|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
21-499 |
0e+00 |
|
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: 803.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARsWAGRLPAERERILLRFADLVEQHGEE 100
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSA-WAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 101 LAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLSIPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIG 180
Cdd:cd07113 80 LAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQGERYTAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 181 MWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAvCGAALTSHPRIAKVSFTGSTATGKQIAR 260
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 261 AAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMS 340
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 341 PEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEA 420
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953939 421 LQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCVRY 499
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIRY 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-499 |
0e+00 |
|
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: 638.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 17 DRQHGLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQ 96
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 97 HGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLSIPlpqgaRYQAWTRKEPVGVVAGIVPWNFP 176
Cdd:COG1012 81 RREELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDAP-----GTRAYVRREPLGVVGAITPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 177 LMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGK 256
Cdd:COG1012 155 LALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 257 QIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVG 336
Cdd:COG1012 235 RIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 337 PGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDG-KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVA 415
Cdd:COG1012 315 DPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 416 DGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLI-DANLPFGGMKQSGTGRDFGPDWLDGWCETKS 494
Cdd:COG1012 395 DEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
....*
gi 515953939 495 VCVRY 499
Cdd:COG1012 475 VTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
23-495 |
0e+00 |
|
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: 583.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 23 WIEGRQaasdseKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELA 102
Cdd:pfam00171 1 WVDSES------ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAF--PAWRKTPAAERAAILRKAADLLEERKDELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 103 QLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMW 182
Cdd:pfam00171 73 ELETLENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETL------PSDPGRLAYTRREPLGVVGAITPWNFPLLLPAW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 183 KVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAA 262
Cdd:pfam00171 146 KIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 263 ADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPE 342
Cdd:pfam00171 226 AQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 343 AFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQ 422
Cdd:pfam00171 306 TDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIE 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953939 423 LANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDA-NLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:pfam00171 386 IANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
60-497 |
0e+00 |
|
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: 561.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 60 DRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRaFEVGCTLNWMRYTAGLTTKIA 139
Cdd:cd07078 1 DAAVAAARAAF--KAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 140 GKTldlsiPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIP 219
Cdd:cd07078 78 GEV-----IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 220 EGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSF 299
Cdd:cd07078 153 PGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 300 LNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPD 379
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 380 G-KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVN 458
Cdd:cd07078 313 GgKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 515953939 459 SHTL-IDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07078 393 DYSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
21-495 |
0e+00 |
|
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: 556.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEE 100
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 101 LAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIG 180
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTI------PIDGNFLAYTRREPIGVCGQIIPWNFPLLML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 181 MWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIAR 260
Cdd:cd07091 159 AWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 261 AAADT-LTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGM 339
Cdd:cd07091 239 AAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 340 SPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEE 419
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 420 ALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
39-495 |
0e+00 |
|
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: 543.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRa 118
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAF--PGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 FEVGCTLNWMRYTAglttkiagktlDLSIP---LPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIV 195
Cdd:cd07106 78 FEVGGAVAWLRYTA-----------SLDLPdevIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 196 IKPSETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGG 275
Cdd:cd07106 147 LKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 276 KNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCD 355
Cdd:cd07106 225 NDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 356 KVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASV 435
Cdd:cd07106 305 KVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 436 WTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-495 |
0e+00 |
|
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: 522.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 fEVGCTLNWMRYTAGLTTKIAGKTldlsIPLPQGArYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:cd07114 81 -QVRYLAEWYRYYAGLADKIEGAV----IPVDKGD-YLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAELIAGNRGPDG----KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTAS 434
Cdd:cd07114 315 RYVARAREEGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953939 435 VWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
19-480 |
0e+00 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 519.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 19 QHGLWIEGRQAASDSEKrLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHG 98
Cdd:PRK13473 2 QTKLLINGELVAGEGEK-QPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF--PEWSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 99 EELAQLETLEQGKSINISRAFEVGCTLNWMRYTAG----LTTKIAGKTLdlsiplpqgARYQAWTRKEPVGVVAGIVPWN 174
Cdd:PRK13473 79 DEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGaarcLEGKAAGEYL---------EGHTSMIRRDPVGVVASIAPWN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 175 FPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTAT 254
Cdd:PRK13473 150 YPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 255 GKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLS 334
Cdd:PRK13473 229 GKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 335 VGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAH-NAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVR 413
Cdd:PRK13473 309 VGDPDDEDTELGPLISAAHRDRVAGFVERAKALgHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTP 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953939 414 VADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRD 480
Cdd:PRK13473 389 FDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKD 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
41-495 |
5.86e-180 |
|
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: 512.53 E-value: 5.86e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 41 NPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAFE 120
Cdd:cd07112 8 NPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 121 VGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSE 200
Cdd:cd07112 88 VPSAANTFRWYAEAIDKVYGEVA------PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 201 TTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADT-LTGVTLELGGKNPA 279
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 280 IVLKDA-DPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAELIAGNR--GPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVW 436
Cdd:cd07112 322 GYIESGKAEGARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVW 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953939 437 TQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07112 402 TSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
39-497 |
2.34e-179 |
|
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: 510.95 E-value: 2.34e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAF--PGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 FEVG-CTLNWmRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIK 197
Cdd:cd07093 79 RDIPrAAANF-RFFADYILQLDGESY------PQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 198 PSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKN 277
Cdd:cd07093 152 PSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 278 PAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKV 357
Cdd:cd07093 232 PNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 358 QAFLDEAKAHNAELIAGNRGPD----GKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTA 433
Cdd:cd07093 312 LGYVELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953939 434 SVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07093 392 YVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-495 |
4.35e-175 |
|
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: 501.07 E-value: 4.35e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 23 WIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEELA 102
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 103 QLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLsiplpqGARYQAWTRKEPVGVVAGIVPWNFPLMIGMW 182
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDV------PPHVISRTVREPVGVCGLITPWNYPLLQAAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 183 KVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAA 262
Cdd:cd07119 154 KLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 263 ADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPE 342
Cdd:cd07119 234 AGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 343 AFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDG----KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGE 418
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953939 419 EALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07119 394 EAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
39-497 |
4.31e-173 |
|
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: 494.64 E-value: 4.31e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAF--KTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 fEVGCTLNWMRYTAGLTTKIAGKTldlsIPLPQGARYQaWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:cd07103 79 -EVDYAASFLEWFAEEARRIYGRT----IPSPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07103 153 AEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQ 438
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953939 439 NISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
39-497 |
3.94e-172 |
|
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: 492.23 E-value: 3.94e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAF--PSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 FEVGCTLNWMRYTAG----LTTKIAGKTLdlsiplpqgARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSI 194
Cdd:cd07092 79 DELPGAVDNFRFFAGaartLEGPAAGEYL---------PGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 195 VIKPSETTPLTLLRVAELASEaGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELG 274
Cdd:cd07092 150 VLKPSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 275 GKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHC 354
Cdd:cd07092 229 GKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 355 DKVQAFLDEAKAHnAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTAS 434
Cdd:cd07092 309 ERVAGFVERAPAH-ARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953939 435 VWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
41-497 |
5.03e-172 |
|
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: 492.34 E-value: 5.03e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 41 NPATGEVIASTADASVDDVDRAVMSGWRAFVArsWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAFE 120
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 121 VGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSE 200
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVI------PVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 201 TTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAI 280
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 281 VLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAF 360
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 361 LDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNI 440
Cdd:cd07115 315 VDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515953939 441 SKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07115 395 GRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-495 |
1.59e-165 |
|
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: 476.30 E-value: 1.59e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 22 LWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAFEVGCTLNWMRYTAGLttkiaGKTLDLSIPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGM 181
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAAL-----ARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 182 WKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIARA 261
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREV-GEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 262 AADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSP 341
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 342 EAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDG--KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEE 419
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 420 ALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNsHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
39-495 |
3.75e-161 |
|
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: 464.79 E-value: 3.75e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAgRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 FEVGCTLNWMRYTAGLTTKIAGKTlDLSIPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEF-DLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAELIAGNRGPDG--KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVW 436
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953939 437 TQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
21-495 |
1.50e-160 |
|
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: 464.19 E-value: 1.50e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPA-ERERILLRFADLVEQHGE 99
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAF--ESWWSKVTGeERGELLDKLADLVEKNRD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 100 ELAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMI 179
Cdd:cd07144 87 LLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTI------PTSPNKLAYTLHEPYGVCGQIIPWNYPLAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 180 GMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIA 259
Cdd:cd07144 161 AAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 260 RAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLS-VGPG 338
Cdd:cd07144 241 KAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkVGSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 339 MSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRG---PDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVA 415
Cdd:cd07144 321 FDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKapeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 416 DGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07144 401 TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
39-497 |
1.08e-158 |
|
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: 458.24 E-value: 1.08e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRL-PAERERILLRFADLVEQHGEELAQLETLEQGKSINISR 117
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAF--ESGWLRLsPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 118 AfEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIK 197
Cdd:cd07109 79 A-DVEAAARYFEYYGGAADKLHGETI------PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 198 PSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKN 277
Cdd:cd07109 152 PAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 278 PAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSpEAFINPLVSRAHCDKV 357
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 358 QAFLDEAKAHNAELIAGNR---GPDGKGYYVSPTLV--VNPDNhlRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLT 432
Cdd:cd07109 311 EGFVARARARGARIVAGGRiaeGAPAGGYFVAPTLLddVPPDS--RLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLV 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953939 433 ASVWTQNISKALAYTDRLQAGTVWVNSHTL---IDanLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07109 389 AGVWTRDGDRALRVARRLRAGQVFVNNYGAgggIE--LPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
20-497 |
1.32e-155 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 451.64 E-value: 1.32e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 20 HGLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGE 99
Cdd:PRK13252 7 QSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 100 ELAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKtldlSIPLPQGARYqaWTRKEPVGVVAGIVPWNFPLMI 179
Cdd:PRK13252 85 ELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGE----QIPLRGGSFV--YTRREPLGVCAGIGAWNYPIQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 180 GMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIA 259
Cdd:PRK13252 159 ACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 260 RAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGM 339
Cdd:PRK13252 238 AAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 340 SPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPD----GKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVA 415
Cdd:PRK13252 318 DPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 416 DGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:PRK13252 398 DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
..
gi 515953939 496 CV 497
Cdd:PRK13252 478 QV 479
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
31-498 |
4.52e-155 |
|
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: 450.26 E-value: 4.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 31 SDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPA-ERERILLRFADLVEQHGEELAQLETLEQ 109
Cdd:cd07141 18 SVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDAsERGRLLNKLADLIERDRAYLASLETLDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 110 GKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALA 189
Cdd:cd07141 98 GKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTI------PMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 190 AGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADT-LTG 268
Cdd:cd07141 172 CGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSnLKR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 269 VTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPL 348
Cdd:cd07141 252 VTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 349 VSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTE 428
Cdd:cd07141 332 IDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTT 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 429 YGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCVR 498
Cdd:cd07141 412 YGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
39-498 |
1.52e-154 |
|
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: 447.91 E-value: 1.52e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQ--KEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 fEVGCTLNWMRYTAGLTTKIAGKTldlsIPLPQGARyqAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:cd07090 79 -DIDSSADCLEYYAGLAPTLSGEH----VPLPGGSF--AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07090 152 SPFTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07090 231 LIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAELIAGNRGPDGK-----GYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTA 433
Cdd:cd07090 311 GYIESAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953939 434 SVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCVR 498
Cdd:cd07090 391 GVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-495 |
1.95e-154 |
|
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: 447.72 E-value: 1.95e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 22 LWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVArsWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIA-----GKTLdlsiplpqgaryqawTRKEPVGVVAGIVPWNFP 176
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEfeerrGNSL---------------VVREPIGVCGLITPWNWP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 177 LMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGK 256
Cdd:cd07138 144 LNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 257 QIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVG 336
Cdd:cd07138 224 RVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 337 PGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRG-PDG--KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVR 413
Cdd:cd07138 304 DPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGrPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 414 VADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNsHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETK 493
Cdd:cd07138 384 YDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
..
gi 515953939 494 SV 495
Cdd:cd07138 463 SI 464
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
67-497 |
1.17e-153 |
|
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: 442.05 E-value: 1.17e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 67 WRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGktLDLS 146
Cdd:cd06534 4 RAAF--KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGG--PELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 147 IPLPQGaryQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVV 226
Cdd:cd06534 79 SPDPGG---EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 227 TGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVC 306
Cdd:cd06534 156 PGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 307 AASSRIYIEAPLFDtlvsgfeqavkslsvgpgmspeafinplvsrahcdkvqAFLDEAKahnaeliagnrgpdgkgyyvs 386
Cdd:cd06534 236 TAASRLLVHESIYD--------------------------------------EFVEKLV--------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 387 pTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTL-IDA 465
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 515953939 466 NLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
39-497 |
2.26e-152 |
|
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: 442.18 E-value: 2.26e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAgRLPA-ERERILLRFADLVEQHGEELAQLETLEQGKSINISR 117
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWA-ATPArERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 118 AFEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIK 197
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETL------PFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 198 PSETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKN 277
Cdd:cd07108 152 AAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 278 PAIVLKDADPAWVIEGLMTGS-FLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDK 356
Cdd:cd07108 231 PMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 357 VQAFLDEAKAH-NAELIAGNR----GPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGL 431
Cdd:cd07108 311 VCGYIDLGLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515953939 432 TASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPD-WLDGWCETKSVCV 497
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEgMLEHFTQKKTVNI 457
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
23-495 |
4.85e-152 |
|
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: 442.07 E-value: 4.85e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 23 WIEGRQAASDSekRLNVYNPA-TGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:cd07097 4 YIDGEWVAGGD--GEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAF--PAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLSIPlpqGARYQawTRKEPVGVVAGIVPWNFPLMIGM 181
Cdd:cd07097 80 ARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRP---GVEVE--TTREPLGVVGLITPWNFPIAIPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 182 WKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARA 261
Cdd:cd07097 154 WKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 262 AADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSP 341
Cdd:cd07097 234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 342 EAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNR---GPDgKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGE 418
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGErlkRPD-EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYD 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953939 419 EALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTL-IDANLPFGGMKQSGTG-RDFGPDWLDGWCETKSV 495
Cdd:cd07097 393 EALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
21-498 |
8.90e-152 |
|
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: 441.58 E-value: 8.90e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvARSWAGRLP-AERERILLRFADLVEQHGE 99
Cdd:cd07143 8 GLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAF-ETDWGLKVSgSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 100 ELAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLSIplpqgaRYQAWTRKEPVGVVAGIVPWNFPLMI 179
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDI------KKLTYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 180 GMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIA 259
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 260 RAAADT-LTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPG 338
Cdd:cd07143 241 EAAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 339 MSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGE 418
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 419 EALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCVR 498
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-495 |
3.10e-150 |
|
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: 436.78 E-value: 3.10e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFVarSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISrA 118
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 FEVGCTLNWMRYTAGLTTKIAGKTlDLSIPLPQgARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLDAKA-ERAVPLPS-EDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07110 156 SELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAELIAGNRGPD--GKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVW 436
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953939 437 TQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
20-493 |
1.16e-149 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 435.78 E-value: 1.16e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 20 HGLWIEgrqaaSDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGE 99
Cdd:TIGR01804 3 DGEYVE-----DSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 100 ELAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLSIPlpqgarYQAWTRKEPVGVVAGIVPWNFPLMI 179
Cdd:TIGR01804 76 ELAKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGP------SFAYTIREPLGVCVGIGAWNYPLQI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 180 GMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIA 259
Cdd:TIGR01804 150 ASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 260 RAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGM 339
Cdd:TIGR01804 230 AAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 340 SPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPD----GKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVA 415
Cdd:TIGR01804 310 DEATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFS 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953939 416 DGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETK 493
Cdd:TIGR01804 390 DEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
22-495 |
2.48e-149 |
|
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: 435.38 E-value: 2.48e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 22 LWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGM 181
Cdd:cd07142 86 AALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTL------PADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 182 WKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARA 261
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 262 AADT-LTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMS 340
Cdd:cd07142 240 AAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 341 PEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEA 420
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953939 421 LQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
20-499 |
1.38e-148 |
|
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: 433.69 E-value: 1.38e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 20 HGLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVarSWAGRLPAERERILLRFADLVEQHGE 99
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK--TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 100 ELAQLETLEQGKSINISRAFEVGCTLNWMRYTAGL-------TTKIAGKTLdlsiplpqgaryqAWTRKEPVGVVAGIVP 172
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGViraqegsLSEIDEDTL-------------SYHFHEPLGVVGQIIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 173 WNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGST 252
Cdd:cd07559 146 WNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 253 ATGKQIARAAADTLTGVTLELGGKNPAIVLKDA---DPAWVI--EGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFE 327
Cdd:cd07559 225 TVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAmdaDDDFDDkaEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 328 QAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAG----NRGPDGKGYYVSPTLVVNPDNHLRLTREE 403
Cdd:cd07559 305 ERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGgerlTLGGLDKGYFYEPTLIKGGNNDMRIFQEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 404 VFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGP 483
Cdd:cd07559 385 IFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHK 464
|
490
....*....|....*.
gi 515953939 484 DWLDGWCETKSVCVRY 499
Cdd:cd07559 465 MMLDHYQQTKNILVSY 480
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
42-495 |
9.84e-148 |
|
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: 430.22 E-value: 9.84e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 42 PATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAfEV 121
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 122 GCTLNWMRYTAGLTTKIAGKTLDlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSET 201
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYN-----NLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 202 TPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIV 281
Cdd:cd07118 158 TSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 282 LKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFL 361
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 362 DEAKAHNAELI-AGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNI 440
Cdd:cd07118 318 DAGRAEGATLLlGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515953939 441 SKALAYTDRLQAGTVWVNshTLID--ANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07118 398 DTALTVARRIRAGTVWVN--TFLDgsPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
21-497 |
1.72e-147 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 431.15 E-value: 1.72e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEE 100
Cdd:TIGR02299 2 GHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAF--KRWAELKAAERKRYLHKIADLIEQHADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 101 LAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLdlsiPLPQGARYqawTRKEPVGVVAGIVPWNFPLMIG 180
Cdd:TIGR02299 80 IAVLECLDCGQPLRQTRQQVIRAAENFRFFADKCEEAMDGRTY----PVDTHLNY---TVRVPVGPVGLITPWNAPFMLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 181 MWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIAR 260
Cdd:TIGR02299 153 TWKIAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 261 AAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMS 340
Cdd:TIGR02299 233 NGADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 341 PEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPD-------GKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVR 413
Cdd:TIGR02299 313 PETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 414 VADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDfGPDW-LDGWCET 492
Cdd:TIGR02299 393 FKDEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGRE-GGTYsFDFYTET 471
|
....*
gi 515953939 493 KSVCV 497
Cdd:TIGR02299 472 KNVAL 476
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-499 |
2.13e-146 |
|
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: 427.18 E-value: 2.13e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAF--PEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 fEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:cd07107 79 -DVMVAAALLDYFAGLVTELKGETI------PVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07107 152 PEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTG-SFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKV 357
Cdd:cd07107 231 LIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 358 QAFLDEAKAHNAELIAGNRGPDG----KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTA 433
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 434 SVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCVRY 499
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
22-495 |
9.32e-146 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 427.31 E-value: 9.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 22 LWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:PLN02766 23 LFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLSiplpqgARYQAWTRKEPVGVVAGIVPWNFPLMIGM 181
Cdd:PLN02766 103 AALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMS------RQLQGYTLKEPIGVVGHIIPWNFPSTMFF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 182 WKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARA 261
Cdd:PLN02766 177 MKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 262 AADT-LTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMS 340
Cdd:PLN02766 257 AATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 341 PEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEA 420
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515953939 421 LQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:PLN02766 417 IKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
39-497 |
1.52e-144 |
|
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: 422.12 E-value: 1.52e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGkSINISRA 118
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGG-STYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 FEVGCTLNWMRYTAGLTTKIAGKTLDlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLP-----SDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07150 155 SEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAELIAGNRgpdGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQ 438
Cdd:cd07150 315 RQVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 439 NISKALAYTDRLQAGTVWVNSHTLID-ANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
16-497 |
2.11e-144 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 423.72 E-value: 2.11e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 16 LDRQHGLwIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVE 95
Cdd:PLN02278 22 LLRTQGL-IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAF--PSWSKLTASERSKILRRWYDLII 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 96 QHGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGktlDLsIPLPQGARyQAWTRKEPVGVVAGIVPWNF 175
Cdd:PLN02278 99 ANKEDLAQLMTLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYG---DI-IPSPFPDR-RLLVLKQPVGVVGAITPWNF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 176 PLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATG 255
Cdd:PLN02278 173 PLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 256 KQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSV 335
Cdd:PLN02278 253 KKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 336 GPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAE-LIAGNRGPDGKGYYvSPTLVVNPDNHLRLTREEVFGPVVNLVRV 414
Cdd:PLN02278 333 GDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKvLLGGKRHSLGGTFY-EPTVLGDVTEDMLIFREEVFGPVAPLTRF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 415 ADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKS 494
Cdd:PLN02278 412 KTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKY 491
|
...
gi 515953939 495 VCV 497
Cdd:PLN02278 492 VCL 494
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
24-495 |
9.54e-143 |
|
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: 418.21 E-value: 9.54e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 24 IEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAgRLPA-ERERILLRFADLVEQHGEELA 102
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQ--KAWE-RLPAiERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 103 QLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLSIPlpqgaRYQAWTRKEPVGVVAGIVPWNFPLMIGMW 182
Cdd:cd07088 79 KLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDRP-----NENIFIFKVPIGVVAGILPWNFPFFLIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 183 KVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAA 262
Cdd:cd07088 153 KLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 263 ADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPE 342
Cdd:cd07088 233 AENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 343 AFINPLVSRAHCDKVQAFLDEAKAHNAEL-IAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEAL 421
Cdd:cd07088 313 TDMGPLVNEAALDKVEEMVERAVEAGATLlTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 422 QLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNS---------HTlidanlpfgGMKQSGTGRDFGPDWLDGWCET 492
Cdd:cd07088 393 ELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRenfeamqgfHA---------GWKKSGLGGADGKHGLEEYLQT 463
|
...
gi 515953939 493 KSV 495
Cdd:cd07088 464 KVV 466
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
20-499 |
2.29e-141 |
|
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: 415.36 E-value: 2.29e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 20 HGLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGE 99
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 100 ELAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLSIPLPQgaRYQAWTRKEPVGVVAGIVPWNFPLMI 179
Cdd:cd07140 86 ELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPN--RNLTLTKREPIGVCGIVIPWNYPLMM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 180 GMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIA 259
Cdd:cd07140 164 LAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 260 RAAADT-LTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPG 338
Cdd:cd07140 244 KSCAVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 339 MSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADG- 417
Cdd:cd07140 324 LDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGd 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 418 -EEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVC 496
Cdd:cd07140 404 vDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVT 483
|
...
gi 515953939 497 VRY 499
Cdd:cd07140 484 IEY 486
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
24-499 |
2.76e-140 |
|
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: 412.13 E-value: 2.76e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 24 IEGRQAASDSEKRLNVYNPATG-EVIASTADASVDDVDRAVMSGWRAFvaRSWAgRLPA-ERERILLRFADLVEQHGEEL 101
Cdd:cd07131 3 IGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAF--PEWR-KVPApRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLSIPlpqgaRYQAWTRKEPVGVVAGIVPWNFPLMIGM 181
Cdd:cd07131 80 ARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSELP-----NKDAMTRRQPIGVVALITPWNFPVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 182 WKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARA 261
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGET 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 262 AADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSP 341
Cdd:cd07131 234 CARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 342 EAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDG----KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADG 417
Cdd:cd07131 314 ETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 418 EEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTL-IDANLPFGGMKQSGTG-RDFGPDWLDGWCETKSV 495
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
....
gi 515953939 496 CVRY 499
Cdd:cd07131 474 YVDY 477
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-485 |
1.36e-139 |
|
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: 408.84 E-value: 1.36e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 58 DVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGkSINISRAFEVGCTLNWMRYTAGLTTK 137
Cdd:cd07104 1 DVDRAYAAAAAAQ--KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESG-STRPKAAFEVGAAIAILREAAGLPRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 138 IAGKTLdlsiPLPQGARYQAWTRkEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTL-LRVAELASEA 216
Cdd:cd07104 78 PEGEIL----PSDVPGKESMVRR-VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 217 GIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMT 296
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 297 GSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNR 376
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 377 gpdGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVW 456
Cdd:cd07104 313 ---YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVH 389
|
410 420 430
....*....|....*....|....*....|
gi 515953939 457 VNSHTLID-ANLPFGGMKQSGTGRdFGPDW 485
Cdd:cd07104 390 INDQTVNDePHVPFGGVKASGGGR-FGGPA 418
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
39-493 |
5.38e-139 |
|
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: 408.27 E-value: 5.38e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRa 118
Cdd:cd07145 3 VRNPANGEVIDTVPSLSREEVREAIEVAEKAK--DVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 FEVGCTLNWMRYTAGLTTKIAGKTldlsIPL---PQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIV 195
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGET----IPVdayEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 196 IKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGG 275
Cdd:cd07145 156 VKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 276 KNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCD 355
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 356 KVQAFLDEAKAHNAELIAGNRGPDgkGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASV 435
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 436 WTQNISKALAYTDRLQAGTVWVNSHTL--IDaNLPFGGMKQSGTGRDFGPDWLDGWCETK 493
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRfrWD-NLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
20-497 |
2.29e-137 |
|
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: 404.91 E-value: 2.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 20 HGLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVarSWAGRLPAERERILLRFADLVEQHGE 99
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK--TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 100 ELAQLETLEQGKSINISRAFEVGCTLNWMRYTAGL-------TTKIAGKTLDLsiplpqgaryqawTRKEPVGVVAGIVP 172
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGViraeegsANMIDEDTLSI-------------VLREPIGVVGQIIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 173 WNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGST 252
Cdd:cd07117 146 WNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 253 ATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKS 332
Cdd:cd07117 225 EVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFEN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 333 LSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNR----GPDGKGYYVSPTLVVNPDNHLRLTREEVFGPV 408
Cdd:cd07117 305 VKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHrlteNGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 409 VNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDG 488
Cdd:cd07117 385 ATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDA 464
|
....*....
gi 515953939 489 WCETKSVCV 497
Cdd:cd07117 465 YTQMKNIYI 473
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
39-497 |
1.71e-135 |
|
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: 399.28 E-value: 1.71e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFVArswAGRLPA-ERERILLRFADLVEQHGEELAQLETLEQGKSINISR 117
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKE---MKSLPAyERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 118 AfEVGCTLNWMRYTAGLTTKIAGKTldlsIPL---PQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSI 194
Cdd:cd07149 80 K-EVDRAIETLRLSAEEAKRLAGET----IPFdasPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 195 VIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAAdtLTGVTLELG 274
Cdd:cd07149 155 VLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 275 GKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHC 354
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 355 DKVQAFLDEAKAHNAELIAGNRgPDGKgyYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTAS 434
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGK-RDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 435 VWTQNISKALAYTDRLQAGTVWVN--SHTLIDAnLPFGGMKQSGTGRDfGPDW-LDGWCETKSVCV 497
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINdsSTFRVDH-MPYGGVKESGTGRE-GPRYaIEEMTEIKLVCF 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
40-497 |
1.19e-134 |
|
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: 397.10 E-value: 1.19e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 40 YNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAgRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRaF 119
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEAR-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 120 EVGCTLNWMRYTAGLTTKIAGKTLDlsiplPQGARYQAWTRkEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPS 199
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIE-----PEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 200 ETTPLTLLRVAELASEA-GIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07120 154 GQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAE-LIAGNRGPDG--KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASV 435
Cdd:cd07120 314 RMVERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953939 436 WTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
17-486 |
6.61e-133 |
|
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: 393.68 E-value: 6.61e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 17 DRQHGLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVarSWAGRLPAERERILLRFADLVEQ 96
Cdd:cd07111 19 DRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE--SWSALPGHVRARHLYRIARHIQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 97 HGEELAQLETLEQGKSINISRAFEVGCTLNWMRYTAGLttkiaGKTLDLSIPlpqgaryqAWtrkEPVGVVAGIVPWNFP 176
Cdd:cd07111 97 HQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGW-----AQLLDTELA--------GW---KPVGVVGQIVPWNFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 177 LMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGK 256
Cdd:cd07111 161 LLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 257 QIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVG 336
Cdd:cd07111 240 ALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 337 PGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVAD 416
Cdd:cd07111 320 DPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRT 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 417 GEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWL 486
Cdd:cd07111 400 AKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGL 469
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
9-499 |
2.57e-131 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 390.25 E-value: 2.57e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 9 LPGVQQFLDrqhGLWIEGRQAasdseKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAF---VARSWAGRLPAERER 85
Cdd:PLN02467 5 VPRRQLFIG---GEWREPVLG-----KRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 86 ILLRFADLVEQHGEELAQLETLEQGKSI--------NISRAFEvgctlnwmrYTAGLTTKIAGK-TLDLSIPLPQgarYQ 156
Cdd:PLN02467 77 YLRAIAAKITERKSELAKLETLDCGKPLdeaawdmdDVAGCFE---------YYADLAEALDAKqKAPVSLPMET---FK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 157 AWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAA 236
Cdd:PLN02467 145 GYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 237 LTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEA 316
Cdd:PLN02467 225 LASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 317 PLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDG--KGYYVSPTLVVNPD 394
Cdd:PLN02467 305 RIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 395 NHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVwtqnISKALAYTDR----LQAGTVWVNSHTLIDANLPFG 470
Cdd:PLN02467 385 TSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAV----ISNDLERCERvseaFQAGIVWINCSQPCFCQAPWG 460
|
490 500
....*....|....*....|....*....
gi 515953939 471 GMKQSGTGRDFGPDWLDGWCETKSVcVRY 499
Cdd:PLN02467 461 GIKRSGFGRELGEWGLENYLSVKQV-TKY 488
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
22-495 |
9.15e-131 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 389.94 E-value: 9.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 22 LWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGM 181
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTV------PADGPHHVQTLHEPIGVAGQIIPWNFPLLMFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 182 WKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARA 261
Cdd:PLN02466 214 WKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 262 AADT-LTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLV----------------- 323
Cdd:PLN02466 294 AAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVekakaralkrvvgdpfk 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 324 SGFEQavkslsvGPGMSPEAFinplvsrahcDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREE 403
Cdd:PLN02466 374 KGVEQ-------GPQIDSEQF----------EKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 404 VFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGP 483
Cdd:PLN02466 437 IFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGI 516
|
490
....*....|..
gi 515953939 484 DWLDGWCETKSV 495
Cdd:PLN02466 517 YSLNNYLQVKAV 528
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-495 |
3.27e-128 |
|
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: 380.41 E-value: 3.27e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 40 YNPATGEVIASTADASVDDVDRAVMSGWRAfvARSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAf 119
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAA--QRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 120 EVGCTLNWMRYTAglttKIAGKTL-DLSIPLPQGARYQ-AWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIK 197
Cdd:cd07099 78 EVLLALEAIDWAA----RNAPRVLaPRKVPTGLLMPNKkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 198 PSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHpRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKN 277
Cdd:cd07099 154 PSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 278 PAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKV 357
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 358 QAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWT 437
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 438 QNISKALAYTDRLQAGTVWVNSHTLIDAN--LPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
23-498 |
8.01e-127 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 377.91 E-value: 8.01e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 23 WIEGRQAASDseKRLNVYNPATGEVIASTADASVDDVDRAVMSGwRAFVARSWAGRLPAERERILLRFADLVEQHGEELA 102
Cdd:TIGR03216 4 FINGAFVESG--KTFANINPVDGRVIARVHEAGAAEVDAAVAAA-RAALKGPWGKMTVAERADLLYAVADEIERRFDDFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 103 QLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLsiPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMW 182
Cdd:TIGR03216 81 AAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTECFEM--ATPDGKGALNYAVRKPLGVVGVISPWNLPLLLMTW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 183 KVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSG-AVCGAALTSHPRIAKVSFTGSTATGKQIARA 261
Cdd:TIGR03216 159 KVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGpDSAGEFLTRHPGVDAITFTGETRTGSAIMKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 262 AADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSP 341
Cdd:TIGR03216 239 AADGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 342 EAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPD-----GKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVAD 416
Cdd:TIGR03216 319 ATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVPDfgdalAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 417 GEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVC 496
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVC 478
|
..
gi 515953939 497 VR 498
Cdd:TIGR03216 479 IK 480
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-495 |
2.73e-126 |
|
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: 375.43 E-value: 2.73e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 40 YNPATGEVIASTADASVDDVDRAVMsgwRAFVA-RSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALE---RARAAqKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 fEVGCTLNWMRYTAglttKIAGKTLdLSIPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:cd07102 78 -EIRGMLERARYMI----SIAEEAL-ADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNP 278
Cdd:cd07102 152 SPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 279 AIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQ 358
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 359 AFLDEAKAHNAE-LIAGNRGP--DGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASV 435
Cdd:cd07102 311 AQIADAIAKGARaLIDGALFPedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 436 WTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
37-497 |
8.17e-126 |
|
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: 374.46 E-value: 8.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 37 LNVYNPATGEVIASTADASVDDVDRAVMSGWRAfvARSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINIS 116
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAG--AENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 117 RaFEVGCTLNWMRYTAGLTTKIAGKTLDLSIPLPQGARyQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVI 196
Cdd:cd07094 79 R-VEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNR-LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 197 KPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAAdtLTGVTLELGGK 276
Cdd:cd07094 157 KPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 277 NPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDK 356
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 357 VQAFLDEAKAHNAELIAGNRgPDGKGYYvsPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVW 436
Cdd:cd07094 315 VERWVEEAVEAGARLLCGGE-RDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953939 437 TQNISKALAYTDRLQAGTVWVNSHTLIDA-NLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
30-497 |
1.97e-125 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 375.76 E-value: 1.97e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 30 ASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMsgwRAFVA-RSWAGRLPAERERILLRFADLVEQHGEELAQLETLE 108
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFA---RARAAqRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 109 QGKSinisR--AFE-----VGCTLNWMRYTAGL--TTKIAGktldlSIPLPQGARyqawTRKEPVGVVAGIVPWNFPLMI 179
Cdd:PRK09407 104 TGKA----RrhAFEevldvALTARYYARRAPKLlaPRRRAG-----ALPVLTKTT----ELRQPKGVVGVISPWNYPLTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 180 GMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHprIAKVSFTGSTATGKQIA 259
Cdd:PRK09407 171 AVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 260 RAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGM 339
Cdd:PRK09407 249 EQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 340 SPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRG-PDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGE 418
Cdd:PRK09407 329 DYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKArPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 419 EALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVN-----SHTLIDAnlPFGGMKQSGTGRDFGPDWLDGWCETK 493
Cdd:PRK09407 409 EAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVDA--PMGGMKDSGLGRRHGAEGLLKYTESQ 486
|
....
gi 515953939 494 SVCV 497
Cdd:PRK09407 487 TIAT 490
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
39-493 |
3.94e-125 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 372.53 E-value: 3.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA 118
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAF--KTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 119 fEVGCTLNWMRYTAGLTTKIAGKTldlsIPLPQGARyQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:TIGR01780 79 -EILYAASFLEWFAEEAKRVYGDT----IPSPQSDK-RLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLRVAELASEAGIPEGVFNVVTGSGAV-CGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKN 277
Cdd:TIGR01780 153 AEQTPLSALALARLAEQAGIPKGVLNVITGSRAKeVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 278 PAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKV 357
Cdd:TIGR01780 233 PFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 358 QAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWT 437
Cdd:TIGR01780 313 EKHIADAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 438 QNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETK 493
Cdd:TIGR01780 393 RDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
22-495 |
2.45e-124 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 372.31 E-value: 2.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 22 LWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAFEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGM 181
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVA------TTSSHELAMIVREPVGVIAAIVPWNFPLLLTC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 182 WKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARA 261
Cdd:PRK09847 176 WKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 262 AADT-LTGVTLELGGKNPAIVLKDA-DPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGM 339
Cdd:PRK09847 256 AGDSnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 340 SPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRgpDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEE 419
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRN--AGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQ 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 420 ALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:PRK09847 414 ALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
24-499 |
4.02e-124 |
|
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: 370.74 E-value: 4.02e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 24 IEGRQAASDSEkRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAgRLPA-ERERILLRFADLVEQHGEELA 102
Cdd:cd07086 3 IGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWR-KVPApRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 103 QLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLSIPlpqgaRYQAWTRKEPVGVVAGIVPWNFPLMIGMW 182
Cdd:cd07086 79 RLVSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTIPSERP-----GHRLMEQWNPLGVVGVITAFNFPVAVPGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 183 KVMPALAAGCSIVIKPSETTPLTLLRVAELASEA----GIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQI 258
Cdd:cd07086 153 NAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 259 ARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPG 338
Cdd:cd07086 232 GETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 339 MSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDG--KGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVAD 416
Cdd:cd07086 312 LDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 417 GEEALQLANDTEYGLTASVWTQNISKALAYTDR--LQAGTVWVNSHTlIDA--NLPFGGMKQSGTGRDFGPDWLDGWCET 492
Cdd:cd07086 392 LEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPT-SGAeiGGAFGGEKETGGGRESGSDAWKQYMRR 470
|
....*..
gi 515953939 493 KSVCVRY 499
Cdd:cd07086 471 STCTINY 477
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
21-497 |
4.88e-124 |
|
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: 370.10 E-value: 4.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGrqaasDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAfvARSWAGRLPAERERILLRFADLVEQHGEE 100
Cdd:cd07151 1 GEWRDG-----TSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 101 LAQLETLEQGKSInISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLSIPLPQGARYqawtrKEPVGVVAGIVPWNFPLMIG 180
Cdd:cd07151 74 IVEWLIRESGSTR-IKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVY-----REPLGVVGVISPWNFPLHLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 181 MWKVMPALAAGCSIVIKPSETTPLT--LLrVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPrIAKV-SFTGSTATGKQ 257
Cdd:cd07151 148 MRSVAPALALGNAVVLKPASDTPITggLL-LAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHP-VPRLiSFTGSTPVGRH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 258 IARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGP 337
Cdd:cd07151 226 IGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 338 GMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNrgpDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADG 417
Cdd:cd07151 306 PSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 418 EEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLID-ANLPFGGMKQSGTGRdFGPDW-LDGWCETKSV 495
Cdd:cd07151 383 EEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSGLGR-FNGEWaLEEFTTDKWI 461
|
..
gi 515953939 496 CV 497
Cdd:cd07151 462 SV 463
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-495 |
3.97e-123 |
|
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: 366.90 E-value: 3.97e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 58 DVDRAVMSGWRAFVArsWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRaFEVGCTLNWMRYTAGLTTK 137
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 138 IAGKTldlsIPLPQGARYqAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAG 217
Cdd:cd07105 78 IIGGS----IPSDKPGTL-AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 218 IPEGVFNVVTGS---GAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGL 294
Cdd:cd07105 153 LPKGVLNVVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 295 MTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPeafinPLVSRAHCDKVQAFLDEAKAHNAELIAG 374
Cdd:cd07105 233 LFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLG-----SLVSAAAADRVKELVDDALSKGAKLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 375 NRGPDGK-GYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAG 453
Cdd:cd07105 308 GLADESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 515953939 454 TVWVNSHTLID-ANLPFGGMKQSGTGRdFGPDW-LDGWCETKSV 495
Cdd:cd07105 388 AVHINGMTVHDePTLPHGGVKSSGYGR-FNGKWgIDEFTETKWI 430
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
42-497 |
1.44e-121 |
|
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: 363.55 E-value: 1.44e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 42 PATGEVIASTADASVDDVDRAVMSGWRAfvARSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKsiNISRAF-E 120
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGK--ARRHAFeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 121 VGCTLNWMRYTAglttKIAGKTLDL-----SIPLPQGARYQawtrKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIV 195
Cdd:cd07101 79 VLDVAIVARYYA----RRAERLLKPrrrrgAIPVLTRTTVN----RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 196 IKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIakVSFTGSTATGKQIARAAADTLTGVTLELGG 275
Cdd:cd07101 151 LKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 276 KNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCD 355
Cdd:cd07101 229 KNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 356 KVQAFLDEAKAHNAELIAGNRG-PDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTAS 434
Cdd:cd07101 309 RVTAHVDDAVAKGATVLAGGRArPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953939 435 VWTQNISKALAYTDRLQAGTVWVN-----SHTLIDAnlPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNegyaaAWASIDA--PMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-497 |
2.53e-121 |
|
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: 362.16 E-value: 2.53e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 59 VDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAgltTKI 138
Cdd:cd07100 1 IEAALDRAHAAF--LAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYA---ENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 139 AGKTLDLSIPLPQGaryQAWTRKEPVGVVAGIVPWNFPLmigmWKVM----PALAAGCSIVIKPSETTPLTLLRVAELAS 214
Cdd:cd07100 75 EAFLADEPIETDAG---KAYVRYEPLGVVLGIMPWNFPF----WQVFrfaaPNLMAGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 215 EAGIPEGVF-NVVTGSGAVcgAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEG 293
Cdd:cd07100 148 EAGFPEGVFqNLLIDSDQV--EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 294 LMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIA 373
Cdd:cd07100 226 AVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 374 GNRGPDGKGYYVSPTLVVN--PDNhlRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQ 451
Cdd:cd07100 306 GGKRPDGPGAFYPPTVLTDvtPGM--PAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 515953939 452 AGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07100 384 AGMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-499 |
1.09e-115 |
|
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: 350.37 E-value: 1.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 12 VQQFLDRQHGLWIEGRQAasDSEKRLNVYNPA-TGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRF 90
Cdd:cd07124 25 VREELGREYPLVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAF--PTWRRTPPEERARLLLRA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 91 ADLVEQHGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLdLSIPLPQGaRYqawtRKEPVGVVAGI 170
Cdd:cd07124 101 AALLRRRRFELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPV-EMVPGEDN-RY----VYRPLGVGAVI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 171 VPWNFPLMI--GMwkVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSF 248
Cdd:cd07124 174 SPWNFPLAIlaGM--TTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 249 TGSTATGKQIARAAADTLTG------VTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTL 322
Cdd:cd07124 252 TGSREVGLRIYERAAKVQPGqkwlkrVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 323 VSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAhNAELIAGNRGPDG--KGYYVSPTLVVNPDNHLRLT 400
Cdd:cd07124 332 LERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKS-EGRLLLGGEVLELaaEGYFVQPTIFADVPPDHRLA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 401 REEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHT---LIDANlPFGGMKQSGT 477
Cdd:cd07124 411 QEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKItgaLVGRQ-PFGGFKMSGT 489
|
490 500
....*....|....*....|...
gi 515953939 478 G-RDFGPDWLDGWCETKSVCVRY 499
Cdd:cd07124 490 GsKAGGPDYLLQFMQPKTVTENF 512
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
22-499 |
4.04e-114 |
|
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: 345.27 E-value: 4.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 22 LWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAF--PAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLSiplpqGARYQAWTRKEPVGVVAGIVPWNFPLMIGM 181
Cdd:cd07085 81 ARLITLEHGKTLADARG-DVLRGLEVVEFACSIPHLLKGEYLENV-----ARGIDTYSYRQPLGVVAGITPFNFPAMIPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 182 WKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQI-AR 260
Cdd:cd07085 155 WMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEA-VNALLDHPDIKAVSFVGSTPVGEYIyER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 261 AAAdtlTG--VTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPG 338
Cdd:cd07085 234 AAA---NGkrVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 339 MSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRG--PDG--KGYYVSPTLV--VNPDnhLRLTREEVFGPVVNLV 412
Cdd:cd07085 311 DDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGvkVPGyeNGNFVGPTILdnVTPD--MKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 413 RVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNshtlID-----ANLPFGGMKQS--GTGRDFGPDW 485
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPipvplAFFSFGGWKGSffGDLHFYGKDG 464
|
490
....*....|....
gi 515953939 486 LDGWCETKSVCVRY 499
Cdd:cd07085 465 VRFYTQTKTVTSRW 478
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-479 |
1.48e-112 |
|
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: 340.38 E-value: 1.48e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 37 LNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVArswAGRLPA-ERERILLRFADLVEQHGEELAQLETLEQGKSINI 115
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRP---MRALPAhRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 116 SRAfEVGCTLNWMRYTAGLTTKIAGKTLDLSIpLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIV 195
Cdd:cd07147 78 ARG-EVARAIDTFRIAAEEATRIYGEVLPLDI-SARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 196 IKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQI-ARAAADTltgVTLELG 274
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLkARAGKKK---VVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 275 GKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHC 354
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 355 DKVQAFLDEAKAHNAELIAGNRgpdGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTAS 434
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 515953939 435 VWTQNISKALAYTDRLQAGTVWVN--SHTLIDaNLPFGGMKQSGTGR 479
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINdvPTFRVD-HMPYGGVKDSGIGR 434
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
21-479 |
9.65e-112 |
|
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: 339.16 E-value: 9.65e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGrqaasdSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLP-AERERILLRFADLVEQHGE 99
Cdd:cd07082 8 GEWKES------SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG--RGWWPTMPlEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 100 ELAQLETLEQGKSINISRAfEVGCTLNWMRYTAglttkIAGKTLDL-SIPLPQGARYQ---AWTRKEPVGVVAGIVPWNF 175
Cdd:cd07082 80 EVANLLMWEIGKTLKDALK-EVDRTIDYIRDTI-----EELKRLDGdSLPGDWFPGTKgkiAQVRREPLGVVLAIGPFNY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 176 PLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATG 255
Cdd:cd07082 154 PLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 256 KQIARAAAdtLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSV 335
Cdd:cd07082 234 NRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 336 GPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGpdGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVA 415
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 416 DGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTL--IDaNLPFGGMKQSGTGR 479
Cdd:cd07082 390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgPD-HFPFLGRKDSGIGT 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
45-482 |
6.20e-111 |
|
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: 335.80 E-value: 6.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 45 GEVIASTADASVDDVDRAVMSGWRAfvARSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGkSINISRAFEVGCT 124
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-SIRPKAGFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 125 LNWMRYTAGLTTKIAGKTLdlsiplPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPL 204
Cdd:cd07152 78 IGELHEAAGLPTQPQGEIL------PSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 205 TL-LRVAELASEAGIPEGVFNVVTGsGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLK 283
Cdd:cd07152 152 SGgVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 284 DADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDE 363
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 364 AKAHNAELIAGNRgpdGKGYYVSPTLV--VNPDNhlRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNIS 441
Cdd:cd07152 311 SVAAGARLEAGGT---YDGLFYRPTVLsgVKPGM--PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 515953939 442 KALAYTDRLQAGTVWVNSHTLID-ANLPFGGMKQSGTGRDFG 482
Cdd:cd07152 386 RAMALADRLRTGMLHINDQTVNDePHNPFGGMGASGNGSRFG 427
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
42-499 |
7.65e-111 |
|
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: 337.12 E-value: 7.65e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 42 PATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAFEV 121
Cdd:cd07116 23 PVTGKVFCEVPRSTAEDIELALDAAHAAK--EAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAADI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 122 GCTLNWMRYTAGLTTKIAGKTLDLSiplpqgARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSET 201
Cdd:cd07116 101 PLAIDHFRYFAGCIRAQEGSISEID------ENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 202 TPLTLLRVAELASEAgIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIV 281
Cdd:cd07116 175 TPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 282 LKD---ADPAWV---IEGLMTGSFlNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCD 355
Cdd:cd07116 254 FADvmdADDAFFdkaLEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 356 KVQAFLDEAKAHNAELIAG----NRGPDGKGYYVSPTLVVNpDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGL 431
Cdd:cd07116 333 KILSYIDIGKEEGAEVLTGgernELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGL 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953939 432 TASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCVRY 499
Cdd:cd07116 412 GAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSY 479
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
37-478 |
3.48e-105 |
|
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: 321.62 E-value: 3.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 37 LNVYNPATGEVIASTADASVDDVDRAVMSgwrafvARSWAGRLPA-ERERILLRFADLVEQHGEELAQLETLEQGKSINI 115
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAL------AASYRSTLTRyQRSAILNKAAALLEARREEFARLITLESGLCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 116 SRaFEVGCTLNWMRYTAGLTTKIAGKTLDLSIPLPQGARyQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIV 195
Cdd:cd07146 75 TR-YEVGRAADVLRFAAAEALRDDGESFSCDLTANGKAR-KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 196 IKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAAdtLTGVTLELGG 275
Cdd:cd07146 153 LKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 276 KNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCD 355
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 356 KVQAFLDEAKAHNAELIAGNRgpdGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASV 435
Cdd:cd07146 311 QIENRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 515953939 436 WTQNISKALAYTDRLQAGTVWVNSHTLIDANL-PFGGMKQSGTG 478
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNEVPGFRSELsPFGGVKDSGLG 431
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
16-497 |
4.57e-105 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 322.24 E-value: 4.57e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 16 LDRQHGLwIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVArsWAGRLPAERERILLRFADLVE 95
Cdd:PRK11241 8 LFRQQAL-INGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRRWFNLMM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 96 QHGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTldlsIPLPQGARyQAWTRKEPVGVVAGIVPWNF 175
Cdd:PRK11241 85 EHQDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDT----IPGHQADK-RLIVIKQPIGVTAAITPWNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 176 PLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATG 255
Cdd:PRK11241 159 PAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 256 KQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSV 335
Cdd:PRK11241 239 RQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 336 GPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVA 415
Cdd:PRK11241 319 GDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 416 DGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:PRK11241 399 DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYM 478
|
..
gi 515953939 496 CV 497
Cdd:PRK11241 479 CI 480
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
12-499 |
9.16e-100 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 309.56 E-value: 9.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 12 VQQFLDRQHGLWIEGRQAasDSEKRLNVYNPA-TGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRF 90
Cdd:PRK03137 29 VEKELGQDYPLIIGGERI--TTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAF--ETWKKWSPEDRARILLRA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 91 ADLVEQHGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIA-GKTLdlsIPLPqGARYQawTRKEPVGVVAG 169
Cdd:PRK03137 105 AAIIRRRKHEFSAWLVKEAGKPWAEADA-DTAEAIDFLEYYARQMLKLAdGKPV---ESRP-GEHNR--YFYIPLGVGVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 170 IVPWNFPL--MIGMwkVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVS 247
Cdd:PRK03137 178 ISPWNFPFaiMAGM--TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFIT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 248 FTGSTATGKQIARAAADTLTG------VTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDT 321
Cdd:PRK03137 256 FTGSREVGLRIYERAAKVQPGqiwlkrVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 322 LVSGFEQAVKSLSVGPGMSPeAFINPLVSRAHCDKVQAFLDEAKAhNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTR 401
Cdd:PRK03137 336 VLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKE-EGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 402 EEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQN---ISKALA-------YTDRLQAGTVwVNSHtlidanlPFGG 471
Cdd:PRK03137 414 EEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNrehLEKARRefhvgnlYFNRGCTGAI-VGYH-------PFGG 485
|
490 500
....*....|....*....|....*....
gi 515953939 472 MKQSGT-GRDFGPDWLDGWCETKSVCVRY 499
Cdd:PRK03137 486 FNMSGTdSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
87-499 |
2.00e-98 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 302.81 E-value: 2.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 87 LLRFADLVEQHGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLSIPlpqgaRYQAWTRKEPVGV 166
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDYMAEWARRYEGEIIQSDRP-----GENILLFKRALGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 167 VAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKV 246
Cdd:PRK10090 75 TTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 247 SFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGF 326
Cdd:PRK10090 155 SMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 327 EQAVKSLSVG-PGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVF 405
Cdd:PRK10090 235 GEAMQAVQFGnPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 406 GPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLiDANLPF-GGMKQSGTGRDFGPD 484
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENF-EAMQGFhAGWRKSGIGGADGKH 393
|
410
....*....|....*
gi 515953939 485 WLDGWCETKSVCVRY 499
Cdd:PRK10090 394 GLHEYLQTQVVYLQS 408
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
40-497 |
1.07e-95 |
|
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: 297.29 E-value: 1.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 40 YNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSiNISRAF 119
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQ--REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKT-MVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 120 -EVGCTLNWMRYTAglttKIAGKTLDlsiPLPQGARYQAWTRK-----EPVGVVAGIVPWNFPLMIGMWKVMPALAAGCS 193
Cdd:cd07098 78 gEILVTCEKIRWTL----KHGEKALR---PESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 194 IVIKPSETTP------LTLLRvaELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIARAAADTLT 267
Cdd:cd07098 151 IVVKVSEQVAwssgffLSIIR--ECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 268 GVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINP 347
Cdd:cd07098 228 PVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 348 LVSRAHCDKVQAFLDEAKAHNAELIAG----NRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQL 423
Cdd:cd07098 308 MISPARFDRLEELVADAVEKGARLLAGgkryPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 424 ANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVN--SHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSVCV 497
Cdd:cd07098 388 ANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
41-495 |
6.79e-95 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 295.11 E-value: 6.79e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 41 NPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAfE 120
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARF--RDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA-E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 121 VGCTLNWMRYTAGLTTK-IAGKTLDLSiplPQGARyQAWTRKEPVGVVAGIVPWNFPLmigmWKVM----PALAAGCSIV 195
Cdd:PRK09406 84 ALKCAKGFRYYAEHAEAlLADEPADAA---AVGAS-RAYVRYQPLGVVLAVMPWNFPL----WQVVrfaaPALMAGNVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 196 IKPSETTPLTLLRVAELASEAGIPEGVF-NVVTGSGAVcgAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELG 274
Cdd:PRK09406 156 LKHASNVPQTALYLADLFRRAGFPDGCFqTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 275 GKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHC 354
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 355 DKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTAS 434
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953939 435 VWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:PRK09406 394 AWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
19-495 |
1.81e-89 |
|
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: 282.55 E-value: 1.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 19 QHGLWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHG 98
Cdd:cd07083 17 RAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 99 EELAQLETLEQGKSInISRAFEVGCTLNWMRYTAGLTTKIAGKTLDLsiPLPQGARYQAWTRkePVGVVAGIVPWNFPLM 178
Cdd:cd07083 95 RELIATLTYEVGKNW-VEAIDDVAEAIDFIRYYARAALRLRYPAVEV--VPYPGEDNESFYV--GLGAGVVISPWNFPVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 179 IGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQI 258
Cdd:cd07083 170 IFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 259 ARAAADTLTGVT------LELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKS 332
Cdd:cd07083 250 YEAAARLAPGQTwfkrlyVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAER 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 333 LSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKaHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLV 412
Cdd:cd07083 330 LSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGK-NEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 413 RVADGE--EALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTL--IDANLPFGGMKQSGTG-RDFGPDWLD 487
Cdd:cd07083 409 RYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITgaLVGVQPFGGFKLSGTNaKTGGPHYLR 488
|
....*...
gi 515953939 488 GWCETKSV 495
Cdd:cd07083 489 RFLEMKAV 496
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
22-499 |
6.40e-84 |
|
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: 267.52 E-value: 6.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 22 LWIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVarSWAGRLPAERERILLRFADLVEQHGEEL 101
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFL--TWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLdlsiplPQGAR-YQAWTRKEPVGVVAGIVPWNFPLMIG 180
Cdd:TIGR01722 81 AELITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETS------TQVATrVDVYSIRQPLGVCAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 181 MWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGsGAVCGAALTSHPRIAKVSFTGSTATGKQIAR 260
Cdd:TIGR01722 154 LWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 261 AAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAA-SSRIYIEAPlfDTLVSGFEQAVKSLSVGPGM 339
Cdd:TIGR01722 233 TGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAiSAAVLVGAA--DEWVPEIRERAEKIRIGPGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 340 SPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGY----YVSPTLVVNPDNHLRLTREEVFGPVVNLVRVA 415
Cdd:TIGR01722 311 DPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 416 DGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNshTLIDANLP---FGGMKQS--GTGRDFGPDWLDGWC 490
Cdd:TIGR01722 391 TLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN--VPIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYT 468
|
....*....
gi 515953939 491 ETKSVCVRY 499
Cdd:TIGR01722 469 RGKTVTTRW 477
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
29-497 |
4.53e-82 |
|
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: 263.67 E-value: 4.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 29 AASDSEKRLNVYNPATGE-VIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETL 107
Cdd:cd07125 40 EETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGELIALAAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 108 EQGKSINISRAfEVGCTLNWMRYTAglttKIAGKTL-DLSIPLPQGARYQAwtRKEPVGVVAGIVPWNFPLMIGMWKVMP 186
Cdd:cd07125 118 EAGKTLADADA-EVREAIDFCRYYA----AQARELFsDPELPGPTGELNGL--ELHGRGVFVCISPWNFPLAIFTGQIAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 187 ALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARA-AADT 265
Cdd:cd07125 191 ALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRAlAERD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 266 LTGVTL--ELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEA 343
Cdd:cd07125 271 GPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLST 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 344 FINPLVSRAHCDKVQAfLDEAKAHNAELIAGNRGPDGKGYYVSPTLV--VNPDNHLRltreEVFGPVVNLVRVADG--EE 419
Cdd:cd07125 351 DVGPLIDKPAGKLLRA-HTELMRGEAWLIAPAPLDDGNGYFVAPGIIeiVGIFDLTT----EVFGPILHVIRFKAEdlDE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 420 ALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTlIDANL---PFGGMKQSGTGRDFG-PDWLDGWCETKSV 495
Cdd:cd07125 426 AIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI-TGAIVgrqPFGGWGLSGTGPKAGgPNYLLRFGNEKTV 504
|
..
gi 515953939 496 CV 497
Cdd:cd07125 505 SL 506
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
37-478 |
1.72e-80 |
|
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: 257.73 E-value: 1.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 37 LNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVARSwaGRLPA-ERERILLRFADLVEQHGEELAQLETLEQGKSINI 115
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRN--NWLPAhERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 116 SRAfEVGCTLNWMRYTAGLTTKIAGKtldlSIPL---PQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGC 192
Cdd:cd07148 79 AKV-EVTRAIDGVELAADELGQLGGR----EIPMgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 193 SIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIaRAAADTLTGVTLE 272
Cdd:cd07148 154 PVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAV-AEKLVTDPRVAFFSFIGSARVGWML-RSKLAPGTRCALE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 273 LGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRA 352
Cdd:cd07148 232 HGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 353 HCDKVQAFLDEAKAHNAELIAGNRgPDGKGYYvSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLT 432
Cdd:cd07148 312 EVDRVEEWVNEAVAAGARLLCGGK-RLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 515953939 433 ASVWTQNISKALAYTDRLQAGTVWVNSHTLIDAN-LPFGGMKQSGTG 478
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
41-495 |
3.38e-80 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 257.10 E-value: 3.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 41 NPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAfE 120
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGF--RDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 121 VGCTLNWMRYTA--GLTTKIAGKTLdlsiplpqGARYQAWTRKEPVGVVAGIVPWNFPLmigmWKVM----PALAAGCSI 194
Cdd:PRK13968 90 VAKSANLCDWYAehGPAMLKAEPTL--------VENQQAVIEYRPLGTILAIMPWNFPL----WQVMrgavPILLAGNGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 195 VIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTShPRIAKVSFTGSTATGKQIARAAADTLTGVTLELG 274
Cdd:PRK13968 158 LLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 275 GKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHC 354
Cdd:PRK13968 237 GSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 355 DKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTAS 434
Cdd:PRK13968 317 DELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953939 435 VWTQNISKALAYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRDFGPDWLDGWCETKSV 495
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-479 |
1.07e-76 |
|
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: 247.18 E-value: 1.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 58 DVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRAfEVGCTLNwmrytaglttK 137
Cdd:cd07095 1 QVDAAVAAARAAF--PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQT-EVAAMAG----------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 138 IA-------GKTLDLSIPLPQGaryQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVA 210
Cdd:cd07095 68 IDisikayhERTGERATPMAQG---RAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 211 ELASEAGIPEGVFNVVTGSGAvCGAALTSHPRIAKVSFTGSTATGKQIARAAADTlTGV--TLELGGKNPAIVLKDADPA 288
Cdd:cd07095 145 ELWEEAGLPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGR-PGKilALEMGGNNPLVVWDVADID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 289 WVIEGLMTGSFLNQGQVCAASSRIYIEAPLF-DTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAH 367
Cdd:cd07095 223 AAAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 368 NAELIAGNRGPDGKGYYVSPTLV------VNPDnhlrltrEEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNIS 441
Cdd:cd07095 303 GGEPLLAMERLVAGTAFLSPGIIdvtdaaDVPD-------EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEA 375
|
410 420 430
....*....|....*....|....*....|....*....
gi 515953939 442 KALAYTDRLQAGTV-WVNSHTLIDANLPFGGMKQSGTGR 479
Cdd:cd07095 376 LFERFLARIRAGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
33-485 |
6.10e-76 |
|
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: 246.35 E-value: 6.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 33 SEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFvaRSWAgRLPA-ERERILLRFADLVEQHGEELAQLETLEQGK 111
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAF--KEWR-DVPApKRGEIVRQIGDALRKKKEALGKLVSLEMGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 112 SINISRAfEVGCTLNWMRYTAGLTTKIAGKTldlsIP--LPQGARYQAWtrkEPVGVVAGIVPWNFPLMIGMWKVMPALA 189
Cdd:cd07130 87 ILPEGLG-EVQEMIDICDFAVGLSRQLYGLT----IPseRPGHRMMEQW---NPLGVVGVITAFNFPVAVWGWNAAIALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 190 AGCSIVIKPSETTPLTLLRVAELASEA----GIPEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIARAAADT 265
Cdd:cd07130 159 CGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 266 LTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFI 345
Cdd:cd07130 238 FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 346 NPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTlVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLAN 425
Cdd:cd07130 318 GPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPT-IVEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515953939 426 DTEYGLTASVWTQNISKALAYTDRLQA--GTVWVN---SHTLIDAnlPFGGMKQSGTGRDFGPD-W 485
Cdd:cd07130 397 EVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNigtSGAEIGG--AFGGEKETGGGRESGSDaW 460
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
83-479 |
2.34e-71 |
|
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: 233.19 E-value: 2.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 83 RERILLRFADLVEQHGEELAqlETLEQ--GKSINISRAFEVGCTLNWMRYTAGLTTKIAgKTLDLSIPLPQGArYQAWTR 160
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIA--AALYAdlGKPPAEAYLTEIAVVLGEIDHALKHLKKWM-KPRRVSVPLLLQP-AKAYVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 161 KEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVCgAALTSH 240
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVA-TALLAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 241 PrIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFD 320
Cdd:cd07087 176 P-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 321 TLVSGFEQAVKSLsVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAhnaeLIAGNRGPDGKgyYVSPTLVVNPDNHLRLT 400
Cdd:cd07087 255 ELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGKV----VIGGQVDKEER--YIAPTILDDVSPDSPLM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 401 REEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNS---HTLIDaNLPFGGMKQSGT 477
Cdd:cd07087 328 QEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvllHAAIP-NLPFGGVGNSGM 406
|
..
gi 515953939 478 GR 479
Cdd:cd07087 407 GA 408
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
21-479 |
2.15e-68 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 227.15 E-value: 2.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGRQAASDSEkRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVArsWAGRLPAERERILLRFADLVEQHGEE 100
Cdd:PRK09457 2 TLWINGDWIAGQGE-AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 101 LAQLETLEQGKSINISRAfEVgctlnwmrytagltTKIAGKtLDLSI------------PLPQGaryQAWTRKEPVGVVA 168
Cdd:PRK09457 79 LAEVIARETGKPLWEAAT-EV--------------TAMINK-IAISIqayhertgekrsEMADG---AAVLRHRPHGVVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 169 GIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGsGAVCGAALTSHPRIAKVSF 248
Cdd:PRK09457 140 VFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 249 TGSTATGKQIARA-AADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLF-DTLVSGF 326
Cdd:PRK09457 219 TGSANTGYLLHRQfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 327 EQAVKSLSVG-PGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSP-----TLVVN-PDnhlrl 399
Cdd:PRK09457 299 VAVAKRLTVGrWDAEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPgiidvTGVAElPD----- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 400 trEEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTV-WVNSHTLIDANLPFGGMKQSGTG 478
Cdd:PRK09457 374 --EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNH 451
|
.
gi 515953939 479 R 479
Cdd:PRK09457 452 R 452
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
81-479 |
4.63e-65 |
|
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: 216.58 E-value: 4.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 81 AERERILLRFADLVEQHGEELAqlETLEQ---GKSINISRAFEVGCTLNWMRYTAglttkiagKTLD-------LSIPLP 150
Cdd:cd07133 20 EERRDRLDRLKALLLDNQDALA--EAISAdfgHRSRHETLLAEILPSIAGIKHAR--------KHLKkwmkpsrRHVGLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 151 -QGARyqAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAgIPEGVFNVVTGS 229
Cdd:cd07133 90 fLPAK--AEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 230 GAVcGAALTSHPrIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAAS 309
Cdd:cd07133 167 ADV-AAAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 310 SRIYIEAPLFDTLVSGFEQAVKSlsvgpgMSPEAFINP----LVSRAHCDKVQAFLDEAKAHNAELI--AGNRGPDGKGY 383
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAK------MYPTLADNPdytsIINERHYARLQGLLEDARAKGARVIelNPAGEDFAATR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 384 YVSPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVN---SH 460
Cdd:cd07133 319 KLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtlLH 398
|
410
....*....|....*....
gi 515953939 461 TLIDaNLPFGGMKQSGTGR 479
Cdd:cd07133 399 VAQD-DLPFGGVGASGMGA 416
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
156-479 |
6.76e-65 |
|
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: 216.32 E-value: 6.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 156 QAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVCGA 235
Cdd:cd07135 101 KPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 236 ALTShpRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIE 315
Cdd:cd07135 180 LLEQ--KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 316 APLFDTLVSGFEQAVKSLSVGPGMSPEAFINpLVSRAHCDKVQAFLDEAKahnAELIAGNRGpDGKGYYVSPTLVVNPDN 395
Cdd:cd07135 258 PSVYDEFVEELKKVLDEFYPGGANASPDYTR-IVNPRHFNRLKSLLDTTK---GKVVIGGEM-DEATRFIPPTIVSDVSW 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 396 HLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNS---HTLIDaNLPFGGM 472
Cdd:cd07135 333 DDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDtliHVGVD-NAPFGGV 411
|
....*..
gi 515953939 473 KQSGTGR 479
Cdd:cd07135 412 GDSGYGA 418
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
23-478 |
2.70e-64 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 216.55 E-value: 2.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 23 WIEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAfvARSWAgRLPA-ERERILLRFADLVEQHGEEL 101
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWA-KTPLwKRAELLHKAAAILKEHKAPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 102 AQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGK-TLDLSIPLPQGARYQ-AWTRKEPVGVVAGIVPWNFPLMI 179
Cdd:PLN00412 96 AECLVKEIAKPAKDAVT-EVVRSGDLISYTAEEGVRILGEgKFLVSDSFPGNERNKyCLTSKIPLGVVLAIPPFNYPVNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 180 GMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTaTGKQIA 259
Cdd:PLN00412 175 AVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGIAIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 260 RAAAdtLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPgm 339
Cdd:PLN00412 254 KKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP-- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 340 sPE--AFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGpdgKGYYVSPTLV--VNPDnhLRLTREEVFGPVVNLVRVA 415
Cdd:PLN00412 330 -PEddCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR---EGNLIWPLLLdnVRPD--MRIAWEEPFGPVLPVIRIN 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953939 416 DGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDAN-LPFGGMKQSGTG 478
Cdd:PLN00412 404 SVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIG 467
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
12-497 |
2.38e-63 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 222.77 E-value: 2.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 12 VQQFLDRQhglWIEGRQAASDSEKRlNVYNPA-TGEVIASTADASVDDVDRAVMSGWRAFvaRSWAgRLPAE-RERILLR 89
Cdd:PRK11904 543 IAAFLEKQ---WQAGPIINGEGEAR-PVVSPAdRRRVVGEVAFADAEQVEQALAAARAAF--PAWS-RTPVEeRAAILER 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 90 FADLVEQHGEELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIAGKTLDLsiPLPQGARYQAwtRKEPVGVVAG 169
Cdd:PRK11904 616 AADLLEANRAELIALCVREAGKTLQDAIA-EVREAVDFCRYYAAQARRLFGAPEKL--PGPTGESNEL--RLHGRGVFVC 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 170 IVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFT 249
Cdd:PRK11904 691 ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFT 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 250 GSTATGKQIARA-AADTLTGVTL--ELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGF 326
Cdd:PRK11904 771 GSTETARIINRTlAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEML 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 327 EQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHnAELIAGNRGPDG--KGYYVSPTLVVNPDnhLRLTREEV 404
Cdd:PRK11904 851 KGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAGteNGHFVAPTAFEIDS--ISQLEREV 927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 405 FGPVVNLVR--VADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTlIDANL---PFGGMKQSGTG- 478
Cdd:PRK11904 928 FGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQ-IGAVVgvqPFGGQGLSGTGp 1006
|
490
....*....|....*....
gi 515953939 479 RDFGPDWLDGWCETKSVCV 497
Cdd:PRK11904 1007 KAGGPHYLLRFATEKTVTV 1025
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
29-478 |
3.11e-62 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 219.81 E-value: 3.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 29 AASDSEKRLNVYNPA-TGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETL 107
Cdd:COG4230 564 GEAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAF--PAWSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 108 EQGKSIN--ISrafEVGCTLNWMRYTAglttkiagktldlsiplpQGAR--YQAWTRKEPVGVVAGIVPWNFPLMIGMWK 183
Cdd:COG4230 642 EAGKTLPdaIA---EVREAVDFCRYYA------------------AQARrlFAAPTVLRGRGVFVCISPWNFPLAIFTGQ 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 184 VMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAA 263
Cdd:COG4230 701 VAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLA 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 264 DTLTG-VTL--ELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAAsSRIyieapLF------DTLVSGFEQAVKSLS 334
Cdd:COG4230 781 ARDGPiVPLiaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSA-LRV-----LCvqediaDRVLEMLKGAMAELR 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 335 VGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDG-KGYYVSPTLV-VNPDNHLrltREEVFGPVVNLV 412
Cdd:COG4230 855 VGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECaNGTFVAPTLIeIDSISDL---EREVFGPVLHVV 931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953939 413 RVAdGEEALQLA---NDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTlIDANL---PFGGMKQSGTG 478
Cdd:COG4230 932 RYK-ADELDKVIdaiNATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNI-IGAVVgvqPFGGEGLSGTG 1001
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
152-479 |
1.10e-61 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 207.85 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 152 GARyqAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFnVVTGsGA 231
Cdd:cd07134 91 GTK--SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-DA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 232 VCGAALTSHPrIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSR 311
Cdd:cd07134 167 EVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 312 IYIEAPLFDTLVSGFEQAV-KSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNrGPDGKGYYVSPTLV 390
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIeKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 391 VNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQN---ISKALAYTdrlQAGTVWVNsHTLI---D 464
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDkanVNKVLART---SSGGVVVN-DVVLhflN 400
|
330
....*....|....*
gi 515953939 465 ANLPFGGMKQSGTGR 479
Cdd:cd07134 401 PNLPFGGVNNSGIGS 415
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
39-478 |
3.45e-61 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 217.04 E-value: 3.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 39 VYNPA-TGEVIASTADASVDDVDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISR 117
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAF--PEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAI 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 118 AfEVGCTLNWMRYTAGlttkiagktldlsiplpQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIK 197
Cdd:PRK11905 649 A-EVREAVDFLRYYAA-----------------QARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAK 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 198 PSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLT-GVTL--ELG 274
Cdd:PRK11905 711 PAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETG 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 275 GKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIE---APLFDTLVSGfeqAVKSLSVGPgmsPEAF---INPL 348
Cdd:PRK11905 791 GQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQedvADRVLTMLKG---AMDELRIGD---PWRLstdVGPV 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 349 VSRAHCDKVQAFLDEAKAHNAELIAGNRGPD-GKGYYVSPTLV-VnpdNHLRLTREEVFGPVVNLVRV-ADGEEALQLA- 424
Cdd:PRK11905 865 IDAEAQANIEAHIEAMRAAGRLVHQLPLPAEtEKGTFVAPTLIeI---DSISDLEREVFGPVLHVVRFkADELDRVIDDi 941
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515953939 425 NDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTlIDANL---PFGGMKQSGTG 478
Cdd:PRK11905 942 NATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNI-IGAVVgvqPFGGEGLSGTG 997
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
45-477 |
1.38e-59 |
|
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: 204.74 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 45 GEVIASTADASVDDVDRAVMSGWRAfvARSWAgRLP-AERERILLRFADLVE-QHGEELAQLETLEQGKSI---NISRAF 119
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEA--RKEWA-RMPfEDRAAIFLKAADLLSgKYRYELNAATMLGQGKNVwqaEIDAAC 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 120 EVgctLNWMRYTAGLTTKIAGKTldlsiPLPQGAryQAWTRKE--PV-GVVAGIVPWNFPLMIGMWKVMPALAaGCSIVI 196
Cdd:cd07123 134 EL---IDFLRFNVKYAEELYAQQ-----PLSSPA--GVWNRLEyrPLeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLW 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 197 KPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTG------VT 270
Cdd:cd07123 203 KPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRyrtyprIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 271 LELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVS 350
Cdd:cd07123 283 GETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVID 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 351 RAHCDKVQAFLDEAKA-HNAELIAGNRGPDGKGYYVSPTLVVNPDNHLRLTREEVFGPVVNlVRV---ADGEEALQLAND 426
Cdd:cd07123 363 EKAFDRIKGYIDHAKSdPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLT-VYVypdSDFEETLELVDT 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953939 427 T-EYGLTASVWTQN---ISKAlayTDRLQ--AGTVWVN--SHTLIDANLPFGGMKQSGT 477
Cdd:cd07123 442 TsPYALTGAIFAQDrkaIREA---TDALRnaAGNFYINdkPTGAVVGQQPFGGARASGT 497
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
20-486 |
1.12e-58 |
|
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: 201.68 E-value: 1.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 20 HGLWIEGRQAASDSEKRlNVYNPATGEVIASTA-DASVDDVDRAVMSGWRAFVarSWAGRLPAERERILLRFADLVEQHG 98
Cdd:TIGR01238 37 QAAPIIGHSYKADGEAQ-PVTNPADRRDIVGQVfHANLAHVQAAIDSAQQAFP--TWNATPAKERAAKLDRLADLLELHM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 99 EELAQLETLEQGKSINISRAfEVGCTLNWMRYTAGLTTKIagktldlsipLPQGAryqawtrKEPVGVVAGIVPWNFPLM 178
Cdd:TIGR01238 114 PELMALCVREAGKTIHNAIA-EVREAVDFCRYYAKQVRDV----------LGEFS-------VESRGVFVCISPWNFPLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 179 IGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQI 258
Cdd:TIGR01238 176 IFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 259 ARAAA---DTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSV 335
Cdd:TIGR01238 256 NQTLAqreDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 336 GPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHN---AELIAGNRGPDGKGYYVSPTLV-VNPDNHLrltREEVFGPVVNL 411
Cdd:TIGR01238 336 GVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFeLDDIAEL---SEEVFGPVLHV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 412 VRVADGE--EALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTL--IDANLPFGGMKQSGTG-RDFGPDWL 486
Cdd:TIGR01238 413 VRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVgaVVGVQPFGGQGLSGTGpKAGGPHYL 492
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-499 |
5.19e-54 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 191.50 E-value: 5.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 24 IEGRQAASDSEKRLNVYNPATGEVIASTADASVDDVDRAVMSGWRAFVArsWAGRLPAERERILLRFADLVEQHGEELAQ 103
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL--WRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 104 LETLEQGKSI-----NISRAFEVgctlnwMRYTAGLTTkiagktLDLSIPLPQGAR-YQAWTRKEPVGVVAGIVPWNFPL 177
Cdd:PLN02419 196 NITTEQGKTLkdshgDIFRGLEV------VEHACGMAT------LQMGEYLPNVSNgVDTYSIREPLGVCAGICPFNFPA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 178 MIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGaALTSHPRIAKVSFTGSTATGKQ 257
Cdd:PLN02419 264 MIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 258 IARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYI--EAPLF-DTLVsgfeQAVKSLS 334
Cdd:PLN02419 343 IYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgDAKSWeDKLV----ERAKALK 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 335 VGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGY----YVSPTLV--VNPDnhLRLTREEVFGPV 408
Cdd:PLN02419 419 VTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILsgVTPD--MECYKEEIFGPV 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 409 VNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNshTLIDANLP---FGGMKQSGTG--RDFGP 483
Cdd:PLN02419 497 LVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN--VPIPVPLPffsFTGNKASFAGdlNFYGK 574
|
490
....*....|....*.
gi 515953939 484 DWLDGWCETKSVCVRY 499
Cdd:PLN02419 575 AGVDFFTQIKLVTQKQ 590
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
160-498 |
1.68e-51 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 182.15 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 160 RKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAgIPEGVFNVVTGsGAVCGAALTS 239
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 240 HPrIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLF 319
Cdd:PTZ00381 184 EP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 320 DTLVSGFEQAVKSLsVGPGMSPEAFINPLVSRAHCDKVQAFLdeaKAHNAELIAGNRGpDGKGYYVSPTLVVNPDNHLRL 399
Cdd:PTZ00381 263 DKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGGEV-DIENKYVAPTIIVNPDLDSPL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 400 TREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNS---HtLIDANLPFGGMKQSG 476
Cdd:PTZ00381 338 MQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvfH-LLNPNLPFGGVGNSG 416
|
330 340
....*....|....*....|..
gi 515953939 477 TGRDFGPDWLDGWCETKSVCVR 498
Cdd:PTZ00381 417 MGAYHGKYGFDTFSHPKPVLNK 438
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
28-478 |
6.12e-49 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 181.33 E-value: 6.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 28 QAASDSEKRlNVYNPA-TGEVIASTADASVDDVDRAVMSGWRAfvARSWAGRLPAERERILLRFADLVEQHGEELAQLET 106
Cdd:PRK11809 653 DPVAAGEMS-PVINPAdPRDIVGYVREATPAEVEQALESAVNA--APIWFATPPAERAAILERAADLMEAQMQTLMGLLV 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 107 LEQGKSINISRAfEVGCTLNWMRYTAGlttkiagktldlsiplpQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMP 186
Cdd:PRK11809 730 REAGKTFSNAIA-EVREAVDFLRYYAG-----------------QVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAA 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 187 ALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTL 266
Cdd:PRK11809 792 ALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 267 ------TGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGpgmS 340
Cdd:PRK11809 872 dpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMG---N 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 341 PEAF---INPLV---SRAHCDK-VQAFldEAKAHNAELIA-GNRGPDGKGYYVSPTLvVNPDNHLRLTReEVFGPVVNLV 412
Cdd:PRK11809 949 PDRLstdIGPVIdaeAKANIERhIQAM--RAKGRPVFQAArENSEDWQSGTFVPPTL-IELDSFDELKR-EVFGPVLHVV 1024
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515953939 413 RVA--DGEEALQLANDTEYGLTASVWTQnISKALAY-TDRLQAGTVWVNSHtLIDANL---PFGGMKQSGTG 478
Cdd:PRK11809 1025 RYNrnQLDELIEQINASGYGLTLGVHTR-IDETIAQvTGSAHVGNLYVNRN-MVGAVVgvqPFGGEGLSGTG 1094
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
157-479 |
2.36e-46 |
|
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: 167.30 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 157 AWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAgIPEGVFNVVTGSGAVCGAA 236
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 237 LtsHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDAD-------PAWvieglmtGSFLNQGQVCAAS 309
Cdd:cd07136 173 L--DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANlklaakrIVW-------GKFLNAGQTCVAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 310 SRIYIEAPLFDTLVSGFEQAVKSLsvgpgMSPEAFINP----LVSRAHCDKVQAFLDEAKAhnaeLIAGNRGPDGKgyYV 385
Cdd:cd07136 244 DYVLVHESVKEKFIKELKEEIKKF-----YGEDPLESPdygrIINEKHFDRLAGLLDNGKI----VFGGNTDRETL--YI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 386 SPTLVVNPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVN---SHtL 462
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtiMH-L 391
|
330
....*....|....*..
gi 515953939 463 IDANLPFGGMKQSGTGR 479
Cdd:cd07136 392 ANPYLPFGGVGNSGMGS 408
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
162-495 |
8.39e-46 |
|
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: 165.66 E-value: 8.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 162 EPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVfNVVTGSGAVcGAALTSHp 241
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI-KVIEGGVPE-TTALLEQ- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 242 RIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSF-LNQGQVCAASSRIYIEAPLFD 320
Cdd:cd07137 177 KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 321 TLVSGFEQAVKSLsVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRgpDGKGYYVSPTLVVNPDNHLRLT 400
Cdd:cd07137 257 TLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGER--DEKNLYIEPTILLDPPLDSSIM 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 401 REEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNS---HTLIDAnLPFGGMKQSGT 477
Cdd:cd07137 334 TEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDtvvQYAIDT-LPFGGVGESGF 412
|
330
....*....|....*...
gi 515953939 478 GRDFGPDWLDGWCETKSV 495
Cdd:cd07137 413 GAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
157-498 |
3.49e-44 |
|
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: 161.24 E-value: 3.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 157 AWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELaseagIPEGV----FNVVTGsGAV 232
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLdkecYPVVLG-GVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 233 CGAALTSHpRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRI 312
Cdd:cd07132 168 ETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 313 YIEAPLFDTLVSGFEQAVKSL-SVGPGMSPEafINPLVSRAHCDKVQAFLDEAKahnaeLIAGNRGpDGKGYYVSPTLVV 391
Cdd:cd07132 247 LCTPEVQEKFVEALKKTLKEFyGEDPKESPD--YGRIINDRHFQRLKKLLSGGK-----VAIGGQT-DEKERYIAPTVLT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 392 NPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQN---ISKALAYTdrlQAGTVWVN---SHTLIDa 465
Cdd:cd07132 319 DVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNkkvINKILSNT---SSGGVCVNdtiMHYTLD- 394
|
330 340 350
....*....|....*....|....*....|...
gi 515953939 466 NLPFGGMKQSGTGRDFGPDWLDGWCETKSVCVR 498
Cdd:cd07132 395 SLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
41-484 |
1.65e-43 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 160.77 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 41 NPATGEVIASTADASVDDVDRAVMSGWRAfvARSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKsINISRAFE 120
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEA--AKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGK-ILAEGIGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 121 VGCTLNWMRYTAGLTTKIAGKTldlsIP--LPQGARYQAWTrkePVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP 198
Cdd:PLN02315 117 VQEIIDMCDFAVGLSRQLNGSI----IPseRPNHMMMEVWN---PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 199 SETTPLTLLR----VAELASEAGIPEGVFNVVTGsGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTGVTLELG 274
Cdd:PLN02315 190 APTTPLITIAmtklVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 275 GKNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHC 354
Cdd:PLN02315 269 GNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 355 DKVQAFLDEAKAHNAELIAGNRGPDGKGYYVSPTLV-VNPDnhLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTA 433
Cdd:PLN02315 349 KNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVeISPD--ADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSS 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953939 434 SVWTQNISKALAytdrlqagtvWVNSH----TLIDANLP---------FGGMKQSGTGRDFGPD 484
Cdd:PLN02315 427 SIFTRNPETIFK----------WIGPLgsdcGIVNVNIPtngaeiggaFGGEKATGGGREAGSD 480
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-437 |
8.26e-37 |
|
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: 141.14 E-value: 8.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 59 VDRAVMSGWRAFvaRSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGksINISRAF-EVGCTLNWMRYTAGLTtk 137
Cdd:cd07129 1 VDAAAAAAAAAF--ESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgELGRTTGQLRLFADLV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 138 IAGKTLDLSI--PLPQGA--------RYQAwtrkePVGVVAGIVPWNFPLMIGmwkVM-----PALAAGCSIVIKPSETT 202
Cdd:cd07129 75 REGSWLDARIdpADPDRQplprpdlrRMLV-----PLGPVAVFGASNFPLAFS---VAggdtaSALAAGCPVVVKAHPAH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 203 PLTLLRVAELASEA----GIPEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQIARAAADTLTG--VTLELGGK 276
Cdd:cd07129 147 PGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPipFYAELGSV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 277 NPAIVLKDA---DPAWVIEGLmTGSF-LNQGQVCAASSRIY-IEAPLFDTLVSGFEQAVKSLSVGPgMspeafINPLVSR 351
Cdd:cd07129 227 NPVFILPGAlaeRGEAIAQGF-VGSLtLGAGQFCTNPGLVLvPAGPAGDAFIAALAEALAAAPAQT-M-----LTPGIAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 352 AHCDKVQAFLDeakAHNAELIAGNrGPDGKGYYVSPTLVVNPDNHLRLT---REEVFGPVVNLVRVADGEEALQLANDTE 428
Cdd:cd07129 300 AYRQGVEALAA---APGVRVLAGG-AAAEGGNQAAPTLFKVDAAAFLADpalQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
....*....
gi 515953939 429 YGLTASVWT 437
Cdd:cd07129 376 GQLTATIHG 384
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
61-472 |
7.74e-36 |
|
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: 138.52 E-value: 7.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 61 RAVMSGWRAFVARSWAGRLpaererilLRFADLVEQHGEELAQLETLEQGKSINIsrAFEVGCTLNWMRYTA--GLTTKI 138
Cdd:cd07084 9 DISTKAARRLALPKRADFL--------ARIIQRLAAKSYDIAAGAVLVTGKGWMF--AENICGDQVQLRARAfvIYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 139 AGKTLDlsiPLPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGI 218
Cdd:cd07084 79 PHEPGN---HLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 219 -PEGVFNVVTGSGAVcGAALTSHPRIAKVSFTGSTATGKQIARAAADtlTGVTLELGGKNPAIVLKDADP-AWVIEGLMT 296
Cdd:cd07084 156 lPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQAvDYVAWQCVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 297 GSFLNQGQVCAASSRIYIEA-----PLFDTLVSGFEQ-AVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFldEAKAHNAE 370
Cdd:cd07084 233 DMTACSGQKCTAQSMLFVPEnwsktPLVEKLKALLARrKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLF--SGKELKNH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 371 LIAGNRGPDgkgyyVSPTLVVNPDNHLRLTR---EEVFGPVVNLVRVADGEEALQLA-NDTEYG-LTASVWTQNIskalA 445
Cdd:cd07084 311 SIPSIYGAC-----VASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLALVLElLERMHGsLTAAIYSNDP----I 381
|
410 420
....*....|....*....|....*..
gi 515953939 446 YTDRLqAGTVWVNSHTLIDANLPFGGM 472
Cdd:cd07084 382 FLQEL-IGNLWVAGRTYAILRGRTGVA 407
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
162-498 |
1.93e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 126.70 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 162 EPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVvtgSGAVCGAALTSHP 241
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVV---EGAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 242 RIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVLKDADPAWVIEGLMTGSF-LNQGQVCAASSRIYIEAPLFD 320
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 321 TLVSGFEQAVKSLsVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRgpDGKGYYVSPTLVVNPDNHLRLT 400
Cdd:PLN02174 268 KVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEK--DRENLKIAPTILLDVPLDSLIM 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 401 REEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTLIDA--NLPFGGMKQSGTG 478
Cdd:PLN02174 345 SEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGVGESGMG 424
|
330 340
....*....|....*....|
gi 515953939 479 RDFGPDWLDGWCETKSVCVR 498
Cdd:PLN02174 425 AYHGKFSFDAFSHKKAVLYR 444
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
162-498 |
1.28e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 121.37 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 162 EPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTllrVAELAseAGIPE----GVFNVVTGsGAVCGAAL 237
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPAT---SAFLA--ANIPKyldsKAVKVIEG-GPAVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 238 TSHpRIAKVSFTGSTATGKQIARAAADTLTGVTLELGGKNPAIVlKDADPAW----VIEGLMTGSFLN-QGQVCAASSRI 312
Cdd:PLN02203 181 LQH-KWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV-DSLSSSRdtkvAVNRIVGGKWGScAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 313 YIEAPLFDTLVSGFEQAVKSLSVGPGMSPEaFINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRgpDGKGYYVSPTLVVN 392
Cdd:PLN02203 259 LVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIVHGGSI--DEKKLFIEPTILLN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 393 PDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQNISKALAYTDRLQAGTVWVNSHTL---IDAnLPF 469
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIqyaCDS-LPF 414
|
330 340
....*....|....*....|....*....
gi 515953939 470 GGMKQSGTGRDFGPDWLDGWCETKSVCVR 498
Cdd:PLN02203 415 GGVGESGFGRYHGKYSFDTFSHEKAVLRR 443
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
21-437 |
3.91e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 120.19 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGRQAASdsekrlNVYNPATGEVIASTADASVD---DVDRAVMSGWRAFVARSWAgrlpaERERILLRFADLVEQH 97
Cdd:PRK11903 11 GRWQAGSGAGT------PLFDPVTGEELVRVSATGLDlaaAFAFAREQGGAALRALTYA-----QRAALLAAIVKVLQAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 98 GEELAQLETLEQGKSINISrAFEVGCTLNWMRYTAGLttkiaGKTLDLSIPLPQGARYQawTRKEPV-----------GV 166
Cdd:PRK11903 80 RDAYYDIATANSGTTRNDS-AVDIDGGIFTLGYYAKL-----GAALGDARLLRDGEAVQ--LGKDPAfqgqhvlvptrGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 167 VAGIVPWNFPLMiGMW-KVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGI-PEGVFNVVTGSGAVCGAALTSHPria 244
Cdd:PRK11903 152 ALFINAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFD--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 245 KVSFTGSTATGKQIARAAADTLTGVTL--ELGGKNPAIVLKDADP------AWVIEGL--MTgsfLNQGQVCAASSRIYI 314
Cdd:PRK11903 228 VVSFTGSAETAAVLRSHPAVVQRSVRVnvEADSLNSALLGPDAAPgseafdLFVKEVVreMT---VKSGQKCTAIRRIFV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 315 EAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAHnAELIAGNRG------PDGKGYYVSPT 388
Cdd:PRK11903 305 PEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGfalvdaDPAVAACVGPT 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 515953939 389 LVV--NPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWT 437
Cdd:PRK11903 384 LLGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
21-439 |
4.57e-26 |
|
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: 111.21 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 21 GLWIEGRQAASdsekrlNVYNPATGEVIASTADASVDdVDRAVmsgwrAFvARSWAGRLP-----AERERILLRFADLVE 95
Cdd:cd07128 7 GQWHAGTGDGR------TLHDAVTGEVVARVSSEGLD-FAAAV-----AY-AREKGGPALraltfHERAAMLKALAKYLM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 96 QHGEELAQLetleqgksinisrAFEVGCTL--NWMRYTAGLTTKIA----GKTL---------DLSIPLPQGARYQA--- 157
Cdd:cd07128 74 ERKEDLYAL-------------SAATGATRrdSWIDIDGGIGTLFAyaslGRRElpnahflveGDVEPLSKDGTFVGqhi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 158 WTRKEpvGVVAGIVPWNFPLMiGMW-KVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGI-PEGVFNVVTGSGAVCGA 235
Cdd:cd07128 141 LTPRR--GVAVHINAFNFPVW-GMLeKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 236 ALTSHPriaKVSFTGSTATGKQIARAAADTLTGV--TLELGGKNPAIVLKDADP-----AWVIEGL---MTGsflNQGQV 305
Cdd:cd07128 218 HLGEQD---VVAFTGSAATAAKLRAHPNIVARSIrfNAEADSLNAAILGPDATPgtpefDLFVKEVareMTV---KAGQK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 306 CAASSRIYIEAPLFDTLVSGFEQAVKSLSVGPGMSPEAFINPLVSRAHCDKVQAFLDEAKAhNAELIAGNR-------GP 378
Cdd:cd07128 292 CTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLA-EAEVVFGGPdrfevvgAD 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953939 379 DGKGYYVSPTLVV--NPDNHLRLTREEVFGPVVNLVRVADGEEALQLANDTEYGLTASVWTQN 439
Cdd:cd07128 371 AEKGAFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
162-459 |
9.56e-13 |
|
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: 69.83 E-value: 9.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 162 EPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAEL----ASEAGIPEGVFNVVTGSGAVCGAAL 237
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 238 TSHPRIAKVSFTGSTAtgkqIARAAADTLT---GVtlelG-GKNPAIVLKDADpawvIEG-----LMTGSFLNqGQVCAA 308
Cdd:cd07122 174 MKHPDVDLILATGGPG----MVKAAYSSGKpaiGV----GpGNVPAYIDETAD----IKRavkdiILSKTFDN-GTICAS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 309 SSRIYIEAPLFDTLVSGFEQAvkslsvgpG---MSPEAFinplvsrahcDKVQAFL-DEAKAHN-------AELIAGNRG 377
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRR--------GayfLNEEEK----------EKLEKALfDDGGTLNpdivgksAQKIAELAG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 378 ---PDGKGYYVSPTLVVNPDNhlRLTREEVFgPVVNLVRVADGEEALQLAND-TEY---GLTASVWTQNISKALAYTDRL 450
Cdd:cd07122 303 ievPEDTKVLVAEETGVGPEE--PLSREKLS-PVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDEEVIEEFALRM 379
|
....*....
gi 515953939 451 QAGTVWVNS 459
Cdd:cd07122 380 PVSRILVNT 388
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
61-437 |
1.68e-10 |
|
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: 63.27 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 61 RAVMSGWRAFVARSWAGrLPAErerILLRFADLVEqhgeELAQLETLEQGKSINIsrAFEVG------CTLNWMRYTAGL 134
Cdd:cd07127 94 RAAMPGWRDAGARARAG-VCLE---ILQRLNARSF----EMAHAVMHTTGQAFMM--AFQAGgphaqdRGLEAVAYAWRE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 135 TTKIAGKTLDLSiplPQGaryqawtRKEPVGVVA--GIVPWNFPLMIG-----MWKVMPA----LAAGCSIVIKPSETTP 203
Cdd:cd07127 164 MSRIPPTAEWEK---PQG-------KHDPLAMEKtfTVVPRGVALVIGcstfpTWNGYPGlfasLATGNPVIVKPHPAAI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 204 LTL---LRVA-ELASEAGI-PEGVFNVVTGSGAVCGAALTSHPRIAKVSFTGSTATG---KQIARAAAdtltgVTLELGG 275
Cdd:cd07127 234 LPLaitVQVArEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGdwlEANARQAQ-----VYTEKAG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 276 KNPAIVLKDADPAWVIEGLMTGSFLNQGQVCAASSRIYI---------EAPLFDTLVSGFEQAVKSLSVGPGMSPEafin 346
Cdd:cd07127 309 VNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAADLAAAIDGLLADPARAAA---- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 347 pLVSRAHCDKVQAFLDEAKAHNAELIAGNR--GPDGKGYYVSPTLVVNPD-NHLRLTREEVFGPVVNLVRVADGEEALQL 423
Cdd:cd07127 385 -LLGAIQSPDTLARIAEARQLGEVLLASEAvaHPEFPDARVRTPLLLKLDaSDEAAYAEERFGPIAFVVATDSTDHSIEL 463
|
410
....*....|....*..
gi 515953939 424 ANDT--EYG-LTASVWT 437
Cdd:cd07127 464 ARESvrEHGaMTVGVYS 480
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
163-483 |
3.57e-10 |
|
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: 62.13 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 163 PVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPSETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAALT-SHP 241
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 242 RIakVSFTGSTATGKQIARaaadtltgvtlELGGKnpaIVLKDADPAWVIEGLMTGSF------LNQ------GQVCAAS 309
Cdd:cd07126 222 RM--TLFTGSSKVAERLAL-----------ELHGK---VKLEDAGFDWKILGPDVSDVdyvawqCDQdayacsGQKCSAQ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 310 SRIY-----IEAPLFDTLVSGFEQ-AVKSLSVGPGMSpeafINPLVSRAHCDKVQAFLDEAKAHNAELIAGNRGPDGKGY 383
Cdd:cd07126 286 SILFahenwVQAGILDKLKALAEQrKLEDLTIGPVLT----WTTERILDHVDKLLAIPGAKVLFGGKPLTNHSIPSIYGA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 384 YvSPTLVVNP------DNHLRLTREEVFGPVVNLVRVADGEEALQLA--NDTEYGLTASVwtqnISKALAYTDRLQAGTv 455
Cdd:cd07126 362 Y-EPTAVFVPleeiaiEENFELVTTEVFGPFQVVTEYKDEQLPLVLEalERMHAHLTAAV----VSNDIRFLQEVLANT- 435
|
330 340 350
....*....|....*....|....*....|..
gi 515953939 456 wVNSHTlidanlpFGGMKQSGTGRD----FGP 483
Cdd:cd07126 436 -VNGTT-------YAGIRARTTGAPqnhwFGP 459
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
73-327 |
2.57e-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: 56.08 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 73 RSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSINISRA---FEVGCT---LNWMRYTAGLTTKIAGKTLDLS 146
Cdd:cd07077 8 RTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIAnwiAMMGCSeskLYKNIDTERGITASVGHIQDVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 147 IPlpqgARYQAWTRKEPVGVVAGIVPWNFPLMiGMWKVMPALAAGCSIVIKPSETTP-----LTLLRVAELAseAGIPEG 221
Cdd:cd07077 88 LP----DNGETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPftnraLALLFQAADA--AHGPKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 222 VFNVVTGSGAVCGAALTSHPRIAKVSFTGstatGKQIARAAADTLTGV-TLELGGKNPAIVLKDADPAWVIEGLMTGSFL 300
Cdd:cd07077 161 LVLYVPHPSDELAEELLSHPKIDLIVATG----GRDAVDAAVKHSPHIpVIGFGAGNSPVVVDETADEERASGSVHDSKF 236
|
250 260
....*....|....*....|....*..
gi 515953939 301 NQGQVCAASSRIYIEAPLFDTLVSGFE 327
Cdd:cd07077 237 FDQNACASEQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
73-327 |
4.09e-07 |
|
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: 52.27 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 73 RSWAGRLPAERERILLRFADLVEQHGEELAQLETLEQGKSIN----ISRAFEVGCTLNwmRYTAGLTTKIagktldlsip 148
Cdd:cd07081 13 QGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVedkvIKNHFAAEYIYN--VYKDEKTCGV---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 149 LPQGARYQAWTRKEPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKP----SETTPLTLLRVAELASEAGIPEGVFN 224
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 225 VVTGSGAVCGAALTSHPRIAKVSFTGSTATGKQiARAAADTLTGVTlelGGKNPAIVLKDADPAWVIEGLMTGSFLNQGQ 304
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKA-AYSSGKPAIGVG---AGNTPVVIDETADIKRAVQSIVKSKTFDNGV 236
|
250 260
....*....|....*....|...
gi 515953939 305 VCAASSRIYIEAPLFDTLVSGFE 327
Cdd:cd07081 237 ICASEQSVIVVDSVYDEVMRLFE 259
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
162-459 |
8.30e-07 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 51.72 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 162 EPVGVVAGIVPWNFPLMIGMWKVMPALAAGCSIVIKPS----ETTPLTLLRVAELASEAGIPEGVFNVVTGSGAVCGAAL 237
Cdd:PRK13805 107 EPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHpraqKSSIAAAKIVLDAAVAAGAPKDIIQWIEEPSVELTNAL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 238 TSHPRIAKVSFTGstatGKQIARAAADTLT---GVtlelG-GKNPAIVLKDADpawvIEG-----LMTGSFLNqGQVCAA 308
Cdd:PRK13805 187 MNHPGIALILATG----GPGMVKAAYSSGKpalGV----GaGNVPAYIDKTAD----IKRavndiLLSKTFDN-GMICAS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 309 SSRIYIEAPLFDTLVSGFEqavkslsvgpgmSPEAFInplVSRAHCDKVQAF-LDEAKAH-NAELI----------AGNR 376
Cdd:PRK13805 254 EQAVIVDDEIYDEVKEEFA------------SHGAYF---LNKKELKKLEKFiFGKENGAlNADIVgqsaykiaemAGFK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953939 377 GPDGKGYYVSPTLVVNPDNhlRLTREEVFgPVVNLVRVADGEEALQLAND-TEY---GLTASVWTQNISKALAYTDRLQA 452
Cdd:PRK13805 319 VPEDTKILIAEVKGVGESE--PLSHEKLS-PVLAMYKAKDFEDAVEKAEKlVEFgglGHTAVIYTNDDELIKEFGLRMKA 395
|
....*..
gi 515953939 453 GTVWVNS 459
Cdd:PRK13805 396 CRILVNT 402
|
|
| |
