEAMggrpllaprllQAGTSLLTPG-----IIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNT 399
Cdd:cd07149 316 E-EWVE-EAV-----------EGGARLLTGGkrdgaILEPTVLTDVPPdmkvvcEEVFAPVVSLNPFDTLDEAIAMANDS 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129700 400 RFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYA 458
Cdd:cd07149 383 PYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGREGPRYA 441
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
5-404 |
3.08e-79 |
|
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: 254.50 E-value: 3.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDWITGQ-GASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAII 83
Cdd:cd07088 2 INGEFVPSSsGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 84 ARETGKPRWEAATEVTAminkiAISIKAYHV---RTGEQR---SEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVP 157
Cdd:cd07088 82 VEEQGKTLSLARVEVEF-----TADYIDYMAewaRRIEGEiipSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 158 ALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQP 236
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 237 EKiLALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEpQP 316
Cdd:cd07088 237 TK-VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIY-DEFMEKLVEKMKAVKVGDPFDA-AT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 317 FIGGLISEQAAQQVvtawqqlEAMggrpllAPRLLQAGTSLLTPGII---------EMTGVAGV-PD-----EEVFGPLL 381
Cdd:cd07088 314 DMGPLVNEAALDKV-------EEM------VERAVEAGATLLTGGKRpegekgyfyEPTVLTNVrQDmeivqEEIFGPVL 380
|
410 420
....*....|....*....|...
gi 16129700 382 RVWRYDTFDEAIRMANNTRFGLS 404
Cdd:cd07088 381 PVVKFSSLDEAIELANDSEYGLT 403
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
3-402 |
5.85e-78 |
|
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: 251.67 E-value: 5.85e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:cd07085 3 LFINGEWVESKTTEWLDvYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDG--AASLRhRPHGVLAVFGPYNFPGHLPNGHIVPAL 159
Cdd:cd07085 83 LITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGidTYSYR-QPLGVVAGITPFNFPAMIPLWMFPMAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 160 LAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKI 239
Cdd:cd07085 162 ACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 240 LALeMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTcARRLLLKSGAQGDAFLARLVAVSQRLTPGNWDDePQPFIG 319
Cdd:cd07085 242 QAL-GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCM-ALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD-PGADMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 320 GLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQA---------GTSLLTPGIIEMTgvagVPDEEVFGPLLRVWRYDTFD 390
Cdd:cd07085 319 PVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVpgyengnfvGPTILDNVTPDMK----IYKEEIFGPVLSIVRVDTLD 394
|
410
....*....|..
gi 16129700 391 EAIRMANNTRFG 402
Cdd:cd07085 395 EAIAIINANPYG 406
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
3-452 |
9.45e-78 |
|
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: 250.88 E-value: 9.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:cd07138 1 FYIDGAWVAPAGTETIDvINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPRWEA-ATEVTAMINKIAISIKAyhVRTGEQRSEMpdGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALL 160
Cdd:cd07138 81 AITLEMGAPITLArAAQVGLGIGHLRAAADA--LKDFEFEERR--GNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 161 AGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHrQLSGQPEKI 239
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVSFTGSTRAGKRVA-EAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 240 LALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSgAQGDAFLARLVAVSQRLTPGNWDDePQPFIG 319
Cdd:cd07138 236 VALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPR-SRYAEAEEIAAAAAEAYVVGDPRD-PATTLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 320 GLISEQAAQQVVTAWQQLEAMGGRpLLA-----PRLLQAG-----T--SLLTPgiiEMTgvagVPDEEVFGPLLRVWRYD 387
Cdd:cd07138 314 PLASAAQFDRVQGYIQKGIEEGAR-LVAggpgrPEGLERGyfvkpTvfADVTP---DMT----IAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129700 388 TFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNkpltGAA--STAPFGGIGASGNHR 452
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAfnPGAPFGGYKQSGNGR 448
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
25-450 |
4.40e-75 |
|
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: 242.97 E-value: 4.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 25 GEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVtamink 104
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 105 iAISIKAYHVRTG---EQRSEM---PDGAASL-RHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSG 177
Cdd:cd07152 75 -GAAIGELHEAAGlptQPQGEIlpsAPGRLSLaRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 178 EAVM-RLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKIlALEMGGNNPLIIDEVA 256
Cdd:cd07152 154 GVVIaRLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKV-SLELGGKNALIVLDDA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 257 DIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAqGDAFLARLVAVSQRLTPGNWDDEpQPFIGGLISEQAAQQV---VTA 333
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICMAAGRHLVHESV-ADAYTAKLAAKAKHLPVGDPATG-QVALGPLINARQLDRVhaiVDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 334 WQQLEAmggrpllapRLLQAGTS---LLTPGIIemTGV-AGVP--DEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGL 407
Cdd:cd07152 311 SVAAGA---------RLEAGGTYdglFYRPTVL--SGVkPGMPafDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGI 379
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 16129700 408 VSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGN 450
Cdd:cd07152 380 ISRDVGRAMALADRLRTGMLHINDQTVNDEPHNPFGGMGASGN 422
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
21-449 |
2.90e-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: 241.44 E-value: 2.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTA 100
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 MIN------KIAISIKAYHVrtgeqrsEMPDGA-ASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELT 173
Cdd:cd07090 83 SADcleyyaGLAPTLSGEHV-------PLPGGSfAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 174 PWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPeKILALEMGGNNPLIID 253
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI-KHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 254 EVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEpQPFIGGLISEQAAQQVVTA 333
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIK-DEFTERLVERTKKIRIGDPLDE-DTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 334 WQQLEAMGGRPL-----LAPRLLQAGTSLLTPGII-----EMTGVagvpDEEVFGPLLRVWRYDTFDEAIRMANNTRFGL 403
Cdd:cd07090 313 IESAKQEGAKVLcggerVVPEDGLENGFYVSPCVLtdctdDMTIV----REEIFGPVMSILPFDTEEEVIRRANDTTYGL 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16129700 404 SCGLVSPEREKFDQLLLEARAGIV---NWNKpltgAASTAPFGGIGASG 449
Cdd:cd07090 389 AAGVFTRDLQRAHRVIAQLQAGTCwinTYNI----SPVEVPFGGYKQSG 433
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
21-452 |
4.25e-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: 240.99 E-value: 4.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWA-RLSFAERHAVVERFAALLESNKAELTAIIARETGKPRweaaTEVT 99
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPV----MTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINKIAISIKAY---HVRTGEQRSEMPDGA-------ASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKP 169
Cdd:cd07089 79 AMQVDGPIGHLRYfadLADSFPWEFDLPVPAlrggpgrRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 170 SELTPWSGEAVMRLWQQAGLPPGVLNLVQGG-RETGQALSALEDLDGLLFTGSANTGYQLHRQlSGQPEKILALEMGGNN 248
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSdNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQ-AAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 249 PLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQ 328
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRY-DEVVEALAAAFEALPVGDPAD-PGTVMGPLISAAQRD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 329 QVVTAWQQLEAMGGrpllapRLLQAGTSL--LTPGI-IEMTGVAGV-PD-----EEVFGPLLRVWRYDTFDEAIRMANNT 399
Cdd:cd07089 316 RVEGYIARGRDEGA------RLVTGGGRPagLDKGFyVEPTLFADVdNDmriaqEEIFGPVLVVIPYDDDDEAVRIANDS 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16129700 400 RFGLSCGLVSPEREKFDQLLLEARAGIVNWNkPLTGAASTAPFGGIGASGNHR 452
Cdd:cd07089 390 DYGLSGGVWSADVDRAYRVARRIRTGSVGIN-GGGGYGPDAPFGGYKQSGLGR 441
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
5-449 |
3.94e-73 |
|
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: 239.01 E-value: 3.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDWITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWAR-LSFAERHAVVERFAALLESNKAELTAII 83
Cdd:cd07082 6 INGEWKESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 84 ARETGKPRWEAATEVTAMINKIAISIKAY-----HVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPA 158
Cdd:cd07082 86 MWEIGKTLKDALKEVDRTIDYIRDTIEELkrldgDSLPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 159 LLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPe 237
Cdd:cd07082 166 LIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKR- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 238 kiLALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGN-WDDEPQp 316
Cdd:cd07082 245 --LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVA-DELVELLKEEVAKLKVGMpWDNGVD- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 317 fIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRllQAGTSLLTPGIIE-MTGVAGVPDEEVFGPLLRVWRYDTFDEAIRM 395
Cdd:cd07082 321 -ITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDpVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129700 396 ANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWN-KPLTGAASTaPFGGIGASG 449
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINsKCQRGPDHF-PFLGRKDSG 451
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
3-449 |
6.40e-73 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 239.45 E-value: 6.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGaSRVKRNPVS-GEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:PRK03137 39 LIIGGERITTED-KIVSINPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPRWEAATEVTAminkiAISIKAYHVRT------GEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHI 155
Cdd:PRK03137 118 WLVKEAGKPWAEADADTAE-----AIDFLEYYARQmlkladGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 156 VPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLH-RQLS 233
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREVGLRIYeRAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 234 GQPEKI----LALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGN 309
Cdd:PRK03137 273 VQPGQIwlkrVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVY-DEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 310 WDDepQPFIGGLISEQAAQQVVTAWQQLEAMGgrpllapRLLQAGTSLLTPG-IIEMTGVAGVP------DEEVFGPLLR 382
Cdd:PRK03137 352 PED--NAYMGPVINQASFDKIMSYIEIGKEEG-------RLVLGGEGDDSKGyFIQPTIFADVDpkarimQEEIFGPVVA 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129700 383 VWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAAS-TAPFGGIGASG 449
Cdd:PRK03137 423 FIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVgYHPFGGFNMSG 490
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-449 |
9.04e-73 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 238.82 E-value: 9.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAII 83
Cdd:PLN02278 29 IGGKWTDAYDGKTFPvYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 84 ARETGKPRWEAATEVTaminkIAISIKAYHVRTGEQ------RSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVP 157
Cdd:PLN02278 109 TLEQGKPLKEAIGEVA-----YGASFLEYFAEEAKRvygdiiPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 158 ALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQlSGQP 236
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGdAPEIGDALLASPKVRKITFTGSTAVGKKLMAG-AAAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 237 EKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNwDDEPQP 316
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIY-DKFAEAFSKAVQKLVVGD-GFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 317 FIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGII-EMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRM 395
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLgDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16129700 396 ANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAAStAPFGGIGASG 449
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV-APFGGVKQSG 473
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
21-449 |
1.13e-72 |
|
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: 237.25 E-value: 1.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTA 100
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 minkiAISIKAYHVRTGEQRS---------EMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSE 171
Cdd:cd07110 83 -----VAGCFEYYADLAEQLDakaeravplPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 172 LTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSgQPEKILALEMGGNNPL 250
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGtGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 251 IIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAqGDAFLARLVAVSQRLTPGNwDDEPQPFIGGLISEQAAQQV 330
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESI-ADAFLERLATAAEAIRVGD-PLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 331 VTAWQQLEAMGGRPLLAPRLLQAgtslLTPG-IIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGL 403
Cdd:cd07110 315 LSFIARGKEEGARLLCGGRRPAH----LEKGyFIAPTVFADVPTdsriwrEEIFGPVLCVRSFATEDEAIALANDSEYGL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 16129700 404 SCGLVSPEREKFDQLLLEARAGIVNWNKPlTGAASTAPFGGIGASG 449
Cdd:cd07110 391 AAAVISRDAERCDRVAEALEAGIVWINCS-QPCFPQAPWGGYKRSG 435
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
21-460 |
5.55e-72 |
|
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: 235.41 E-value: 5.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAAtevta 100
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 mINKIAISIKAYHVRTGEQR----SEMPDGAASL---RHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELT 173
Cdd:cd07115 78 -RLDVPRAADTFRYYAGWADkiegEVIPVRGPFLnytVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 174 PWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKIlALEMGGNNPLII 252
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRV-SLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 253 DEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQVVT 332
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIY-DEFLERFTSLARSLRPGDPLD-PKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 333 AWQQLEAMGGrpllapRLLQAGTSLLTPG-IIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSC 405
Cdd:cd07115 314 YVDVGREEGA------RLLTGGKRPGARGfFVEPTIFAAVPPemriaqEEIFGPVVSVMRFRDEEEALRIANGTEYGLAA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129700 406 GLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASGNHRPSAWYAAD 460
Cdd:cd07115 388 GVWTRDLGRAHRVAAALKAGTV-WINTYNRFDPGSPFGGYKQSGFGREMGREALD 441
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
3-449 |
6.44e-72 |
|
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: 235.55 E-value: 6.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPR--WARLSFAERHAVVERFAALLESNKAEL 79
Cdd:cd07139 1 LFIGGRWVAPSGSETIDvVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGKPRWEAATEV----TAMINKIAISIKAYHVRtgEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHI 155
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQgpgpAALLRYYAALARDFPFE--ERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 156 VPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRqLSGQ 235
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAA-VCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 236 PEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLkSGAQGDAFLARLVAVSQRLTPGNWDDePQ 315
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILV-PRSRYDEVVEALAAAVAALKVGDPLD-PA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 316 PFIGGLISEQAAQQV-------VTAWQQLEAMGGRPllaprllqagtSLLTPG-IIEMTGVAGV-PD-----EEVFGPLL 381
Cdd:cd07139 316 TQIGPLASARQRERVegyiakgRAEGARLVTGGGRP-----------AGLDRGwFVEPTLFADVdNDmriaqEEIFGPVL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129700 382 RVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKplTGAASTAPFGGIGASG 449
Cdd:cd07139 385 SVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNG--FRLDFGAPFGGFKQSG 450
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
21-431 |
8.50e-72 |
|
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: 234.83 E-value: 8.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTA 100
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 MINKIAISIKAYHVRTGEQRSEMPDGAAS-LRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEA 179
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGFERyIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 180 VMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGqPEKILALEMGGNNPLIIDEVADID 259
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 260 AAVHLTIQSAFVTAGQRCTCARRLLLKSgAQGDAFLARLVAVSQRLTPGNwDDEPQPFIGGLISEQAAQQVVTAWQQLEA 339
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHE-SIYDAFVEAFVAVVKGYKLGD-PLDPSTTLGPVVSARAADFVRAQIADAIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 340 MGGRPLLAPRLL---QAGTSLLTPGII-----EMTgvagVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPE 411
Cdd:cd07102 319 KGARALIDGALFpedKAGGAYLAPTVLtnvdhSMR----VMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420
....*....|....*....|
gi 16129700 412 REKFDQLLLEARAGIVNWNK 431
Cdd:cd07102 395 IARAEALGEQLETGTVFMNR 414
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
3-449 |
2.15e-71 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 234.42 E-value: 2.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAI 82
Cdd:PRK13473 5 LLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 83 IARETGKPRwEAAT--EVTAMINKIAISIKAYHVRTGEQRSE-MPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPAL 159
Cdd:PRK13473 85 ESLNCGKPL-HLALndEIPAIVDVFRFFAGAARCLEGKAAGEyLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 160 LAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPeK 238
Cdd:PRK13473 164 AAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSV-K 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 239 ILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFI 318
Cdd:PRK13473 242 RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY-DDLVAKLAAAVATLKVGDPDD-EDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 319 GGLISEQAAQQVVTAWQQLEAMGGrpllaPRLLQAGTSLLTPG-IIEMTGVAGVP--DE----EVFGPLLRVWRYDTFDE 391
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGH-----IRVVTGGEAPDGKGyYYEPTLLAGARqdDEivqrEVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 392 AIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGI--VNWNKPLTgaaSTAPFGGIGASG 449
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCtwVNTHFMLV---SEMPHGGQKQSG 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
21-449 |
2.87e-71 |
|
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: 233.37 E-value: 2.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAAT-EVT 99
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINKIAISIKAYHVRTGEQRSE-MPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGE 178
Cdd:cd07092 83 GAVDNFRFFAGAARTLEGPAAGEyLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 179 AVMRLWQQaGLPPGVLNLVQGGRE-TGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPeKILALEMGGNNPLIIDEVAD 257
Cdd:cd07092 163 LLAELAAE-VLPPGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTL-KRVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 258 IDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPQPfIGGLISEQAAQQVvtawqqL 337
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVY-DEFVAALVEAVSAIRVGDPDDEDTE-MGPLNSAAQRERV------A 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 338 EAMGGRPLLApRLLQAGTSLLTPGI-IEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSP 410
Cdd:cd07092 313 GFVERAPAHA-RVLTGGRRAEGPGYfYEPTVVAGVAQddeivqEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16129700 411 EREKFDQLLLEARAGIV--NWNKPLTgaaSTAPFGGIGASG 449
Cdd:cd07092 392 DVGRAMRLSARLDFGTVwvNTHIPLA---AEMPHGGFKQSG 429
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
21-449 |
4.37e-71 |
|
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: 233.21 E-value: 4.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAF--PRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRweaaTEV 98
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLI----RET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 99 TAMINKIAisiKAYHVRTGEQR--------SEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPS 170
Cdd:cd07114 79 RAQVRYLA---EWYRYYAGLADkiegavipVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 171 ELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQlSGQPEKILALEMGGNNP 249
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARA-AAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 250 LIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQ 329
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIY-DEFVERLVARARAIRVGDPLD-PETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 330 V---VTAWQQLEA---MGGRPlLAPRLLQAGtSLLTPGIIEMTGV-AGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFG 402
Cdd:cd07114 313 VeryVARAREEGArvlTGGER-PSGADLGAG-YFFEPTILADVTNdMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 16129700 403 LSCGLVSperEKFDQLLLEAR---AGIVnWNKPLTGAASTAPFGGIGASG 449
Cdd:cd07114 391 LAAGIWT---RDLARAHRVARaieAGTV-WVNTYRALSPSSPFGGFKDSG 436
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
20-458 |
5.70e-70 |
|
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: 230.31 E-value: 5.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 20 RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVT 99
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINKIAISIKAYHVRTGEQ-RSEMPDG-----AASLRHrPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELT 173
Cdd:cd07145 84 RTIRLFKLAAEEAKVLRGETiPVDAYEYnerriAFTVRE-PIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 174 PWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKIlALEMGGNNPLII 252
Cdd:cd07145 163 PLTAIELAKILEEAGLPPGVINVVTGyGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKV-ALELGGSDPMIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 253 DEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPQPfIGGLISEQAAQQVVT 332
Cdd:cd07145 242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVY-DKFLKLLVEKVKKLKVGDPLDESTD-LGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 333 AWQQLEAMGGRPLLAPRLLQAgtSLLTPGIIEMTGV-AGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPE 411
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRDEG--SFFPPTVLENDTPdMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16129700 412 REKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYA 458
Cdd:cd07145 398 INRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYT 444
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
11-452 |
1.37e-69 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 230.92 E-value: 1.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 11 TGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKP 90
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 91 RWEAATEVTAMINkiaisIKAYHVRTGEQ--RSEMPDGAASL------RHRPHGVLAVFGPYNFPGHLPNGHIVPALLAG 162
Cdd:PRK09407 108 RRHAFEEVLDVAL-----TARYYARRAPKllAPRRRAGALPVltktteLRQPKGVVGVISPWNYPLTLAVSDAIPALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 163 NTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALsaLEDLDGLLFTGSANTGyqlhRQLSGQPEKIL- 240
Cdd:PRK09407 183 NAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGpGPVVGTAL--VDNADYLMFTGSTATG----RVLAEQAGRRLi 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 241 --ALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLkSGAQGDAFLARLVAVSQRLTPG-NWDDEPQpf 317
Cdd:PRK09407 257 gfSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYV-HESIYDEFVRAFVAAVRAMRLGaGYDYSAD-- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 318 IGGLISEqaaqqvvtawQQLEAM----------------GG--RPLLAPRLLqagtslltpgiiEMTGVAGVPD------ 373
Cdd:PRK09407 334 MGSLISE----------AQLETVsahvddavakgatvlaGGkaRPDLGPLFY------------EPTVLTGVTPdmelar 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 374 EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGA-AST-APFGGIGASGNH 451
Cdd:PRK09407 392 EETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAwGSVdAPMGGMKDSGLG 471
|
.
gi 16129700 452 R 452
Cdd:PRK09407 472 R 472
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
22-452 |
2.99e-69 |
|
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: 228.35 E-value: 2.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 22 PVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAm 101
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 102 inkIAISIKAY------HVRTGEQRSEMPdGAASLR--HRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELT 173
Cdd:cd07101 82 ---VAIVARYYarraerLLKPRRRRGAIP-VLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 174 PWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALsaLEDLDGLLFTGSANTGYQLHRQ----LSGqpekiLALEMGGNN 248
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGpGSEVGGAI--VDNADYVMFTGSTATGRVVAERagrrLIG-----CSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 249 PLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKsGAQGDAFLARLVAVSQRLTPG---NWDDEpqpfIGGLISEQ 325
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVH-ESVYDEFVRRFVARTRALRLGaalDYGPD----MGSLISQA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 326 AAQQVVTAWQQLEAMGGrpllapRLLQAGTSL--LTPGIIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMAN 397
Cdd:cd07101 306 QLDRVTAHVDDAVAKGA------TVLAGGRARpdLGPYFYEPTVLTGVTEdmelfaEETFGPVVSIYRVADDDEAIELAN 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16129700 398 NTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGA-AST-APFGGIGASGNHR 452
Cdd:cd07101 380 DTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAwASIdAPMGGMKDSGLGR 436
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
20-450 |
5.44e-69 |
|
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: 227.24 E-value: 5.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 20 RNPVSGEVLwqgNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVT 99
Cdd:cd07146 4 RNPYTGEVV---GTVPAGTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINkiAISIKAYHVRTGEQRSEMPDGAASLRHR-------PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSEL 172
Cdd:cd07146 81 RAAD--VLRFAAAEALRDDGESFSCDLTANGKARkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 173 TPWSGEAVMRLWQQAGLPPGVLNLVQGG-RETGQALSALEDLDGLLFTGSANTGYQLHRQLSGqpeKILALEMGGNNPLI 251
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGY---KRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 252 IDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLL-KSGAqgDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQV 330
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVhESVA--DEFVDLLVEKSAALVVGDPMD-PATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 331 VTAWQQLEAMGGRPLLAPRLLQAgtsLLTPGIIEmtgvaGVP------DEEVFGPLLRVWRYDTFDEAIRMANNTRFGLS 404
Cdd:cd07146 313 ENRVEEAIAQGARVLLGNQRQGA---LYAPTVLD-----HVPpdaelvTEETFGPVAPVIRVKDLDEAIAISNSTAYGLS 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16129700 405 CGLVSPEREKFDQLLLEARAGIVN-WNKPltGAAS-TAPFGGIGASGN 450
Cdd:cd07146 385 SGVCTNDLDTIKRLVERLDVGTVNvNEVP--GFRSeLSPFGGVKDSGL 430
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
3-452 |
7.02e-69 |
|
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: 227.86 E-value: 7.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVKR-NPVSGEVLWQGNDADAAQVEQACRAARAAFP--RWARLSFAERHAVVERFAALLESNKAEL 79
Cdd:cd07091 6 LFINNEFVDSVSGKTFPTiNPATEEVICQVAEADEEDVDAAVKAARAAFEtgWWRKMDPRERGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGKPRWEAATevtamiNKIAISIKAY----------HVRTGEQRsemPDGAASLRHRPHGVLAVFGPYNFPGH 149
Cdd:cd07091 86 AALESLDNGKPLEESAK------GDVALSIKCLryyagwadkiQGKTIPID---GNFLAYTRREPIGVCGQIIPWNFPLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 150 LPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQL 228
Cdd:cd07091 157 MLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 229 HRQLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPG 308
Cdd:cd07091 237 MEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIY-DEFVEKFKARAEKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 309 NwDDEPQPFIGGLISEqaaqqvvtawQQLEamggrpllapRLL-------QAGTSLLTPG--------IIEMTGVAGVPD 373
Cdd:cd07091 316 D-PFDPDTFQGPQVSK----------AQFD----------KILsyiesgkKEGATLLTGGerhgskgyFIQPTVFTDVKD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 374 ------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIV---NWNKPltgaASTAPFGG 444
Cdd:cd07091 375 dmkiakEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVwvnTYNVF----DAAVPFGG 450
|
....*...
gi 16129700 445 IGASGNHR 452
Cdd:cd07091 451 FKQSGFGR 458
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
6-464 |
2.50e-68 |
|
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: 226.32 E-value: 2.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 6 NGDWItGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIAR 85
Cdd:cd07130 4 DGEWG-GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 86 ETGKPRWEAATEVTAMINkiaisIKAYHVrtGEQR--------SEMPDgaaslrHR------PHGVLAVFGPYNFPG--H 149
Cdd:cd07130 83 EMGKILPEGLGEVQEMID-----ICDFAV--GLSRqlygltipSERPG------HRmmeqwnPLGVVGVITAFNFPVavW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 150 LPNGHIvpALLAGNTIIFKPSELTPWSGEAVMRLWQQA----GLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTG 225
Cdd:cd07130 150 GWNAAI--ALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 226 YQLHRQLSGQPEKILaLEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRL 305
Cdd:cd07130 228 RQVGQAVAARFGRSL-LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIY-DEVLERLKKAYKQV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 306 TPGN-WDDepQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEMTGVAGVPDEEVFGPLLRVW 384
Cdd:cd07130 306 RIGDpLDD--GTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDAPIVKEETFAPILYVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 385 RYDTFDEAIRMANNTRFGLSCGLVSP---EREKFdqllLEARA---GIVNWNKPLTGAASTAPFGGIGASGNHRPS---A 455
Cdd:cd07130 384 KFDTLEEAIAWNNEVPQGLSSSIFTTdlrNAFRW----LGPKGsdcGIVNVNIGTSGAEIGGAFGGEKETGGGRESgsdA 459
|
....*....
gi 16129700 456 WYAadYCAW 464
Cdd:cd07130 460 WKQ--YMRR 466
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
5-455 |
5.89e-68 |
|
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: 226.31 E-value: 5.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDWITGQGASRVKRNPVS-GEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAII 83
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 84 ARETGKPRWEAATEVTAMINKIAISIKaYHVRTGEQRSEMPDGAASLR---HRPHGVLAVFGPYNFPGHLPNGHIVPALL 160
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYYAR-AALRLRYPAVEVVPYPGEDNesfYVGLGAGVVISPWNFPVAIFTGMIVAPVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 161 AGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPE-- 237
Cdd:cd07083 181 VGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGvGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPgq 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 238 ---KILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNwDDEP 314
Cdd:cd07083 261 twfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAY-EPVLERLLKRAERLSVGP-PEEN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 315 QPFIGGLISEQAAQQvVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEM-TGVAGVPDEEVFGPLLRVWRY--DTFDE 391
Cdd:cd07083 339 GTDLGPVIDAEQEAK-VLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEvPPKARIAQEEIFGPVLSVIRYkdDDFAE 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129700 392 AIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGA-ASTAPFGGIGASG-NHRPSA 455
Cdd:cd07083 418 ALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGAlVGVQPFGGFKLSGtNAKTGG 483
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
3-460 |
1.53e-67 |
|
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: 224.30 E-value: 1.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWI-TGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPR--WARLSFAERHAVVERFAALLESNKAEL 79
Cdd:cd07142 6 LFINGQFVdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGKPRWEAAT-EVTAMI----------NKI-AISIKA---YHVRTgeqrsempdgaaslRHRPHGVLAVFGPY 144
Cdd:cd07142 86 AALETWDNGKPYEQARYaEVPLAArlfryyagwaDKIhGMTLPAdgpHHVYT--------------LHEPIGVVGQIIPW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 145 NFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSAN 223
Cdd:cd07142 152 NFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 224 TGYQLHRQLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQ 303
Cdd:cd07142 232 VGKIIMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIY-DEFVEKAKARAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 304 RLTPGNwddepqPFIGGLisEQAAQqvVTAWQQLEAMGgrplLAPRLLQAGTSLLTPG--------IIEMTGVAGVPD-- 373
Cdd:cd07142 311 KRVVGD------PFRKGV--EQGPQ--VDKEQFEKILS----YIEHGKEEGATLITGGdrigskgyYIQPTIFSDVKDdm 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 374 ----EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASG 449
Cdd:cd07142 377 kiarDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTV-WVNCYDVFDASIPFGGYKMSG 455
|
490
....*....|.
gi 16129700 450 NHRPSAWYAAD 460
Cdd:cd07142 456 IGREKGIYALN 466
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
21-452 |
2.72e-67 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 222.88 E-value: 2.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWA-RLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVT 99
Cdd:cd07109 3 DPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINKI---AISIKAYHvrtGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWS 176
Cdd:cd07109 83 AAARYFeyyGGAADKLH---GETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 177 GEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGyQLHRQLSGQPEKILALEMGGNNPLIIDEV 255
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETG-IAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 256 ADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPQpfIGGLISEQAAQQVVTAWQ 335
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIY-DEVLERLVERFRALRVGPGLEDPD--LGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 336 QLEAMGGRPLLAPRLLQAGTS---LLTPGIieMTGVAgvPD-----EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGL 407
Cdd:cd07109 316 RARARGARIVAGGRIAEGAPAggyFVAPTL--LDDVP--PDsrlaqEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 16129700 408 VSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHR 452
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGR 436
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
2-449 |
1.61e-65 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 219.37 E-value: 1.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 2 TLWINGDWITG-QGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELT 80
Cdd:PRK13252 8 SLYIDGAYVEAtSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 81 AIIARETGKPRWEAAT-------EVTAMINKIAISIkayhvrTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNG 153
Cdd:PRK13252 88 ALETLDTGKPIQETSVvdivtgaDVLEYYAGLAPAL------EGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 154 HIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLS 233
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 234 GQpEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDE 313
Cdd:PRK13252 242 AS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIK-AAFEARLLERVERIRIGDPMDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 314 PQPFiGGLISEQAAQQVVTAWQQLEAMGGRpllaprlLQAGTSLLTPGI------IEMTGVAGVPD------EEVFGPLL 381
Cdd:PRK13252 320 ATNF-GPLVSFAHRDKVLGYIEKGKAEGAR-------LLCGGERLTEGGfangafVAPTVFTDCTDdmtivrEEIFGPVM 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129700 382 RVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGI--VN-WNKpltgAASTAPFGGIGASG 449
Cdd:PRK13252 392 SVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGIcwINtWGE----SPAEMPVGGYKQSG 458
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
4-461 |
4.59e-65 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 217.85 E-value: 4.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 4 WINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAI 82
Cdd:PRK11241 14 LINGEWLDANNGEVIDvTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 83 IARETGKPRWEAATEVT---AMINKIAISIKAYHVRT--GEQrsemPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVP 157
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISyaaSFIEWFAEEGKRIYGDTipGHQ----ADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 158 ALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGR-ETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQP 236
Cdd:PRK11241 170 ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 237 EKIlALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPQP 316
Cdd:PRK11241 250 KKV-SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVY-DRFAEKLQQAVSKLHIGDGLEKGVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 317 fIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGI-IEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRM 395
Cdd:PRK11241 328 -IGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTIlVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQ 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129700 396 ANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNkplTGAAST--APFGGIGASGNHRPSAWYA-ADY 461
Cdd:PRK11241 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGIN---TGIISNevAPFGGIKASGLGREGSKYGiEDY 472
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
3-458 |
8.65e-65 |
|
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: 217.40 E-value: 8.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSF--AERHAVVERFAALLESNKAEL 79
Cdd:cd07143 9 LFINGEFVDSVHGGTVKvYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVsgSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGKP-RWEAATEVTAMINKI------AISIKAYHVRTGEQRsempdgAASLRHRPHGVLAVFGPYNFPGHLPN 152
Cdd:cd07143 89 ASIEALDNGKTfGTAKRVDVQASADTFryyggwADKIHGQVIETDIKK------LTYTRHEPIGVCGQIIPWNFPLLMCA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 153 GHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQ 231
Cdd:cd07143 163 WKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 232 LSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNwD 311
Cdd:cd07143 243 AAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIY-DKFVKRFKEKAKKLKVGD-P 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 312 DEPQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGII-EMTGVAGVPDEEVFGPLLRVWRYDTFD 390
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFtDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129700 391 EAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASGNHRPSAWYA 458
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTV-WVNCYNLLHHQVPFGGYKQSGIGRELGEYA 467
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
7-449 |
4.39e-64 |
|
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: 214.86 E-value: 4.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 7 GDWITGqGASRVKR--NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIA 84
Cdd:cd07151 1 GEWRDG-TSERTIDvlNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 85 RETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALLAGN 163
Cdd:cd07151 80 RESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYRePLGVVGVISPWNFPLHLSMRSVAPALALGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 164 TIIFKPSELTPWSGEAVM-RLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRqLSGQPEKILA 241
Cdd:cd07151 160 AVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGE-LAGRHLKKVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 242 LEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIGGL 321
Cdd:cd07151 239 LELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVY-DEFVEKFVERVKALPYGDPSD-PDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 322 ISEQAAQQVVTAWQQLEAMGGRPLLAPrllQAGTSLLTPGIIemtgvAGVPD------EEVFGPLLRVWRYDTFDEAIRM 395
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVL-----SDVTNdmeiarEEIFGPVAPIIKADDEEEALEL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16129700 396 ANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASG 449
Cdd:cd07151 389 ANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSG 442
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
19-460 |
6.04e-64 |
|
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: 214.12 E-value: 6.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 19 KRNPVSGEVLWQGNDADAAQVEQACRAARAAFP--RWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAAT 96
Cdd:cd07118 1 RRSPAHGVVVARYAEGTVEDVDAAVAAARKAFDkgPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 97 EV--TAMINKIAISI-KAYHvrtGEQRSEMPDGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSEL 172
Cdd:cd07118 81 EIegAADLWRYAASLaRTLH---GDSYNNLGDDMLGLVLRePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 173 TpwSGEAVM--RLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQlSGQPEKILALEMGGNNP 249
Cdd:cd07118 158 T--SGTTLMlaELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAA-AARNLKKVSLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 250 LIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAqGDAFLARLVAVSQRLTPGN-WDDEPQpfIGGLISEQAAQ 328
Cdd:cd07118 235 QIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESI-ADAFVAAVVARSRKVRVGDpLDPETK--VGAIINEAQLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 329 QVVTAWQQLEAMGGRPLLAPRLLQAGTSLLtpgiIEMTGVAGV-PD-----EEVFGPLLRVWRYDTFDEAIRMANNTRFG 402
Cdd:cd07118 312 KITDYVDAGRAEGATLLLGGERLASAAGLF----YQPTIFTDVtPDmaiarEEIFGPVLSVLTFDTVDEAIALANDTVYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 16129700 403 LSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTaPFGGIGASGNHRPSAWYAAD 460
Cdd:cd07118 388 LSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPEL-PFGGFKQSGIGRELGRYGVE 444
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
20-458 |
1.47e-63 |
|
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: 213.26 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 20 RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVT 99
Cdd:cd07147 4 TNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINKIAISIKAYHVRTGEQR----SEMPDGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTP 174
Cdd:cd07147 84 RAIDTFRIAAEEATRIYGEVLpldiSARGEGRQGLVRRfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 175 WSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLsgqPEKILALEMGGNNPLIIDE 254
Cdd:cd07147 164 LSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARA---GKKKVVLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 255 VADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSgAQGDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQvVTAW 334
Cdd:cd07147 241 DADLDFAAQRIIFGAFYQAGQSCISVQRVLVHR-SVYDEFKSRLVARVKALKTGDPKD-DATDVGPMISESEAER-VEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 335 QQlEAmggrpllaprlLQAGTSLLTPG-----IIEMTGVAGVP------DEEVFGPLLRVWRYDTFDEAIRMANNTRFGL 403
Cdd:cd07147 318 VN-EA-----------VDAGAKLLTGGkrdgaLLEPTILEDVPpdmevnCEEVFGPVVTVEPYDDFDEALAAVNDSKFGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16129700 404 SCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYA 458
Cdd:cd07147 386 QAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYA 440
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
39-449 |
2.08e-63 |
|
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: 211.93 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 39 VEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVtamiNKIAiSIKAYHVRTGE 118
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEV----EKCA-WICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 119 -----QRSEMPDGAASLRHRPHGVlaVFG--PYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPP 191
Cdd:cd07100 76 afladEPIETDAGKAYVRYEPLGV--VLGimPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 192 GVL-NLVQGGretGQALSALED--LDGLLFTGSANTGYQLhRQLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQS 268
Cdd:cd07100 154 GVFqNLLIDS---DQVEAIIADprVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 269 AFVTAGQRCTCARRLL-LKSGAqgDAFLARLVAVSQRLTPGNWDDEpQPFIGGLISEQAAQQVVtawQQLE---AMGGRP 344
Cdd:cd07100 230 RLQNAGQSCIAAKRFIvHEDVY--DEFLEKFVEAMAALKVGDPMDE-DTDLGPLARKDLRDELH---EQVEeavAAGATL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 345 LLAPRLLQAGTSLLTPGIIemTGVA-GVP--DEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLE 421
Cdd:cd07100 304 LLGGKRPDGPGAFYPPTVL--TDVTpGMPayDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARR 381
|
410 420
....*....|....*....|....*...
gi 16129700 422 ARAGIVNWNKPlTGAASTAPFGGIGASG 449
Cdd:cd07100 382 LEAGMVFINGM-VKSDPRLPFGGVKRSG 408
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
3-452 |
2.62e-63 |
|
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: 213.36 E-value: 2.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVKR-NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNyNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPrweaATEVTAMinKIAISIKAYH-----VRTGEQRSEMPDG--AASLRHRPHGVLAVFGPYNFPGHLPNGH 154
Cdd:cd07559 83 AETLDNGKP----IRETLAA--DIPLAIDHFRyfagvIRAQEGSLSEIDEdtLSYHFHEPLGVVGQIIPWNFPLLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 155 IVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLS 233
Cdd:cd07559 157 LAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 234 gqpEKIL--ALEMGGNNPLII-DEVADIDAAVHLTIQSAFV----TAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLT 306
Cdd:cd07559 236 ---ENLIpvTLELGGKSPNIFfDDAMDADDDFDDKAEEGQLgfafNQGEVCTCPSRALVQESIY-DEFIERAVERFEAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 307 PGN-WDDEPQpfIGGLISEQAAQQVVTAWQQLEAMGGRPLL-APRLLQAGtsLLTPGIIEMTGVAGVPD------EEVFG 378
Cdd:cd07559 312 VGNpLDPETM--MGAQVSKDQLEKILSYVDIGKEEGAEVLTgGERLTLGG--LDKGYFYEPTLIKGGNNdmrifqEEIFG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129700 379 PLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASG----NHR 452
Cdd:cd07559 388 PVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRV-WVNCYHQYPAHAPFGGYKKSGigreTHK 464
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
3-449 |
3.39e-63 |
|
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: 213.04 E-value: 3.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVKR-NPVSGEVLWQGNDADAAQVEQACRAARAAFP-RWARLSFAERHAVVERFAALLESNKAELT 80
Cdd:cd07144 10 LFINNEFVKSSDGETIKTvNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDLLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 81 AIIARETGKPRWEAAT----EVTAMINKIAISIKAYHvrtGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIV 156
Cdd:cd07144 90 AIEALDSGKPYHSNALgdldEIIAVIRYYAGWADKIQ---GKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 157 PALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGyQLHRQLSGQ 235
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATG-RLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 236 PEKILALEMGGNNPLIIDEVADIDAAV---HLTIqsaFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRltpgNWDd 312
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVkwaAAGI---MYNSGQNCTATSRIYVQESIY-DKFVEKFVEHVKQ----NYK- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 313 epqpfIGGLISEQAAQ-QVVTAWQQLEAMG----GRPLLApRLLQAGTSLLTPG----IIEMTGVAGVPD------EEVF 377
Cdd:cd07144 317 -----VGSPFDDDTVVgPQVSKTQYDRVLSyiekGKKEGA-KLVYGGEKAPEGLgkgyFIPPTIFTDVPQdmrivkEEIF 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129700 378 GPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASG 449
Cdd:cd07144 391 GPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMV-WINSSNDSDVGVPFGGFKMSG 461
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
38-449 |
5.01e-63 |
|
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: 211.28 E-value: 5.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 38 QVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAMINKIAISI-KAYHVRT 116
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAAsLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 117 GEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNL 196
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 197 VQGGRE-TGQALSALEDLDGLL---FTGSANTGYQLhRQLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVT 272
Cdd:cd07105 161 VTHSPEdAPEVVEALIAHPAVRkvnFTGSTRVGRII-AETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 273 AGQRCTCARRLLL-KSGAqgDAFLARLVAVSQRLTPGNWDdepqpfIGGLISEQAAQQVVTAWQQLEAMGGRPLL-APRL 350
Cdd:cd07105 240 SGQICMSTERIIVhESIA--DEFVEKLKAAAEKLFAGPVV------LGSLVSAAAADRVKELVDDALSKGAKLVVgGLAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 351 LQAGTSLLTPGIIE-MTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNW 429
Cdd:cd07105 312 ESPSGTSMPPTILDnVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHI 391
|
410 420
....*....|....*....|
gi 16129700 430 NKPLTGAASTAPFGGIGASG 449
Cdd:cd07105 392 NGMTVHDEPTLPHGGVKSSG 411
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
3-460 |
9.08e-63 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 212.45 E-value: 9.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITG-QGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPR--WARLSFAERHAVVERFAALLESNKAEL 79
Cdd:PRK09847 22 LFINGEYTAAaENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGKP-RWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPA 158
Cdd:PRK09847 102 ALLETLDTGKPiRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 159 LLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPE 237
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 238 KILALEMGGNNPLII-DEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQP 316
Cdd:PRK09847 262 KRVWLEAGGKSANIVfADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIA-DEFLALLKQQAQNWQPGHPLD-PAT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 317 FIGGLISEQAAQQVVTAWQQLEAMGgrPLLAPRLLQAGTSLLTPGII-EMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRM 395
Cdd:PRK09847 340 TMGTLIDCAHADSVHSFIREGESKG--QLLLDGRNAGLAAAIGPTIFvDVDPNASLSREEIFGPVLVVTRFTSEEQALQL 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129700 396 ANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAAsTAPFGGIGASGNHRPSAWYAAD 460
Cdd:PRK09847 418 ANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM-TVPFGGYKQSGNGRDKSLHALE 481
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
21-449 |
4.08e-61 |
|
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: 206.83 E-value: 4.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKP-----RWEAA 95
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNAlrtqaRPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 96 T--EVTAMINKIAISIKayhvrtGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELT 173
Cdd:cd07108 83 VlaDLFRYFGGLAGELK------GETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 174 PWsgeAVMRL--WQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSgqpEKI--LALEMGGNN 248
Cdd:cd07108 157 PL---AVLLLaeILAQVLPAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---DRLipVSLELGGKS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 249 PLIIDEVADIDAAVHLTIQSA-FVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPQPfIGGLISEQAA 327
Cdd:cd07108 231 PMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIY-DAFLEKLVAKLSKLKIGDPLDEATD-IGAIISEKQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 328 QQVVT------AWQQLEAMGGRPLLAPRLLQAGTsLLTPGIIemtgvAGVPD------EEVFGPLLRVWRYDTFDEAIRM 395
Cdd:cd07108 309 AKVCGyidlglSTSGATVLRGGPLPGEGPLADGF-FVQPTIF-----SGVDNewrlarEEIFGPVLCAIPWKDEDEVIAM 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16129700 396 ANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTApFGGIGASG 449
Cdd:cd07108 383 ANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQS-YGGFKQSG 435
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
3-452 |
1.74e-60 |
|
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: 205.71 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:cd07111 24 HFINGKWVKPENRKSFPtINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPrweaATEVTAMINKIAISIKAYHVRTGE-QRSEMPDgaaslrHRPHGVLAVFGPYNFPGHLPNGHIVPALL 160
Cdd:cd07111 104 LESLDNGKP----IRESRDCDIPLVARHFYHHAGWAQlLDTELAG------WKPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 161 AGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKiL 240
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKK-L 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 241 ALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAqGDAFLARLVAVSQRLTPGNWDDEPQPfIGG 320
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESV-AEELIRKLKERMSHLRVGDPLDKAID-MGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 321 LISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIE-MTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNT 399
Cdd:cd07111 331 IVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTnVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129700 400 RFGLSCGLVSperEKFDQLL---LEARAGIVnWNKPLTGAASTAPFGGIGASGNHR 452
Cdd:cd07111 411 PYGLAASVWS---ENLSLALevaLSLKAGVV-WINGHNLFDAAAGFGGYRESGFGR 462
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
3-452 |
1.56e-59 |
|
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: 203.35 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDW---ITGQGASRVkrNPVSGEVLWQGNDADAAQVEQACRAARAAFPR---WARLSFAERHAVVERFAALLESNK 76
Cdd:cd07141 9 IFINNEWhdsVSGKTFPTI--NPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 77 AELTAIIARETGKPRWEAATEVTAMINKI----AISIKAYHVRTgeqrseMP-DGA--ASLRHRPHGVLAVFGPYNFPGH 149
Cdd:cd07141 87 AYLASLETLDNGKPFSKSYLVDLPGAIKVlryyAGWADKIHGKT------IPmDGDffTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 150 LPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGyQL 228
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVG-KL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 229 HRQLSGQPE-KILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTP 307
Cdd:cd07141 240 IQQAAGKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIY-DEFVKRSVERAKKRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 308 GNwddepqPFIGGliSEQAAQqvVTAWQQLEAMG----GRPLLApRLLQAGTSLLTPG-IIEMTGVAGVPD------EEV 376
Cdd:cd07141 319 GN------PFDPK--TEQGPQ--IDEEQFKKILEliesGKKEGA-KLECGGKRHGDKGyFIQPTVFSDVTDdmriakEEI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129700 377 FGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASGNHR 452
Cdd:cd07141 388 FGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTV-WVNCYNVVSPQAPFGGYKMSGNGR 462
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
3-460 |
3.21e-59 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 203.13 E-value: 3.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWI-TGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFP--RWARLSFAERHAVVERFAALLESNKAEL 79
Cdd:PLN02766 23 LFINGEFVdAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGK-PRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPA 158
Cdd:PLN02766 103 AALDTIDAGKlFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 159 LLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPE 237
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 238 KILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPF 317
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY-DEFVKKLVEKAKDWVVGDPFD-PRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 318 IGGLISEQAAQQVVTAWQQLEAMGGrpllapRLLQAGTSLLTPG-IIEMTGVAGVPD------EEVFGPLLRVWRYDTFD 390
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGA------TLLTGGKPCGDKGyYIEPTIFTDVTEdmkiaqDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 391 EAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASGNHRPSAWYAAD 460
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTI-WVNCYFAFDPDCPFGGYKMSGFGRDQGMDALD 483
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
20-449 |
7.68e-58 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 197.98 E-value: 7.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 20 RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPrweaateVT 99
Cdd:cd07107 2 INPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNP-------VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINKIAISIKA--YH--VRTGEQRSEMPDGAASL---RHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSEL 172
Cdd:cd07107 75 AMLGDVMVAAALldYFagLVTELKGETIPVGGRNLhytLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 173 TPWSgeaVMRLWQQAG--LPPGVLNLVQGGRET-GQALSALEDLDGLLFTGSANTGYQLHRQlSGQPEKILALEMGGNNP 249
Cdd:cd07107 155 APLS---ALRLAELARevLPPGVFNILPGDGATaGAALVRHPDVKRIALIGSVPTGRAIMRA-AAEGIKHVTLELGGKNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 250 LIIDEVADIDAAVHLTIQSA-FVTAGQRCTCARRLLLKSgAQGDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQ 328
Cdd:cd07107 231 LIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHE-SIYDEVLARVVERVAAIKVGDPTD-PATTMGPLVSRQQYD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 329 QVV-------TAWQQLEAMGGRPllaPRLLQAGTSLLTPGII-EMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTR 400
Cdd:cd07107 309 RVMhyidsakREGARLVTGGGRP---EGPALEGGFYVEPTVFaDVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16129700 401 FGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASG 449
Cdd:cd07107 386 YGLTAAIWTNDISQAHRTARRVEAGYV-WINGSSRHFLGAPFGGVKNSG 433
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
4-449 |
2.99e-57 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 205.05 E-value: 2.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 4 WINGDWITGQGASRVKRNP-----VSGEVLWqgndADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAE 78
Cdd:PRK11904 551 WQAGPIINGEGEARPVVSPadrrrVVGEVAF----ADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAE 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 79 LTAIIARETGKPRWEAATEVTAMIN------KIAISIKAYHVR----TGEQRSempdgaasLRHRPHGVLAVFGPYNFPG 148
Cdd:PRK11904 627 LIALCVREAGKTLQDAIAEVREAVDfcryyaAQARRLFGAPEKlpgpTGESNE--------LRLHGRGVFVCISPWNFPL 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 149 HLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQ 227
Cdd:PRK11904 699 AIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGdGATVGAALTADPRIAGVAFTGSTETARI 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 228 LHRQLSGQPEKILAL--EMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAqGDAFLARLVAVSQRL 305
Cdd:PRK11904 779 INRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDI-ADRVIEMLKGAMAEL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 306 TPGNWDDePQPFIGGLIsEQAAQQVVTAwqQLEAM--GGRPLLA---PRLLQAGTsLLTPGIIEMTGVAgVPDEEVFGPL 380
Cdd:PRK11904 858 KVGDPRL-LSTDVGPVI-DAEAKANLDA--HIERMkrEARLLAQlplPAGTENGH-FVAPTAFEIDSIS-QLEREVFGPI 931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129700 381 LRVWRYDTFD-----EAIrmaNNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAA-STAPFGGIGASG 449
Cdd:PRK11904 932 LHVIRYKASDldkviDAI---NATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVvGVQPFGGQGLSG 1003
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
3-449 |
4.59e-57 |
|
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: 196.52 E-value: 4.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVKR-NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:cd07117 3 LFINGEWVKGSSGETIDSyNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPRWEAATevtaminkIAISIKAYH-------VRTGEQRSEMPDGA--ASLRHRPHGVLAVFGPYNFPGHLPN 152
Cdd:cd07117 83 VETLDNGKPIRETRA--------VDIPLAADHfryfagvIRAEEGSANMIDEDtlSIVLREPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 153 GHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQ 231
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 232 LSgqpEKIL--ALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGN 309
Cdd:cd07117 234 AA---KKLIpaTLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIY-DEFVAKLKEKFENVKVGN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 310 -WDDEPQpfIGGLISEQAAQQVVTAWQQLEAMGGRPLL-APRLLQAGTS---LLTPGIIE-MTGVAGVPDEEVFGPLLRV 383
Cdd:cd07117 310 pLDPDTQ--MGAQVNKDQLDKILSYVDIAKEEGAKILTgGHRLTENGLDkgfFIEPTLIVnVTNDMRVAQEEIFGPVATV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129700 384 WRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASG 449
Cdd:cd07117 388 IKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRV-WVNTYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
21-449 |
1.37e-56 |
|
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: 194.87 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAF--PRWARlSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEV 98
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 99 TAMINKI---AISIKAYHVRTGEQRSempdGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTP 174
Cdd:cd07120 82 SGAISELryyAGLARTEAGRMIEPEP----GSFSLVLRePMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 175 WSGEAVMRLWQQA-GLPPGVLNLV-QGGRETGQALSALEDLDGLLFTGSANTGYQLhrQLSGQPE-KILALEMGGNNPLI 251
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFtESGSEGAAHLVASPDVDVISFTGSTATGRAI--MAAAAPTlKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 252 IDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQG---DAFLARLVAVsqRLTPGNwddEPQPFIGGLISEQAAQ 328
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADevrDRLAARLAAV--KVGPGL---DPASDMGPLIDRANVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 329 QVVTAWQQLEAMGGRPLLAPRLLQAGTS---LLTPGIIEMTGV-AGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLS 404
Cdd:cd07120 311 RVDRMVERAIAAGAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPdADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16129700 405 CGLVSPEREKFDQLLLEARAGIV---NWNKpltgAASTAPFGGIGASG 449
Cdd:cd07120 391 ASVWTRDLARAMRVARAIRAGTVwinDWNK----LFAEAEEGGYRQSG 434
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
3-452 |
1.40e-55 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 193.41 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWI-TGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPR-----WARLSFAERHAVVERFAALLESNK 76
Cdd:PLN02467 10 LFIGGEWRePVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 77 AELTAIIARETGKPRWEAATEvtamINKIAISIKAYHVRT----GEQRSE----MPDGAASLRHRPHGVLAVFGPYNFPG 148
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWD----MDDVAGCFEYYADLAealdAKQKAPvslpMETFKGYVLKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 149 HLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQ 227
Cdd:PLN02467 166 LMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 228 LHRQLSgQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAqGDAFLARLVAVSQRLTP 307
Cdd:PLN02467 246 IMTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERI-ASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 308 GNwddepqPF-----IGGLISEQAAQQVVTAWQQLEAMGGRPLL---APRLLQAGTSLLTPGIIEMTGVAGVPDEEVFGP 379
Cdd:PLN02467 324 SD------PLeegcrLGPVVSEGQYEKVLKFISTAKSEGATILCggkRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGP 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129700 380 LLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIV--NWNKPltgAASTAPFGGIGASGNHR 452
Cdd:PLN02467 398 VLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVwiNCSQP---CFCQAPWGGIKRSGFGR 469
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
34-449 |
1.46e-55 |
|
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: 193.20 E-value: 1.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 34 ADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVtaminKIAISIKAYH 113
Cdd:TIGR01238 71 ANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEV-----REAVDFCRYY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 114 vrTGEQRSEMPDGAaslrHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGV 193
Cdd:TIGR01238 146 --AKQVRDVLGEFS----VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 194 LNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLS--GQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAF 270
Cdd:TIGR01238 220 IQLLPGrGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAqrEDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 271 VTAGQRCTCARRLLLKSGAqGDAFLARLVAVSQRLTPGNwDDEPQPFIGGLISEQAAQQVVTAWQQLEAMGGR----PLL 346
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDV-ADRVLTMIQGAMQELKVGV-PHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKiaqlTLD 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 347 APRLLQAGTsLLTPGIIEMTGVAGVpDEEVFGPLLRVWRY--DTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARA 424
Cdd:TIGR01238 378 DSRACQHGT-FVAPTLFELDDIAEL-SEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARV 455
|
410 420
....*....|....*....|....*.
gi 16129700 425 GIVNWNKPLTGA-ASTAPFGGIGASG 449
Cdd:TIGR01238 456 GNCYVNRNQVGAvVGVQPFGGQGLSG 481
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
13-449 |
1.83e-55 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 200.09 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 13 QGASRVKRNP-----VSGEVLWqgndADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARET 87
Cdd:PRK11905 565 DGGTRPVLNPadhddVVGTVTE----ASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 88 GKPRWEAATEVtaminKIAISIKAYHvrtGEQRSEMPDGAaslRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIF 167
Cdd:PRK11905 641 GKTLANAIAEV-----REAVDFLRYY---AAQARRLLNGP---GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 168 KPSELTPW-SGEAVmRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLS--GQPEKILALE 243
Cdd:PRK11905 710 KPAEQTPLiAARAV-RLLHEAGVPKDALQLLPGdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAkrSGPPVPLIAE 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 244 MGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLksgaQ---GDAFLARLVAVSQRLTPGN-WD---Depqp 316
Cdd:PRK11905 789 TGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCL----QedvADRVLTMLKGAMDELRIGDpWRlstD---- 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 317 fIGGLISEqAAQQVVTAWqqLEAMG--GRPLL---APRLLQAGTsLLTPGIIEMTGVAgVPDEEVFGPLLRVWRY--DTF 389
Cdd:PRK11905 861 -VGPVIDA-EAQANIEAH--IEAMRaaGRLVHqlpLPAETEKGT-FVAPTLIEIDSIS-DLEREVFGPVLHVVRFkaDEL 934
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129700 390 DEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGA-ASTAPFGGIGASG 449
Cdd:PRK11905 935 DRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAvVGVQPFGGEGLSG 995
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
3-458 |
2.57e-54 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 190.79 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWI-TGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPR--WARLSFAERHAVVERFAALLESNKAEL 79
Cdd:PLN02466 60 LLINGQFVdAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGKPRWEAA-TEVTAMI----------NKI-AISIKA---YHVRTgeqrsempdgaaslRHRPHGVLAVFGPY 144
Cdd:PLN02466 140 AALETWDNGKPYEQSAkAELPMFArlfryyagwaDKIhGLTVPAdgpHHVQT--------------LHEPIGVAGQIIPW 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 145 NFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSAN 223
Cdd:PLN02466 206 NFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 224 TGYQLHRQLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQ 303
Cdd:PLN02466 286 TGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVY-DEFVEKAKARAL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 304 RLTPGNwddepqPFIGGLisEQAAQqvvTAWQQLEAMGGrplLAPRLLQAGTSLLTPG--------IIEMTGVAGVPD-- 373
Cdd:PLN02466 365 KRVVGD------PFKKGV--EQGPQ---IDSEQFEKILR---YIKSGVESGATLECGGdrfgskgyYIQPTVFSNVQDdm 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 374 ----EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASG 449
Cdd:PLN02466 431 liaqDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTV-WVNCFDVFDAAIPFGGYKMSG 509
|
....*....
gi 16129700 450 NHRPSAWYA 458
Cdd:PLN02466 510 IGREKGIYS 518
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
21-452 |
4.96e-54 |
|
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: 188.28 E-value: 4.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAAT-EVT 99
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLgEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 100 AMINKIAISIK--AYHVRTgEQRSE---MPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTP 174
Cdd:cd07098 82 VTCEKIRWTLKhgEKALRP-ESRPGgllMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 175 WSGEAVMRLWQQA----GLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSgqpeKILA---LEMGGN 247
Cdd:cd07098 161 WSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAA----ESLTpvvLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 248 NPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPqPFIGGLISEQAA 327
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIY-DKLLEILTDRVQALRQGPPLDGD-VDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 328 QQVVTAWQQLEAMGGRpLLA-----PRLLQAGTSLLTPGII-EMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRF 401
Cdd:cd07098 315 DRLEELVADAVEKGAR-LLAggkryPHPEYPQGHYFPPTLLvDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16129700 402 GLSCGLVSPEREKFDQLLLEARAGIVNWNK-PLTGAASTAPFGGIGASGNHR 452
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAINDfGVNYYVQQLPFGGVKGSGFGR 445
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
3-462 |
2.03e-53 |
|
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: 2.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAF-PRWARLSFAERHAVVERFAALLESNKAELT 80
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDiTNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 81 AIIARETGKP----------------RWEA--ATEVTAmiNKIAISIKAyhvRTGEQRSempdgaASLRHRPHGVLAVFG 142
Cdd:cd07113 82 QLETLCSGKSihlsrafevgqsanflRYFAgwATKING--ETLAPSIPS---MQGERYT------AFTRREPVGVVAGIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 143 PYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSA 222
Cdd:cd07113 151 PWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 223 NTGYQLHRQLSGQPEKIlALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSgAQGDAFLARLVAVS 302
Cdd:cd07113 231 ATGKKIGRQAASDLTRV-TLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHR-SKFDELVTKLKQAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 303 QRLTPGNWDDEpQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEMTGV-AGVPDEEVFGPLL 381
Cdd:cd07113 309 SSFQVGSPMDE-SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSAdSRLMREETFGPVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 382 RVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASGNHRP--SAWYaA 459
Cdd:cd07113 388 SFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTV-WVNMHTFLDPAVPFGGMKQSGIGREfgSAFI-D 465
|
...
gi 16129700 460 DYC 462
Cdd:cd07113 466 DYT 468
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
69-404 |
2.13e-53 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 184.94 E-value: 2.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 69 AALLESNKAELTAIIARETGKPRWEAATEV--TA-MINKIAISIKAYHvrtGE-QRSEMPDGAASLRHRPHGVLAVFGPY 144
Cdd:PRK10090 5 AAGIRERASEISALIVEEGGKIQQLAEVEVafTAdYIDYMAEWARRYE---GEiIQSDRPGENILLFKRALGVTTGILPW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 145 NFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSAN 223
Cdd:PRK10090 82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGrGETVGQELAGNPKVAMVSMTGSVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 224 TGYQLHRQLSGQPEKIlALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQ 303
Cdd:PRK10090 162 AGEKIMAAAAKNITKV-CLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY-DQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 304 RLTPGNWDDEPQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLL-APRLLQAG----TSLLTPGIIEMTgvagVPDEEVFG 378
Cdd:PRK10090 240 AVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALgGKAVEGKGyyypPTLLLDVRQEMS----IMHEETFG 315
|
330 340
....*....|....*....|....*.
gi 16129700 379 PLLRVWRYDTFDEAIRMANNTRFGLS 404
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLT 341
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
5-449 |
2.29e-53 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 194.00 E-value: 2.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDwiTGQGASRVKRNP-----VSGEVLWqgndADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAEL 79
Cdd:COG4230 562 IAGE--AASGEARPVRNPadhsdVVGTVVE----ATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAEL 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGKPRWEAATEVtaminKIAISIKAYHVRTGEQRSEMPDgaaslRHRPHGVLAVFGPYNFPGHLPNGHIVPAL 159
Cdd:COG4230 636 MALLVREAGKTLPDAIAEV-----REAVDFCRYYAAQARRLFAAPT-----VLRGRGVFVCISPWNFPLAIFTGQVAAAL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 160 LAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEK 238
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGdGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGP 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 239 ILAL--EMGGNNPLIID-----E--VADIdaavhltIQSAFVTAGQRCTCARRLLLksgaQ---GDAFLARLVAVSQRLT 306
Cdd:COG4230 786 IVPLiaETGGQNAMIVDssalpEqvVDDV-------LASAFDSAGQRCSALRVLCV----QediADRVLEMLKGAMAELR 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 307 PGN-WD---DepqpfIGGLISEQAAQQVVTAWQQLEAmGGRPLL---APRLLQAGTsLLTPGIIEMTGVAGVPdEEVFGP 379
Cdd:COG4230 855 VGDpADlstD-----VGPVIDAEARANLEAHIERMRA-EGRLVHqlpLPEECANGT-FVAPTLIEIDSISDLE-REVFGP 926
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129700 380 LLRVWRY--DTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGA-ASTAPFGGIGASG 449
Cdd:COG4230 927 VLHVVRYkaDELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAvVGVQPFGGEGLSG 999
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
3-448 |
5.65e-52 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 183.16 E-value: 5.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTA 81
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPvTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 82 IIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALL 160
Cdd:TIGR01722 83 LITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRqPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 161 AGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKIL 240
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 241 ALeMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAqgDAFLARLVAVSQRLTPGNWDDePQPFIGG 320
Cdd:TIGR01722 243 AL-GGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA--DEWVPEIRERAEKIRIGPGDD-PGAEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 321 LISEQAAQQVVTAWQQLEAMGGRPLLaprllqAGTSLLTPG-----IIEMTGVAGVP------DEEVFGPLLRVWRYDTF 389
Cdd:TIGR01722 319 LITPQAKDRVASLIAGGAAEGAEVLL------DGRGYKVDGyeegnWVGPTLLERVPptmkayQEEIFGPVLCVLEADTL 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129700 390 DEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGAS 448
Cdd:TIGR01722 393 EEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDS 451
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
37-449 |
4.87e-49 |
|
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: 173.95 E-value: 4.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 37 AQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEA-ATEVTAMINKIAISIKayHVR 115
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETlLTEVSGVKNDILHMLK--NLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 116 TGEQRSEMPDGAAS-------LRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAg 188
Cdd:cd07135 83 KWAKDEKVKDGPLAfmfgkprIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 189 LPPGVLNLVQGG-RETGQALSalEDLDGLLFTGSANTGyqlhrqlsgqpeKILA-----------LEMGGNNPLIIDEVA 256
Cdd:cd07135 162 LDPDAFQVVQGGvPETTALLE--QKFDKIFYTGSGRVG------------RIIAeaaakhltpvtLELGGKSPVIVTKNA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 257 DIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPQpfIGGLISEQAAQQVVtawQQ 336
Cdd:cd07135 228 DLELAAKRILWGKFGNAGQICVAPDYVLVDPSVY-DEFVEELKKVLDEFYPGGANASPD--YTRIVNPRHFNRLK---SL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 337 LEAMGGrpllapRLLQAGTSLLTPGIIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSP 410
Cdd:cd07135 302 LDTTKG------KVVIGGEMDEATRFIPPTIVSDVSWddslmsEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTD 375
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 16129700 411 EREKFDQLLLEARAGIVNWNKPLT-GAASTAPFGGIGASG 449
Cdd:cd07135 376 DKSEIDHILTRTRSGGVVINDTLIhVGVDNAPFGGVGDSG 415
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
40-449 |
1.64e-48 |
|
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: 172.33 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 40 EQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAA-TEVTAMINKIAISIKayHVR--T 116
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHALK--HLKkwM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 117 GEQRSEMPD----GAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPG 192
Cdd:cd07087 79 KPRRVSVPLllqpAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 193 VLNLVQGGRETGQALSAlEDLDGLLFTGSANTGYQLHRQLSGQ--PekiLALEMGGNNPLIIDEVADIDAAVHLTIQSAF 270
Cdd:cd07087 158 AVAVVEGGVEVATALLA-EPFDHIFFTGSPAVGKIVMEAAAKHltP---VTLELGGKSPCIVDKDANLEVAARRIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 271 VTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLtpgnWDDEPQ--PFIGGLISEQAAQQVVtawqqleamggrpllap 348
Cdd:cd07087 234 LNAGQTCIAPDYVLVHESIK-DELIEELKKAIKEF----YGEDPKesPDYGRIINERHFDRLA----------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 349 RLLQAGTsLLTPG-------IIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKF 415
Cdd:cd07087 292 SLLDDGK-VVIGGqvdkeerYIAPTILDDVSPdsplmqEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQ 370
|
410 420 430
....*....|....*....|....*....|....*
gi 16129700 416 DQLLLEARAGIVNWNKPLTGAASTA-PFGGIGASG 449
Cdd:cd07087 371 ERVLAETSSGGVCVNDVLLHAAIPNlPFGGVGNSG 405
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
3-449 |
1.04e-45 |
|
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: 166.13 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVKR-NPVSGEVLWQGNDADAAQVEQACRAARAAFPR--WARLSFAERHAVVERFAALLESNKAEL 79
Cdd:cd07140 8 LFINGEFVDAEGGKTYNTiNPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 80 TAIIARETGkprweaATEVTAMINKIAISIKAYHVRTGE----QRSEMPDGAAS-------LRHRPHGVLAVFGPYNFPG 148
Cdd:cd07140 88 ATIESLDSG------AVYTLALKTHVGMSIQTFRYFAGWcdkiQGKTIPINQARpnrnltlTKREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 149 HLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQ 227
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGsGSLVGQRLSDHPDVRKLGFTGSTPIGKH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 228 LHRQLSGQPEKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTP 307
Cdd:cd07140 242 IMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIH-DEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 308 GN-----WDDEPQPFIGGLIS-EQAAQQVVTAWQQLEaMGGRPLLAPRLlqagtsLLTPGIIemTGVAG---VPDEEVFG 378
Cdd:cd07140 321 GDpldrsTDHGPQNHKAHLDKlVEYCERGVKEGATLV-YGGKQVDRPGF------FFEPTVF--TDVEDhmfIAKEESFG 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129700 379 PLLRVWRYDT--FDEAIRMANNTRFGLSCGLVSPEREK--FDQLLLEARAGIVN-WNKplTGAAstAPFGGIGASG 449
Cdd:cd07140 392 PIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKalYVSDKLEAGTVFVNtYNK--TDVA--APFGGFKQSG 463
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
4-452 |
1.14e-45 |
|
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: 166.09 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 4 WINGDWIT---GQGASRVkrNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELT 80
Cdd:cd07116 4 FIGGEWVApvkGEYFDNI--TPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 81 AIIARETGKP-RWEAATEVTAMINK---IAISIKAYHVRTGEQRSempDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIV 156
Cdd:cd07116 82 VAETWDNGKPvRETLAADIPLAIDHfryFAGCIRAQEGSISEIDE---NTVAYHFHEPLGVVGQIIPWNFPLLMATWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 157 PALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGyQLHRQLSGQ 235
Cdd:cd07116 159 PALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTG-RLIMQYASE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 236 PEKILALEMGGNNPLI-IDEVAD-----IDAAVHLTIQSAFvTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGN 309
Cdd:cd07116 237 NIIPVTLELGGKSPNIfFADVMDaddafFDKALEGFVMFAL-NQGEVCTCPSRALIQESIY-DRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 310 WDDePQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGtSLLTPGIIEMTGVAG-----VPDEEVFGPLLRVW 384
Cdd:cd07116 315 PLD-TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELG-GLLGGGYYVPTTFKGgnkmrIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129700 385 RYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVnWNKPLTGAASTAPFGGIGASG----NHR 452
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRV-WTNCYHLYPAHAAFGGYKQSGigreNHK 463
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
3-452 |
1.26e-45 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 166.10 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 3 LWINGDWITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPR--WARlSFAERHAVVERFAALLESNKAELT 80
Cdd:TIGR04284 3 LLIDGKLVAGSAGTFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDEtdWSR-DTALRVRCLRQLRDALRAHVEELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 81 AIIARETGKPRW-EAATEVTAMINKIAisikaYHVRTGEQRSEMPD-GAAS---------LRHRPHGVLAVFGPYNFPGH 149
Cdd:TIGR04284 82 ELTIAEVGAPRMlTAGAQLEGPVDDLG-----FAADLAESYAWTTDlGVASpmgiptrrtLRREAVGVVGAITPWNFPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 150 LPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRL-WQQAGLPPGVLNLVQGGR-ETGQALSALEDLDGLLFTGSANTGYQ 227
Cdd:TIGR04284 157 INLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVTSSDhRLGALLAKDPRVDMVSFTGSTATGRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 228 LHRQLSGQPEKILaLEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSgAQGDAFLARLVAVSQRLTP 307
Cdd:TIGR04284 237 VMADAAATLKKVF-LELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPR-ARYDEAVAAAAATMGSIKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 308 GNwDDEPQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLA---PRLLQAGTSLLTPGIIEMTGVAGVPDEEVFGPLLRVW 384
Cdd:TIGR04284 315 GD-PADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGggrPADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVI 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129700 385 RYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAAStAPFGGIGASGNHR 452
Cdd:TIGR04284 394 AHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSAD-APFGGYKQSGIGR 460
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
4-452 |
7.79e-45 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 164.24 E-value: 7.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 4 WINGDWiTGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAII 83
Cdd:PLN02315 24 YVGGEW-RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 84 ARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQ-RSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAG 162
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIiPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 163 NTIIFKPSELTPWSGEAVMRL----WQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEK 238
Cdd:PLN02315 183 NCVVWKGAPTTPLITIAMTKLvaevLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 239 ILaLEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNwDDEPQPFI 318
Cdd:PLN02315 263 CL-LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIY-DDVLEQLLTVYKQVKIGD-PLEKGTLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 319 GGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANN 398
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNS 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16129700 399 TRFGLSCGLVSPEREKFDQLL--LEARAGIVNWNKPLTGAASTAPFGGIGASGNHR 452
Cdd:PLN02315 420 VPQGLSSSIFTRNPETIFKWIgpLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGR 475
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
13-449 |
1.06e-44 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 168.61 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 13 QGASRVKRNP-----VSGEVlwqgNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARET 87
Cdd:PRK11809 657 AGEMSPVINPadprdIVGYV----REATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREA 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 88 GKPRWEAATEVtaminKIAISIKAYHvrTGEQRSEMPDGAaslrHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIF 167
Cdd:PRK11809 733 GKTFSNAIAEV-----REAVDFLRYY--AGQVRDDFDNDT----HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 168 KPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRET-GQALSALEDLDGLLFTGSANTGYQLHRQLS------GQPEKIL 240
Cdd:PRK11809 802 KPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETvGAALVADARVRGVMFTGSTEVARLLQRNLAgrldpqGRPIPLI 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 241 AlEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTcARRLLLKSGAQGDAFLARLVAVSQRLTPGNwddePQPF--- 317
Cdd:PRK11809 882 A-ETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCS-ALRVLCLQDDVADRTLKMLRGAMAECRMGN----PDRLstd 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 318 IGGLISEQAAQQVVTAWQQLEAMGGRPLLAPR----LLQAGTsLLTPGIIEMTGVAGVpDEEVFGPLLRVWRY--DTFDE 391
Cdd:PRK11809 956 IGPVIDAEAKANIERHIQAMRAKGRPVFQAARenseDWQSGT-FVPPTLIELDSFDEL-KREVFGPVLHVVRYnrNQLDE 1033
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129700 392 AIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGA-ASTAPFGGIGASG 449
Cdd:PRK11809 1034 LIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAvVGVQPFGGEGLSG 1092
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
20-397 |
1.35e-44 |
|
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: 162.59 E-value: 1.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 20 RNPVSGEVLWQGNDADAAQVEQACRAARAAF-PRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEV 98
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 99 TAMINKIAISIKAYHVRTGEqrsEMPDG---AASLR-----HRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPS 170
Cdd:cd07148 84 TRAIDGVELAADELGQLGGR---EIPMGltpASAGRiafttREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 171 ELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSgqPEKILALEMGGNNPL 250
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA--PGTRCALEHGGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 251 IIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSgAQGDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQV 330
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPA-EIADDFAQRLAAAAEKLVVGDPTD-PDTEVGPLIRPREVDRV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129700 331 VTAWQQLEAMGGRPLLAPRLLqaGTSLLTPGII-EMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMAN 397
Cdd:cd07148 317 EEWVNEAVAAGARLLCGGKRL--SDTTYAPTVLlDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQAN 382
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
5-448 |
5.70e-44 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 163.76 E-value: 5.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDWITGQGASRVKR-NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAII 83
Cdd:PLN02419 118 IGGSFVESQSSSFIDViNPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 84 ARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQRSEMPDGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALLAG 162
Cdd:PLN02419 198 TTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIRePLGVCAGICPFNFPAMIPLWMFPVAVTCG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 163 NTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKILAl 242
Cdd:PLN02419 278 NTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 243 EMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQG--DAFLARLVAVsqRLTPGNwddEPQPFIGG 320
Cdd:PLN02419 357 NMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSweDKLVERAKAL--KVTCGS---EPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 321 LISEQAAQQVVTAWQQLEAMGGrpllapRLLQAGTSLLTPG-----IIEMTGVAGV-PD-----EEVFGPLLRVWRYDTF 389
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGA------KLLLDGRDIVVPGyekgnFIGPTILSGVtPDmecykEEIFGPVLVCMQANSF 505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16129700 390 DEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTGAASTAPFGGIGAS 448
Cdd:PLN02419 506 DEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKAS 564
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
45-449 |
2.98e-42 |
|
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: 155.85 E-value: 2.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 45 AARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEA-ATEVTAMINKIAISIKAYHVRTGEQRSE- 122
Cdd:cd07134 6 AQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVdLTEILPVLSEINHAIKHLKKWMKPKRVRt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 123 ---MPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPGVLNLVQG 199
Cdd:cd07134 86 pllLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 200 GRETGQALSALEdLDGLLFTGSANTGyqlhRQLSGQPEKILA---LEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQR 276
Cdd:cd07134 165 DAEVAQALLELP-FDHIFFTGSPAVG----KIVMAAAAKHLAsvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 277 CTCARRLLLKSgAQGDAFLARLVAVSQRLTPGNWDDEPQPFIGGLISEQAAQQVVTAWQQLEAMGGrpllapRLLQAGTS 356
Cdd:cd07134 240 CIAPDYVFVHE-SVKDAFVEHLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGA------KVEFGGQF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 357 LLTPGIIEMTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWN 430
Cdd:cd07134 313 DAAQRYIAPTVLTNVTPdmkimqEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
|
410 420
....*....|....*....|
gi 16129700 431 KPLTGAASTA-PFGGIGASG 449
Cdd:cd07134 393 DVVLHFLNPNlPFGGVNNSG 412
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
47-449 |
7.73e-40 |
|
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: 149.17 E-value: 7.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 47 RAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETG-KPRWEAA-TEVTAMINKIAISIKayHVR--TGEQRSE 122
Cdd:cd07133 8 KAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLlAEILPSIAGIKHARK--HLKkwMKPSRRH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 123 ----MPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPGVLNLVQ 198
Cdd:cd07133 86 vgllFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 199 GGRETGQALSALeDLDGLLFTGSANTGyqlhrqlsgqpEKILA----------LEMGGNNPLIIDEVADIDAAVHLTIQS 268
Cdd:cd07133 165 GGADVAAAFSSL-PFDHLLFTGSTAVG-----------RHVMRaaaenltpvtLELGGKSPAIIAPDADLAKAAERIAFG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 269 AFVTAGQRCTCARRLLLKSGaQGDAFLARLVAVSQRLTPgNWDDEPQpfIGGLISEQAAQQVVTAWQQLEAMGGR--PLL 346
Cdd:cd07133 233 KLLNAGQTCVAPDYVLVPED-KLEEFVAAAKAAVAKMYP-TLADNPD--YTSIINERHYARLQGLLEDARAKGARviELN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 347 APRLLQAGTSLLTPgiiemTGVAGVPD------EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLL 420
Cdd:cd07133 309 PAGEDFAATRKLPP-----TLVLNVTDdmrvmqEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLR 383
|
410 420 430
....*....|....*....|....*....|
gi 16129700 421 EARAGIVNWNKPLTGAA-STAPFGGIGASG 449
Cdd:cd07133 384 RTHSGGVTINDTLLHVAqDDLPFGGVGASG 413
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
21-452 |
8.79e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 149.50 E-value: 8.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTa 100
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 minKIAISIKAYHVRTGEQRSEMPDGAASL-------RHRPHG-VLAVFgPYNFPGHLPNGHIVPALLAGNTIIFKPSEL 172
Cdd:PRK09406 86 ---KCAKGFRYYAEHAEALLADEPADAAAVgasrayvRYQPLGvVLAVM-PWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 173 TPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLhRQLSGQPEKILALEMGGNNPLII 252
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 253 DEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDePQPFIGGLISEQAAQQVVT 332
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVY-DAFAEKFVARMAALRVGDPTD-PDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 333 AWQQLEAMGGrpllapRLLQAGTSLLTPG-------IIEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSC 405
Cdd:PRK09406 319 QVDDAVAAGA------TILCGGKRPDGPGwfypptvITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16129700 406 GLVSPEREKFDQLLLEARAGIVNWNKpLTGAASTAPFGGIGASGNHR 452
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFING-MTVSYPELPFGGVKRSGYGR 438
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
34-449 |
1.00e-38 |
|
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: 147.73 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 34 ADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNK-AELTAIIARETGKPRWEA----ATEVTAMIN---KI 105
Cdd:cd07123 66 ADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNVWQAeidaACELIDFLRfnvKY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 106 AISIKAYhvrtgEQRSEMPDGAASLRHRP-HG-VLAVfGPYNFP---GHLPnghIVPALLaGNTIIFKPSELTPWSGEAV 180
Cdd:cd07123 146 AEELYAQ-----QPLSSPAGVWNRLEYRPlEGfVYAV-SPFNFTaigGNLA---GAPALM-GNVVLWKPSDTAVLSNYLV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 181 MRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKI-----LALEMGGNNPLIIDE 254
Cdd:cd07123 216 YKILEEAGLPPGVINFVPGdGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYrtyprIVGETGGKNFHLVHP 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 255 VADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQGDaFLARLVAVSQRLTPGNwDDEPQPFIGGLISEQAAQQVVTAw 334
Cdd:cd07123 296 SADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPE-VKERLLEELKEIKMGD-PDDFSNFMGAVIDEKAFDRIKGY- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 335 qqLEAMGGRPLLapRLLQAGTS------LLTPGIIEMTgvagVPD-----EEVFGPLLRVWRYD--TFDEAIRMANNT-R 400
Cdd:cd07123 373 --IDHAKSDPEA--EIIAGGKCddsvgyFVEPTVIETT----DPKhklmtEEIFGPVLTVYVYPdsDFEETLELVDTTsP 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16129700 401 FGLSCGLVSPEREKFDQLLLEAR--AG--IVNwNKPlTGA-ASTAPFGGIGASG 449
Cdd:cd07123 445 YALTGAIFAQDRKAIREATDALRnaAGnfYIN-DKP-TGAvVGQQPFGGARASG 496
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
39-455 |
4.50e-35 |
|
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: 136.21 E-value: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 39 VEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPrWEAATEVTAMINKI-----AISIKAYH 113
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLrarafVIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 114 VRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAG-LPPG 192
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 193 VLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPekiLALEMGGNNPLIIDEVAD-IDAAVHLTIQSAFV 271
Cdd:cd07084 160 DVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQAR---IYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 272 TAGQRCTCARRLLLKSGAQGDAFLARLVAVSQRLTPGNwddepqPFIGGLISEQAAQQVVtawqQLEAMGGRPLLAP-RL 350
Cdd:cd07084 237 CSGQKCTAQSMLFVPENWSKTPLVEKLKALLARRKLED------LLLGPVQTFTTLAMIA----HMENLLGSVLLFSgKE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 351 LQAGTSLLTPGIIEMTGVAGVPD----------EEVFGPLLRVWRYDTFDEAIRMANNTRF--GLSCGLVSPEREKFDQL 418
Cdd:cd07084 307 LKNHSIPSIYGACVASALFVPIDeilktyelvtEEIFGPFAIVVEYKKDQLALVLELLERMhgSLTAAIYSNDPIFLQEL 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 16129700 419 LLE-ARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSA 455
Cdd:cd07084 387 IGNlWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAG 424
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-403 |
1.81e-34 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 135.27 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 4 WINGDWITGQGASRVK-RNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAI 82
Cdd:PLN00412 19 YADGEWRTSSSGKSVAiTNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 83 IARETGKPRWEAATEVTAMINKIAISIKAyHVRT-GEQRSEMPD---GAAS----LRHR-PHGVLAVFGPYNFPGHLPNG 153
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEE-GVRIlGEGKFLVSDsfpGNERnkycLTSKiPLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 154 HIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGsANTGYQLHRQL 232
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTG-GDTGIAISKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 233 SGQPekiLALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTcARRLLLKSGAQGDAFLARLVAVSQRLTPGNWDD 312
Cdd:PLN00412 257 GMVP---LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCT-AVKVVLVMESVADALVEKVNAKVAKLTVGPPED 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 313 EPQ----------PFIGGLIsEQAAQQVVTAWQQLEAMGGrpLLAPRLLQAGTslltpgiiemtgvagvPD-----EEVF 377
Cdd:PLN00412 333 DCDitpvvsessaNFIEGLV-MDAKEKGATFCQEWKREGN--LIWPLLLDNVR----------------PDmriawEEPF 393
|
410 420
....*....|....*....|....*.
gi 16129700 378 GPLLRVWRYDTFDEAIRMANNTRFGL 403
Cdd:PLN00412 394 GPVLPVIRINSVEEGIHHCNASNFGL 419
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
21-452 |
1.87e-34 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 134.60 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 21 NPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTA 100
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 101 MINKIAISIKAYHVRTGEQRSEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAV 180
Cdd:PRK13968 93 SANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 181 MRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQlSGQPEKILALEMGGNNPLIIDEVADIDA 260
Cdd:PRK13968 173 AQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQ-AGAALKKCVLELGGSDPFIVLNDADLEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 261 AVHLTIQSAFVTAGQRCTCARRLLLKSGAqGDAFLARLVAVSQRLTPGNWDDEpQPFIGGL----ISEQAAQQVvtawQQ 336
Cdd:PRK13968 252 AVKAAVAGRYQNTGQVCAAAKRFIIEEGI-ASAFTERFVAAAAALKMGDPRDE-ENALGPMarfdLRDELHHQV----EA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 337 LEAMGGRPLLAPRLLQAGTSLLTPGII-----EMTGVAgvpdEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPE 411
Cdd:PRK13968 326 TLAEGARLLLGGEKIAGAGNYYAPTVLanvtpEMTAFR----EELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16129700 412 REKFDQLLLEARAGIVNWNKPLTGAASTApFGGIGASGNHR 452
Cdd:PRK13968 402 ETQARQMAARLECGGVFINGYCASDARVA-FGGVKKSGFGR 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
39-440 |
7.03e-34 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 133.05 E-value: 7.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 39 VEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAMINKIAISikAYHVRTG- 117
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLF--ADLVREGs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 118 --EQRSEMPDGAASLRHRPH--------GVLAVFGPYNFP------GhlpnGHIVPALLAGNTIIFKP-------SELTp 174
Cdd:cd07129 79 wlDARIDPADPDRQPLPRPDlrrmlvplGPVAVFGASNFPlafsvaG----GDTASALAAGCPVVVKAhpahpgtSELV- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 175 wsGEAVMRLWQQAGLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKI-LALEMGGNNPLII 252
Cdd:cd07129 154 --ARAIRAALRATGLPAGVFSLLQGgGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIpFYAELGSVNPVFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 253 DEVADIDAAVhlTIQSAFVT-----AGQRCTCARRLLLKSGAQGDAFLARLVAVSQRLTPgnwddepqpfiGGLISEQAA 327
Cdd:cd07129 232 LPGALAERGE--AIAQGFVGsltlgAGQFCTNPGLVLVPAGPAGDAFIAALAEALAAAPA-----------QTMLTPGIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 328 QQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEMTGVAGVPD----EEVFGPLLRVWRYDTFDEAIRMANNTRFGL 403
Cdd:cd07129 299 EAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLADpalqEEVFGPASLVVRYDDAAELLAVAEALEGQL 378
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16129700 404 SCGLVSPERE--KFDQLL--LEARAGIVNWNKPLTGAASTA 440
Cdd:cd07129 379 TATIHGEEDDlaLARELLpvLERKAGRLLFNGWPTGVEVCP 419
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
34-449 |
8.94e-31 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 124.76 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 34 ADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEAA-TEVTAMINKIAISIKAY 112
Cdd:PTZ00381 4 DNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLKHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 113 HVRTGEQRSEMP----DGAASLRHRPHGVLAVFGPYNFPGHLPnghIVP---ALLAGNTIIFKPSELTPWSGEAVMRLWQ 185
Cdd:PTZ00381 84 DEYLKPEKVDTVgvfgPGKSYIIPEPLGVVLVIGAWNYPLNLT---LIPlagAIAAGNTVVLKPSELSPHTSKLMAKLLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 186 QAgLPPGVLNLVQGGRETGQALSAlEDLDGLLFTGSANTGyqlhrqlsgqpeKILA-----------LEMGGNNPLIIDE 254
Cdd:PTZ00381 161 KY-LDPSYVRVIEGGVEVTTELLK-EPFDHIFFTGSPRVG------------KLVMqaaaenltpctLELGGKSPVIVDK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 255 VADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQgDAFLARL-VAVSQRLTPgnwDDEPQPFIGGLISEQAA---QQV 330
Cdd:PTZ00381 227 SCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIK-DKFIEALkEAIKEFFGE---DPKKSEDYSRIVNEFHTkrlAEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 331 VTAWQQLEAMGGRPLLAPRLLQAgTSLLTPGI--IEMTgvagvpdEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLV 408
Cdd:PTZ00381 303 IKDHGGKVVYGGEVDIENKYVAP-TIIVNPDLdsPLMQ-------EEIFGPILPILTYENIDEVLEFINSRPKPLALYYF 374
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 16129700 409 SPEREKFDQLLLEARAGIVNWNKPLTGAA-STAPFGGIGASG 449
Cdd:PTZ00381 375 GEDKRHKELVLENTSSGAVVINDCVFHLLnPNLPFGGVGNSG 416
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
47-449 |
4.80e-29 |
|
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: 119.15 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 47 RAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEA-ATEVTAMINKIAISIKayHVR--TGEQRSEM 123
Cdd:cd07136 8 RAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAyMTEIGFVLSEINYAIK--HLKkwMKPKRVKT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 124 P---DGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSgEAVMRLWQQAGLPPGVLNLVQG 199
Cdd:cd07136 86 PllnFPSKSYIYYePYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNT-SKVIAKIIEETFDEEYVAVVEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 200 GRETGQALSAlEDLDGLLFTGSANTGYQLHRQLSGQ--PekiLALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRC 277
Cdd:cd07136 165 GVEENQELLD-QKFDYIFFTGSVRVGKIVMEAAAKHltP---VTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 278 TCARRLLLKSGAQgDAFLARLVAVSQRLTPGNWDDEPQpfIGGLISEQaaqqvvtAWQQLEAM--------GGRpllapr 349
Cdd:cd07136 241 VAPDYVLVHESVK-EKFIKELKEEIKKFYGEDPLESPD--YGRIINEK-------HFDRLAGLldngkivfGGN------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 350 lLQAGTSLLTPGIieMTGV---AGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSpEREKFDQLLLEARA-- 424
Cdd:cd07136 305 -TDRETLYIEPTI--LDNVtwdDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFS-EDKKVEKKVLENLSfg 380
|
410 420
....*....|....*....|....*.
gi 16129700 425 -GIVNwNKPLTGAASTAPFGGIGASG 449
Cdd:cd07136 381 gGCIN-DTIMHLANPYLPFGGVGNSG 405
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
40-449 |
7.00e-29 |
|
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: 118.48 E-value: 7.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 40 EQACRAARAAFP--RWARLSFaeRHAVVERFAALLESNKAELTAIIARETGKPRWEAA-TEVTAMINKIAISIKAYHVRT 116
Cdd:cd07132 1 AEAVRRAREAFSsgKTRPLEF--RIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlSEILLVKNEIKYAISNLPEWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 117 GEQRSEMP-----DGAAsLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPP 191
Cdd:cd07132 79 KPEPVKKNlatllDDVY-IYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKY-LDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 192 GVLNLVQGG-RETGQALSalEDLDGLLFTGSANTGYQLHRQLSgqpeKILA---LEMGGNNPLIIDEVADIDAAVHLTIQ 267
Cdd:cd07132 157 ECYPVVLGGvEETTELLK--QRFDYIFYTGSTSVGKIVMQAAA----KHLTpvtLELGGKSPCYVDKSCDIDVAARRIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 268 SAFVTAGQRCTCARRLLLKSGAQgDAFLARLVAVSQRLtpgnWDDEPQ--PFIGGLISEQAAQQVVtawQQLE----AMG 341
Cdd:cd07132 231 GKFINAGQTCIAPDYVLCTPEVQ-EKFVEALKKTLKEF----YGEDPKesPDYGRIINDRHFQRLK---KLLSggkvAIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 342 GRPLLAPRllqagtslltpgIIEMTGVAGVP------DEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKF 415
Cdd:cd07132 303 GQTDEKER------------YIAPTVLTDVKpsdpvmQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVI 370
|
410 420 430
....*....|....*....|....*....|....*
gi 16129700 416 DQLLLEARAGIVNWNKPLTGAA-STAPFGGIGASG 449
Cdd:cd07132 371 NKILSNTSSGGVCVNDTIMHYTlDSLPFGGVGNSG 405
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
5-422 |
1.20e-27 |
|
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: 115.83 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 5 INGDWITGQGASRVKRNPVSGEVLWQGnDADAAQVEQACRAARA-AFPRWARLSFAERHAVVERFAALLESNKAELTAII 83
Cdd:cd07128 5 VAGQWHAGTGDGRTLHDAVTGEVVARV-SSEGLDFAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDLYALS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 84 AReTGKPRWEAATEVTAminkiAISIKAYHVRTGeqRSEMPD---------------GAASLRH--RPHGVLAVF-GPYN 145
Cdd:cd07128 84 AA-TGATRRDSWIDIDG-----GIGTLFAYASLG--RRELPNahflvegdveplskdGTFVGQHilTPRRGVAVHiNAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 146 FP--GHLpnGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAG-LPPGVLNLVQGGreTGQALSALEDLDGLLFTGSA 222
Cdd:cd07128 156 FPvwGML--EKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS--VGDLLDHLGEQDVVAFTGSA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 223 NTGYQLHRQLSGQPEKI-LALEMGGNNPLIIDEVA-----DIDAAVHLTIQSAFVTAGQRCTCARRLLLKSgAQGDAFLA 296
Cdd:cd07128 232 ATAAKLRAHPNIVARSIrFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPE-ARVDAVIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 297 RLVAVSQRLTPGNWDDEPQPfIGGLISE--------------QAAQQVVTAWQQLEAMGGRPL----LAPRLLQAGTSLl 358
Cdd:cd07128 311 ALKARLAKVVVGDPRLEGVR-MGPLVSReqredvraavatllAEAEVVFGGPDRFEVVGADAEkgafFPPTLLLCDDPD- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129700 359 tpgiiemtGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEA 422
Cdd:cd07128 389 --------AATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
4-421 |
9.41e-24 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 104.40 E-value: 9.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 4 WINGDWITGQGASRVKRNPVSGEVL----WQGNDADAAQV---EQACRAARAafprwarLSFAERHAVVERFAALLESNK 76
Cdd:PRK11903 8 YVAGRWQAGSGAGTPLFDPVTGEELvrvsATGLDLAAAFAfarEQGGAALRA-------LTYAQRAALLAAIVKVLQANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 77 AELTAIIARETGKPRWEAATEVTAMINKIAISIK-------AYHVRTGEQRSEMPDGAASLRH--RPHGVLAVF-GPYNF 146
Cdd:PRK11903 81 DAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKlgaalgdARLLRDGEAVQLGKDPAFQGQHvlVPTRGVALFiNAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 147 PGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAG-LPPGVLNLVQGGreTGQALSALEDLDGLLFTGSANTG 225
Cdd:PRK11903 161 PAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGS--SAGLLDHLQPFDVVSFTGSAETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 226 yqlhRQLSGQPEKI-----LALEMGGNNPLII--DEVAD---IDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQG---D 292
Cdd:PRK11903 239 ----AVLRSHPAVVqrsvrVNVEADSLNSALLgpDAAPGseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDavaE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 293 AFLARLVAVsqrlTPGNWDDEPQPfIGGLISeqaAQQVVTAWQQLEAM--------GGR---PLLAPRLLQA--GTSLLt 359
Cdd:PRK11903 315 ALAARLAKT----TVGNPRNDGVR-MGPLVS---RAQLAAVRAGLAALraqaevlfDGGgfaLVDADPAVAAcvGPTLL- 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129700 360 pGIIEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLE 421
Cdd:PRK11903 386 -GASDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALE 446
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
39-449 |
1.61e-22 |
|
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: 99.79 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 39 VEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEA-ATEVTAMINKIAISIKAYHVRTG 117
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 118 EQRSEMP----DGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPGV 193
Cdd:cd07137 81 PEKVKTPlttfPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 194 LNLVQGGRETGQALsaLE-DLDGLLFTGSANTGyqlhRQLSGQPEKIL---ALEMGGNNPLIIDEVADIDAAVHLTIQSA 269
Cdd:cd07137 160 IKVIEGGVPETTAL--LEqKWDKIFFTGSPRVG----RIIMAAAAKHLtpvTLELGGKCPVIVDSTVDLKVAVRRIAGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 270 F-VTAGQRCTCARRLLLKSGaqgdaFLARLVAVSQRLTPGNWDDEPqpfigglISEQAAQQVVTA--WQQLEAMGGRPLL 346
Cdd:cd07137 234 WgCNNGQACIAPDYVLVEES-----FAPTLIDALKNTLEKFFGENP-------KESKDLSRIVNShhFQRLSRLLDDPSV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 347 APRLLQAGTSLLTPGIIEMTGVAGVP------DEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLL 420
Cdd:cd07137 302 ADKIVHGGERDEKNLYIEPTILLDPPldssimTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVA 381
|
410 420 430
....*....|....*....|....*....|
gi 16129700 421 EARAGIVNWNKP-LTGAASTAPFGGIGASG 449
Cdd:cd07137 382 ETSSGGVTFNDTvVQYAIDTLPFGGVGESG 411
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
65-449 |
8.24e-16 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 79.70 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 65 VERFAALLESNKAELTAIIARETGKPRWEAAT-EVTAMINKIAISIKAYHVRTGEQRSEMP----DGAASLRHRPHGVLA 139
Cdd:PLN02174 38 LKKLMIICDNHEPEIVAALRDDLGKPELESSVyEVSLLRNSIKLALKQLKNWMAPEKAKTSlttfPASAEIVSEPLGVVL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 140 VFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAgLPPGVLNLVQGGRETGQALSAlEDLDGLLFT 219
Cdd:PLN02174 118 VISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLE-QKWDKIFYT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 220 GSANTGYQLHRQLSGQPEKILaLEMGGNNPLIIDEVADIDAAVHLTIQSAF-VTAGQRCTCARRLLLKSgaqgdAFLARL 298
Cdd:PLN02174 196 GSSKIGRVIMAAAAKHLTPVV-LELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTK-----EYAPKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 299 VAVSQRltpgnwddEPQPFIG-GLISEQAAQQVV--TAWQQLEAMGGRPLLAPRLLQAGTSLLTPGIIEMTGVAGVP--- 372
Cdd:PLN02174 270 IDAMKK--------ELETFYGkNPMESKDMSRIVnsTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPlds 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 373 ---DEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLLEARA-GIVNWNKPLTGAASTAPFGGIGAS 448
Cdd:PLN02174 342 limSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAgGIVVNDIAVHLALHTLPFGGVGES 421
|
.
gi 16129700 449 G 449
Cdd:PLN02174 422 G 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
34-449 |
7.37e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 76.69 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 34 ADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWEA-ATEVTAMINKIAISIKAY 112
Cdd:PLN02203 3 APGETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVGVLTKSANLALSNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 113 HVRTGEQRSEMP----DGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPwSGEAVMRLWQQAG 188
Cdd:PLN02203 83 KKWMAPKKAKLPlvafPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAP-ATSAFLAANIPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 189 LPPGVLNLVQGGRETGQALsaLE-DLDGLLFTGSANTGyqlhRQLSGQPEKIL---ALEMGGNNPLIIDEVA---DIDAA 261
Cdd:PLN02203 162 LDSKAVKVIEGGPAVGEQL--LQhKWDKIFFTGSPRVG----RIIMTAAAKHLtpvALELGGKCPCIVDSLSssrDTKVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 262 VHLTIQSAFVT-AGQRCTCARRLLLKSGAQgdAFLARLVAVSQRLTPGNWDDEPQpFIGGLISEQaaqqvvtAWQQLEAM 340
Cdd:PLN02203 236 VNRIVGGKWGScAGQACIAIDYVLVEERFA--PILIELLKSTIKKFFGENPRESK-SMARILNKK-------HFQRLSNL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 341 GGRPLLAPRLLQAGTSLLTPGIIEMTGVAGVP------DEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCgLVSPEREK 414
Cdd:PLN02203 306 LKDPRVAASIVHGGSIDEKKLFIEPTILLNPPldsdimTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAI-YAFTNNEK 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 16129700 415 FDQLLL-EARAGIVNWNKPLTG-AASTAPFGGIGASG 449
Cdd:PLN02203 385 LKRRILsETSSGSVTFNDAIIQyACDSLPFGGVGESG 421
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
134-420 |
9.67e-12 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 67.14 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 134 PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQGGRETGQALSALEDL 213
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 214 DGLLFTGSANTGYQLHRQLSGQpekiLALEMGGNNPLIID-EVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQGD 292
Cdd:cd07126 222 RMTLFTGSSKVAERLALELHGK----VKLEDAGFDWKILGpDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 293 AFLARLVAVSQR-----LTPG---NWDDEP-QPFIGGLISEQAAQQvvtawqqleAMGGRPllaprlLQAGTSLLTPGII 363
Cdd:cd07126 298 GILDKLKALAEQrkledLTIGpvlTWTTERiLDHVDKLLAIPGAKV---------LFGGKP------LTNHSIPSIYGAY 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129700 364 EMTGVAgVPDE-------------EVFGPLLRVWRYDTFDEAI------RMANNtrfgLSCGLVSPErEKFDQLLL 420
Cdd:cd07126 363 EPTAVF-VPLEeiaieenfelvttEVFGPFQVVTEYKDEQLPLvlealeRMHAH----LTAAVVSND-IRFLQEVL 432
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
158-450 |
1.87e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 56.35 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 158 ALLAGNTIIFKPSELTPWSGEAVMRLWQQA----GLPPGVLNLVQG-GRETGQALSALEDLDGLLFTGSAN---TGYQlh 229
Cdd:cd07122 119 ALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEpSIELTQELMKHPDVDLILATGGPGmvkAAYS-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 230 rqlSGQPekilALEMG-GNNPLIIDEVADIDAAVHLTIQS-AF-----VTAGQRCTCARRLLlksgaqgDAFLARLVAV- 301
Cdd:cd07122 197 ---SGKP----AIGVGpGNVPAYIDETADIKRAVKDIILSkTFdngtiCASEQSVIVDDEIY-------DEVRAELKRRg 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 302 --------SQRLTPGNWDDepqpfiGGLISEQAAQQvvTAwQQLEAMGG--RPllaprllqAGTSLLtpgIIEMTGVAgv 371
Cdd:cd07122 263 ayflneeeKEKLEKALFDD------GGTLNPDIVGK--SA-QKIAELAGieVP--------EDTKVL---VAEETGVG-- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 372 PDE----EVFGPLLRVWRYDTFDEAIRMA----NNTRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPltgaastAPFG 443
Cdd:cd07122 321 PEEplsrEKLSPVLAFYRAEDFEEALEKArellEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVNTP-------SSLG 393
|
....*..
gi 16129700 444 GIGASGN 450
Cdd:cd07122 394 GIGDTYN 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
71-270 |
1.98e-08 |
|
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: 56.46 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 71 LLESNKAELTAIIARETGkPRWEAATEVTAMINKIAI-SIKAYHVRTGEQRSEMPD-GAASLRHRPHGVLAVFGPYNFPG 148
Cdd:cd07077 36 LASEAVSERGAYIRSLIA-NWIAMMGCSESKLYKNIDtERGITASVGHIQDVLLPDnGETYVRAFPIGVTMHILPSTNPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 149 HLPNgHIVPALLAGNTIIFKPSELTPWSGEAVMRLWQQAGLPPGVLNLVQ----GGRETGQALSALEDLDGLLFTGsant 224
Cdd:cd07077 115 SGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLyvphPSDELAEELLSHPKIDLIVATG---- 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16129700 225 GYQLHRQLSGQPEKILALEMG-GNNPLIIDEVADIDAAVHLTIQSAF 270
Cdd:cd07077 190 GRDAVDAAVKHSPHIPVIGFGaGNSPVVVDETADEERASGSVHDSKF 236
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
13-447 |
2.60e-07 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 53.25 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 13 QGASRVKRNPVSGEVlwqGNDADAAQVEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRW 92
Cdd:cd07127 63 SGWVGGEVSPYGVEL---GVTYPQCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFM 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 93 EAATEVTAMINKIAISIKAYHVR-----TGEQRSEMPDGAA---SLRHR----PHGVLAVFGPYNFPGHlpNGHivPALL 160
Cdd:cd07127 140 MAFQAGGPHAQDRGLEAVAYAWRemsriPPTAEWEKPQGKHdplAMEKTftvvPRGVALVIGCSTFPTW--NGY--PGLF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 161 A----GNTIIFKPSELTPWSGEAVMRLWQ----QAGLPPGVLNLV--QGGRETGQALSALEDLDGLLFTGSANTGYQLHR 230
Cdd:cd07127 216 AslatGNPVIVKPHPAAILPLAITVQVARevlaEAGFDPNLVTLAadTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 231 QLSGqpeKILALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLL-KSG---AQG----DAFLARLVAVS 302
Cdd:cd07127 296 NARQ---AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGiqtDDGrksfDEVAADLAAAI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 303 QRLTpGNwDDEPQPFIGGLISEQAAQQVVTAWQQLE-AMGGRPLLAPRLLQAGTSllTPGIIEMTGV-AGVPDEEVFGPL 380
Cdd:cd07127 373 DGLL-AD-PARAAALLGAIQSPDTLARIAEARQLGEvLLASEAVAHPEFPDARVR--TPLLLKLDASdEAAYAEERFGPI 448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129700 381 LRVWRYDTFDEAIRMANN---TRFGLSCGLVSPEREKFDQLLLEARAGIVNWNKPLTG------AASTAPFGGIGA 447
Cdd:cd07127 449 AFVVATDSTDHSIELAREsvrEHGAMTVGVYSTDPEVVERVQEAALDAGVALSINLTGgvfvnqSAAFSDFHGTGA 524
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
134-452 |
3.73e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 49.19 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 134 PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKP----SELTPWSGEAVMRLWQQAGLPPGVLNLV-QGGRETGQALS 208
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIdNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 209 ALEDLDGLLFTGSANTGYQLHRqlSGQPekilALEMG-GNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLL-LK 286
Cdd:cd07081 175 KFPGIGLLLATGGPAVVKAAYS--SGKP----AIGVGaGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIvVD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 287 SGAqgDAFLARLVAVSQRLTPGNWDDEPQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLqagtslltpgIIEMT 366
Cdd:cd07081 249 SVY--DEVMRLFEGQGAYKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQETRIL----------IGEVT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 367 GVAGVPD--EEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVS-------PEREKFDQLLLEARAGIVNWNKPltgaa 437
Cdd:cd07081 317 SLAEHEPfaHEKLSPVLAMYRAANFADADAKALALKLEGGCGHTSamysdniKAIENMNQFANAMKTSRFVKNGP----- 391
|
330
....*....|....*
gi 16129700 438 stAPFGGIGASGNHR 452
Cdd:cd07081 392 --CSQGGLGDLYNFR 404
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
39-269 |
2.00e-05 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 46.85 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 39 VEQACRAARAAFPRWARLSFAERHAVVERFAALLESNKAELTAIIARETGKPRWE-------AATEVTAMINKIAISika 111
Cdd:cd07121 6 VDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEdkiaknhLAAEKTPGTEDLTTT--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 112 yhVRTGeqrsempDGAASLRHR-PHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKP----SELTPWSGEAVMRLWQQ 186
Cdd:cd07121 83 --AWSG-------DNGLTLVEYaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129700 187 AGlppGVLNLV----QGGRETGQALSALEDLDGLLFTGsantGYQLHRQL--SGQPekilALEMG-GNNPLIIDEVADID 259
Cdd:cd07121 154 AG---GPDNLVvtveEPTIETTNELMAHPDINLLVVTG----GPAVVKAAlsSGKK----AIGAGaGNPPVVVDETADIE 222
|
250
....*....|
gi 16129700 260 AAVHLTIQSA 269
Cdd:cd07121 223 KAARDIVQGA 232
|
|
| |
