|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-494 |
0e+00 |
|
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: 645.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 59 YRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDFHGVRIDRGQPGRTP- 137
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREGSWLDARIDPADPDRQPl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 138 PRPDLRQWRIGLGPVAVFGASNFPLAFSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAAADSGMPDGVFNMV 217
Cdd:cd07129 95 PRPDLRRMLVPLGPVAVFGASNFPLAFSVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 218 YGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVFAEMSSINPLVVLPEALRRRGRQVAEELAASVTLG 295
Cdd:cd07129 175 QGGGreVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIPFYAELGSVNPVFILPGALAERGEAIAQGFVGSLTLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 296 CGQFCTKPGLVLGLRSPGFDAFVAALGEALAARPAQSMLNAGTLRSYVEGLQRLERHPGIRRLAGAPQEGRQAH--PQLF 373
Cdd:cd07129 255 AGQFCTNPGLVLVPAGPAGDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEALAAAPGVRVLAGGAAAEGGNQaaPTLF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 374 KADVgLLLEGDELLQEEVFGPATVVVEAADEEQLARALDNLHGQLSATLIGEADDLAAFAGLVPLLERKAGRLLFNGYPT 453
Cdd:cd07129 335 KVDA-AAFLADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDDLALARELLPVLERKAGRLLFNGWPT 413
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15596450 454 GVEVCDAMVHGGPYPATSDARGTSVGTLAIERFLRPLCYQD 494
Cdd:cd07129 414 GVEVCPAMVHGGPYPATTDPRFTSVGTAAIERFLRPVCYQN 454
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
57-493 |
1.96e-62 |
|
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: 210.94 E-value: 1.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 57 PHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAaRIEGERTRTANQLRLFAEVLRRGDFHGVRIDRGQPGrt 136
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGW-MFAENICGDQVQLRARAFVIYSYRIPHEPGNHLGQG-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 137 pPRPDLRQWRIGLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAAAdsgMPDGVFNM 216
Cdd:cd07084 90 -LKQQSHGYRWPYGPVLVIGAFNFPL--WIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LPPEDVTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 217 VYGSG-VGEALVRHPAIRAVGFTGSLKGGRALcdlaAARPQPIPVFAEMSSINPLVVLPEAlrRRGRQVAEELAASVTLG 295
Cdd:cd07084 164 INGDGkTMQALLLHPNPKMVLFTGSSRVAEKL----ALDAKQARIYLELAGFNWKVLGPDA--QAVDYVAWQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 296 CGQFCTKPGLVLGLRSPGFDAFVAALGEALAAR-PAQSMLNAGTLRSYVEGLQRLERHPGIRRLAGAPQEGRQAHPQLFK 374
Cdd:cd07084 238 SGQKCTAQSMLFVPENWSKTPLVEKLKALLARRkLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIYG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 375 ADVG--------LLLEGDELLQEEVFGPATVVVEAAD--EEQLARALDNLHGQLSATLIgeADDLAAFAGLVPLLERkAG 444
Cdd:cd07084 318 ACVAsalfvpidEILKTYELVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIY--SNDPIFLQELIGNLWV-AG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15596450 445 RLLFNGY-PTGVEVcdAMVHGGPYPAtsDARGTSVGTL-AIERFLRPLCYQ 493
Cdd:cd07084 395 RTYAILRgRTGVAP--NQNHGGGPAA--DPRGAGIGGPeAIKLVWRCHAEQ 441
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
52-489 |
5.02e-44 |
|
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: 161.22 E-value: 5.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 52 AERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIdrg 131
Cdd:cd07078 7 ARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARR--LHGEVI--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 132 qpgrTPPRPDLRQW--RIGLGPVAVFGASNFPLAFstAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGM 209
Cdd:cd07078 82 ----PSPDPGELAIvrREPLGVVGAITPWNFPLLL--AAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA----GL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 210 PDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEA-LrrrgRQVAE 286
Cdd:cd07078 152 PPGVLNVVTGDGdeVGAALASHPRVDKISFTGSTAVGKAI--MRAAAENLKRVTLELGGKSPLIVFDDAdL----DAAVK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 287 ELAASVTLGCGQFCTKPGLVLGLRSPgFDAFVAALGEALAARPAQSMLNAGTL---------RSYVEGLQRLERHPGIRR 357
Cdd:cd07078 226 GAVFGAFGNAGQVCTAASRLLVHESI-YDEFVERLVERVKALKVGNPLDPDTDmgplisaaqLDRVLAYIEDAKAEGAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 358 LAGAPQEGRQAH----PQLFkADVgllLEGDELLQEEVFGPATVVVEAADEEQLARALDNLHGQLSATLIGEadDLAAFA 433
Cdd:cd07078 305 LCGGKRLEGGKGyfvpPTVL-TDV---DPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTR--DLERAL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596450 434 GLVPLLErkAGRLLFNGYPTGVEvcDAMVHGGPYPATSDARGtsvGTLAIERFLRP 489
Cdd:cd07078 379 RVAERLE--AGTVWINDYSVGAE--PSAPFGGVKQSGIGREG---GPYGLEEYTEP 427
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-465 |
2.61e-41 |
|
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: 154.90 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 1 MPSILGHNYVGGA-RSAAGNLTLRSLDADSGEALPYaFVQATEAEVDAAARAAERAYPHYRQLSATRRAGFLEAIASRLD 79
Cdd:COG1012 1 MTTPEYPLFIGGEwVAAASGETFDVINPATGEVLAR-VPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 80 ALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIDRGQPGRtpprpDLRQWRIGLGPVAVFGASN 159
Cdd:COG1012 80 ERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARR--LYGETIPSDAPGT-----RAYVRREPLGVVGAITPWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 160 FPLAfsTAGGDSAAALAAGCPVVVKAHgghmATAECVADAILQAAADSGMPDGVFNMVYGSG--VGEALVRHPAIRAVGF 237
Cdd:COG1012 153 FPLA--LAAWKLAPALAAGNTVVLKPA----EQTPLSALLLAELLEEAGLPAGVLNVVTGDGseVGAALVAHPDVDKISF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 238 TGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEA-LrrrgRQVAEELAASVTLGCGQFCTKPGLVLGLRSPgFDA 316
Cdd:COG1012 227 TGSTAVGRRI--AAAAAENLKRVTLELGGKNPAIVLDDAdL----DAAVEAAVRGAFGNAGQRCTAASRLLVHESI-YDE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 317 FVAALGEALAARPAQSMLNAGTL---------RSYVEGLQRLERHPGIRRLAG----APQEGRQAHPQLFkADVgllLEG 383
Cdd:COG1012 300 FVERLVAAAKALKVGDPLDPGTDmgpliseaqLERVLAYIEDAVAEGAELLTGgrrpDGEGGYFVEPTVL-ADV---TPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 384 DELLQEEVFGPATVVVEAADEEQ-LARALDNLHGqLSATL----IGEADDLAAfaglvpllERKAGRLLFNGYPTGVEvc 458
Cdd:COG1012 376 MRIAREEIFGPVLSVIPFDDEEEaIALANDTEYG-LAASVftrdLARARRVAR--------RLEAGMVWINDGTTGAV-- 444
|
....*..
gi 15596450 459 DAMVHGG 465
Cdd:COG1012 445 PQAPFGG 451
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
59-489 |
9.52e-40 |
|
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: 147.76 E-value: 9.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 59 YRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIDRGQPGRtpp 138
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADK--LGGPELPSPDPGG--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 139 rpDLRQWRIGLGPVAVFGASNFPLAFstAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFNMVY 218
Cdd:cd06534 85 --EAYVRREPLGVVGVITPWNFPLLL--AAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA----GLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 219 GSG--VGEALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEALRRRgrqVAEELAASVTLGC 296
Cdd:cd06534 157 GGGdeVGAALLSHPRVDKISFTGSTAVGKAI--MKAAAENLKPVTLELGGKSPVIVDEDADLDA---AVEGAVFGAFFNA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 297 GQFCTKPGLVLGLRSPgFDAFVAALgealaarpaqsmlnaGTLRSYVEGLQRLERHpgirrlagapqEgrqahpqlfkad 376
Cdd:cd06534 232 GQICTAASRLLVHESI-YDEFVEKL---------------VTVLVDVDPDMPIAQE-----------E------------ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 377 vglllegdellqeeVFGPATVVVEAADEEQLARALDNLHGQLSATL----IGEADDLAAfaglvpllERKAGRLLFNGYP 452
Cdd:cd06534 273 --------------IFGPVLPVIRFKDEEEAIALANDTEYGLTAGVftrdLNRALRVAE--------RLRAGTVYINDSS 330
|
410 420 430
....*....|....*....|....*....|....*..
gi 15596450 453 TGVEvcDAMVHGGPYPAtsdARGTSVGTLAIERFLRP 489
Cdd:cd06534 331 IGVG--PEAPFGGVKNS---GIGREGGPYGLEEYTRT 362
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
51-327 |
1.11e-34 |
|
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: 135.74 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 51 AAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDFHGVRIDR 130
Cdd:pfam00171 37 AARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 131 GQPGRTPPRPdlrqwrigLGPVAVFGASNFPLAfsTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMP 210
Cdd:pfam00171 117 GRLAYTRREP--------LGVVGAITPWNFPLL--LPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEA----GLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 211 DGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARpqPIPVFAEMSSINPLVVLPEALRRRgrqVAEEL 288
Cdd:pfam00171 183 AGVLNVVTGSGaeVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN--LKRVTLELGGKNPLIVLEDADLDA---AVEAA 257
|
250 260 270
....*....|....*....|....*....|....*....
gi 15596450 289 AASVTLGCGQFCTKPGLVLGLRSPgFDAFVAALGEALAA 327
Cdd:pfam00171 258 VFGAFGNAGQVCTATSRLLVHESI-YDEFVEKLVEAAKK 295
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
56-420 |
2.86e-32 |
|
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: 129.29 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRE--TALPAARieGERTRTANQLRLFA-EVLRrgdFHGVRIDRGQ 132
Cdd:cd07097 50 FPAWRRTSPEARADILDKAGDELEARKEELARLLTREegKTLPEAR--GEVTRAGQIFRYYAgEALR---LSGETLPSTR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 133 PG------RTPprpdlrqwrigLGPVAVFGASNFPLAfsTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaad 206
Cdd:cd07097 125 PGvevettREP-----------LGVVGLITPWNFPIA--IPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEA--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 207 sGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARpqPIPVFAEMSSINPLVVLPEA-LRRrgrq 283
Cdd:cd07097 189 -GLPAGVFNLVMGSGseVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR--GARVQLEMGGKNPLVVLDDAdLDL---- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 284 vAEELAA-SVTLGCGQFCTKPGLVLgLRSPGFDAFVAALGEALAARPAQSMLNAGT-------------LRSYVEglqrL 349
Cdd:cd07097 262 -AVECAVqGAFFSTGQRCTASSRLI-VTEGIHDRFVEALVERTKALKVGDALDEGVdigpvvserqlekDLRYIE----I 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596450 350 ERHPGIRRLAGA-----PQEGRQAHPQLFkADVgllLEGDELLQEEVFGPATVVVEAAD-EEQLARALDNLHGqLSA 420
Cdd:cd07097 336 ARSEGAKLVYGGerlkrPDEGYYLAPALF-AGV---TNDMRIAREEIFGPVAAVIRVRDyDEALAIANDTEFG-LSA 407
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
34-423 |
1.16e-27 |
|
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: 115.50 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 34 PYAFVQ-ATEAEVDAAARAAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLR 112
Cdd:cd07150 11 VYARVAvGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 113 LFAEVLRRgdFHGVRIDRGQPGR---TPPRPdlrqwrigLGPVAVFGASNFPLAFSTAggDSAAALAAGCPVVVKAHGGH 189
Cdd:cd07150 91 AAAGECRR--VRGETLPSDSPGTvsmSVRRP--------LGVVAGITPFNYPLILATK--KVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 190 MATAECVADAILQAaadsGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVfaEMSSI 267
Cdd:cd07150 159 PVIGLKIAEIMEEA----GLPKGVFNVVTGGGaeVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITL--ELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 268 NPLVVLPEALRRRGRQVAeelAASVTLGCGQFCTKPGLVLgLRSPGFDAFVAalgeALAARPAQsmLNAGTLR--SYVEG 345
Cdd:cd07150 233 NPLIVLADADLDYAVRAA---AFGAFMHQGQICMSASRII-VEEPVYDEFVK----KFVARASK--LKVGDPRdpDTVIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 346 -------LQRLERH------PGIRRLAGAPQEGRQAHPQLFkADVgllLEGDELLQEEVFGPATVVVEAAD-EEQLARAL 411
Cdd:cd07150 303 plisprqVERIKRQvedavaKGAKLLTGGKYDGNFYQPTVL-TDV---TPDMRIFREETFGPVTSVIPAKDaEEALELAN 378
|
410
....*....|..
gi 15596450 412 DNLHGqLSATLI 423
Cdd:cd07150 379 DTEYG-LSAAIL 389
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
8-276 |
1.46e-25 |
|
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: 109.74 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 8 NYVGGA-RSAAGNLTLRSLDADSGEALPYAFVQATEAEVDAAARAAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFV 86
Cdd:cd07131 1 NYIGGEwVDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 87 ALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIDRGQPGRtpprpDLRQWRIGLGPVAVFGASNFPLAFst 166
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRR--LFGETVPSELPNK-----DAMTRRQPIGVVALITPWNFPVAI-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 167 AGGDSAAALAAGCPVVVKAhgghMATAECVADAILQAAADSGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGG 244
Cdd:cd07131 152 PSWKIFPALVCGNTVVFKP----AEDTPACALKLVELFAEAGLPPGVVNVVHGRGeeVGEALVEHPDVDVVSFTGSTEVG 227
|
250 260 270
....*....|....*....|....*....|..
gi 15596450 245 RALCDLAAARPQpiPVFAEMSSINPLVVLPEA 276
Cdd:cd07131 228 ERIGETCARPNK--RVALEMGGKNPIIVMDDA 257
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
57-327 |
1.24e-24 |
|
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: 106.58 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 57 PHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIDRGQPGRT 136
Cdd:cd07088 49 KAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARR--IEGEIIPSDRPNEN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 137 pprpdLRQWRIGLGPVAVFGASNFPLAfsTAGGDSAAALAAGCPVVVKAHGGHMATAEcvadAILQAAADSGMPDGVFNM 216
Cdd:cd07088 127 -----IFIFKVPIGVVAGILPWNFPFF--LIARKLAPALVTGNTIVIKPSEETPLNAL----EFAELVDEAGLPAGVLNI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 217 VYGSG--VGEALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEA-LRRrgrqVAEELAASVT 293
Cdd:cd07088 196 VTGRGsvVGDALVAHPKVGMISLTGSTEAGQKI--MEAAAENITKVSLELGGKAPAIVMKDAdLDL----AVKAIVDSRI 269
|
250 260 270
....*....|....*....|....*....|....
gi 15596450 294 LGCGQFCTKPGLVLgLRSPGFDAFVAALGEALAA 327
Cdd:cd07088 270 INCGQVCTCAERVY-VHEDIYDEFMEKLVEKMKA 302
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
56-324 |
2.06e-24 |
|
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: 106.11 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPaarIEGERT----RTANQLRLFAEVLRRGDFHGVRIDRG 131
Cdd:cd07093 32 FPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKP---ITLARTrdipRAAANFRFFADYILQLDGESYPQDGG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 132 QPGRTPPRPdlrqwrigLGPVAVFGASNFPLAFSTAggDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPD 211
Cdd:cd07093 109 ALNYVLRQP--------VGVAGLITPWNLPLMLLTW--KIAPALAFGNTVVLKPSEWTPLTAWLLAELANEA----GLPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 212 GVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEALRRRGRQVAeelA 289
Cdd:cd07093 175 GVVNVVHGFGpeAGAALVAHPDVDLISFTGETATGRTI--MRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAA---V 249
|
250 260 270
....*....|....*....|....*....|....*
gi 15596450 290 ASVTLGCGQFCTKPGLVLgLRSPGFDAFVAALGEA 324
Cdd:cd07093 250 RSSFSNNGEVCLAGSRIL-VQRSIYDEFLERFVER 283
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
56-327 |
3.98e-24 |
|
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: 104.82 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEvlrrgdfHGVRIDrgqpGR 135
Cdd:cd07103 32 FKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAE-------EARRIY----GR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 136 T--PPRPDLRQ--WRIGLGPVAVFGASNFPLAFST--AggdsAAALAAGCPVVVKAhgghmatAE---CVADAILQAAAD 206
Cdd:cd07103 101 TipSPAPGKRIlvIKQPVGVVAAITPWNFPAAMITrkI----APALAAGCTVVLKP-------AEetpLSALALAELAEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 207 SGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEA-LrrrgRQ 283
Cdd:cd07103 170 AGLPAGVLNVVTGSPaeIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK--RVSLELGGNAPFIVFDDAdL----DK 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15596450 284 VAEELAASVTLGCGQFCTKPGLVLGLRSpGFDAFVAALGEALAA 327
Cdd:cd07103 244 AVDGAIASKFRNAGQTCVCANRIYVHES-IYDEFVEKLVERVKK 286
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
51-423 |
1.39e-23 |
|
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: 102.99 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 51 AAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIDR 130
Cdd:cd07104 8 AAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRR--PEGEILPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 131 GQPGRTPprpdlRQWRIGLGPVAVFGASNFPLAFSTAGgdSAAALAAGCPVVVKAhggHMATAECVADAILQAAADSGMP 210
Cdd:cd07104 86 DVPGKES-----MVRRVPLGVVGVISPFNFPLILAMRS--VAPALALGNAVVLKP---DSRTPVTGGLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 211 DGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEA-LrrrgrqvaeE 287
Cdd:cd07104 156 KGVLNVVPGGGseIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLK--KVALELGGNNPLIVLDDAdL---------D 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 288 LAASVT-----LGCGQFCTKPGLVLGLRSpGFDAFVAALGEALAARPAQSMLNAGTL------RSYVEGLQRL---ERHP 353
Cdd:cd07104 225 LAVSAAafgafLHQGQICMAAGRILVHES-VYDEFVEKLVAKAKALPVGDPRDPDTVigplinERQVDRVHAIvedAVAA 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596450 354 GIRRLAGAPQEGRQAHPQLFkADVgllLEGDELLQEEVFGPATVVVEAADEEQ-LARALDNLHGqLSATLI 423
Cdd:cd07104 304 GARLLTGGTYEGLFYQPTVL-SDV---TPDMPIFREEIFGPVAPVIPFDDDEEaVELANDTEYG-LSAAVF 369
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
56-422 |
3.68e-23 |
|
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: 102.05 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETAlPAARIE--GERTRTANQLRLFAEVlrRGDFHGVRIdrgqp 133
Cdd:cd07108 32 FPEWAATPARERGKLLARIADALEARSEELARLLALETG-NALRTQarPEAAVLADLFRYFGGL--AGELKGETL----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 134 grtPPRPDLRQW--RIGLGPVAVFGASNFPLAFSTAggDSAAALAAGCPVVVKahgghmaTAECVADAILQAA--ADSGM 209
Cdd:cd07108 104 ---PFGPDVLTYtvREPLGVVGAILPWNAPLMLAAL--KIAPALVAGNTVVLK-------AAEDAPLAVLLLAeiLAQVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 210 PDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEAlrrrgrqVAEE 287
Cdd:cd07108 172 PAGVLNVITGYGeeCGAALVDHPDVDKVTFTGSTEVGKII--YRAAADRLIPVSLELGGKSPMIVFPDA-------DLDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 288 LAASVTLGC-----GQFCTKpGLVLGLRSPGFDAFVAALGEALAA----RPAQSMLNAGTLRS---------YVE-GLQR 348
Cdd:cd07108 243 AVDGAIAGMrftrqGQSCTA-GSRLFVHEDIYDAFLEKLVAKLSKlkigDPLDEATDIGAIISekqfakvcgYIDlGLST 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 349 lerhPGIRRLAGAPQ-------EGRQAHPQLF-KADVgllleGDELLQEEVFGPATVVVEAADEEQ-LARALDNLHGqLS 419
Cdd:cd07108 322 ----SGATVLRGGPLpgegplaDGFFVQPTIFsGVDN-----EWRLAREEIFGPVLCAIPWKDEDEvIAMANDSHYG-LA 391
|
...
gi 15596450 420 ATL 422
Cdd:cd07108 392 AYV 394
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
60-432 |
7.32e-22 |
|
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: 98.27 E-value: 7.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 60 RQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIdrgqPGRTPPR 139
Cdd:cd07094 38 RALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAER--IRGEEI----PLDATQG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 140 PDLRQ-W--RIGLGPVAVFGASNFPLAFSTAggDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFNM 216
Cdd:cd07094 112 SDNRLaWtiREPVGVVLAITPFNFPLNLVAH--KLAPAIATGCPVVLKPASKTPLSALELAKILVEA----GVPEGVLQV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 217 VYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIpvfaEMSSINPLVVLPEALRRRgrqVAEELAASVTL 294
Cdd:cd07094 186 VTGERevLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIAL----ELGGNAPVIVDRDADLDA---AIEALAKGGFY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 295 GCGQFCTKPGLVL---GLRSPGFDAFVAALGEALAARPAQSMLNAGTLRSyVEGLQRLERH------PGIRRLAGAPQEG 365
Cdd:cd07094 259 HAGQVCISVQRIYvheELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLIS-EEAAERVERWveeaveAGARLLCGGERDG 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596450 366 RQAHPQLFkADVgllLEGDELLQEEVFGPATVVVEAADEEQLARALDNLHGQLSATLIGEadDLAAF 432
Cdd:cd07094 338 ALFKPTVL-EDV---PRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR--DLNVA 398
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
59-276 |
6.82e-21 |
|
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: 95.36 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 59 YRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGdfHGVRIdrgqPGRTPP 138
Cdd:cd07149 37 MKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKRL--AGETI----PFDASP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 139 RPDLRQ---WRIGLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVKAhgghMATAECVADAILQAAADSGMPDGVFN 215
Cdd:cd07149 111 GGEGRIgftIREPIGVVAAITPFNFPL--NLVAHKVGPAIAAGNAVVLKP----ASQTPLSALKLAELLLEAGLPKGALN 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596450 216 MVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARpqpiPVFAEMSSINPLVVLPEA 276
Cdd:cd07149 185 VVTGSGetVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK----KVTLELGSNAAVIVDADA 243
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
56-416 |
7.40e-21 |
|
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: 95.09 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALP-AARIEGERTRTANQLRLFAEVLRrgDFHGVRIDRGQPG 134
Cdd:cd07092 32 FPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPlHLVRDDELPGAVDNFRFFAGAAR--TLEGPAAGEYLPG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 135 RTPPrpdLRqwRIGLGPVAVFGASNFPLAFSTAggDSAAALAAGCPVVVKAHGGHMATAecvadAILQAAADSGMPDGVF 214
Cdd:cd07092 110 HTSM---IR--REPIGVVAQIAPWNYPLMMAAW--KIAPALAAGNTVVLKPSETTPLTT-----LLLAELAAEVLPPGVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 215 NMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEALRRRgrqVAEELAASV 292
Cdd:cd07092 178 NVVCGGGasAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK--RVHLELGGKAPVIVFDDADLDA---AVAGIATAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 293 TLGCGQFCTKPGLVLgLRSPGFDAFVAALGEALAA----RPAQSMLNAGTL-----RSYVEGLqrLERHP-GIRRLA-GA 361
Cdd:cd07092 253 YYNAGQDCTAACRVY-VHESVYDEFVAALVEAVSAirvgDPDDEDTEMGPLnsaaqRERVAGF--VERAPaHARVLTgGR 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596450 362 PQEGRQAH--PQLfkadVGLLLEGDELLQEEVFGPATVVVEAADEEQ-LARALDNLHG 416
Cdd:cd07092 330 RAEGPGYFyePTV----VAGVAQDDEIVQEEIFGPVVTVQPFDDEDEaIELANDVEYG 383
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
56-272 |
8.26e-21 |
|
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: 95.37 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGdfhgvridRGQPGR 135
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRL--------RGFPVE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 136 TPPRPDLRQWRIGLGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVKAHGghmaTAECVADAILQAAADSGMPDGVFN 215
Cdd:cd07124 154 MVPGEDNRYVYRPLGVGAVISPWNFPLAILA--GMTTAALVTGNTVVLKPAE----DTPVIAAKLVEILEEAGLPPGVVN 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596450 216 MVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDlAAARPQPI-----PVFAEMSSINPLVV 272
Cdd:cd07124 228 FLPGPGeeVGDYLVEHPDVRFIAFTGSREVGLRIYE-RAAKVQPGqkwlkRVIAEMGGKNAIIV 290
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
60-413 |
3.52e-20 |
|
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: 93.07 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 60 RQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTAnqlRLFaevlrrgDFHGVRIDRGQpGRT-PP 138
Cdd:cd07109 37 LRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAA---RYF-------EYYGGAADKLH-GETiPL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 139 RPDLRQW--RIGLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVKAhgghMATAECVADAILQAAADSGMPDGVFNM 216
Cdd:cd07109 106 GPGYFVYtvREPHGVTGHIIPWNYPL--QITGRSVAPALAAGNAVVVKP----AEDAPLTALRLAELAEEAGLPAGALNV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 217 V--YGSGVGEALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEALRrrgRQVAEELAASVTL 294
Cdd:cd07109 180 VtgLGAEAGAALVAHPGVDHISFTGSVETGIAV--MRAAAENVVPVTLELGGKSPQIVFADADL---EAALPVVVNAIIQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 295 GCGQFCTKPGLVLGLRSPgFDAFVAALGEALAAR---PAQSMLNAGTL-----RSYVEGLQRLERHPGIRRLAG------ 360
Cdd:cd07109 255 NAGQTCSAGSRLLVHRSI-YDEVLERLVERFRALrvgPGLEDPDLGPLisakqLDRVEGFVARARARGARIVAGgriaeg 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15596450 361 APQEGRQAHPQLFkADVgllLEGDELLQEEVFGPATVVVEAADEEQlARALDN 413
Cdd:cd07109 334 APAGGYFVAPTLL-DDV---PPDSRLAQEEIFGPVLAVMPFDDEAE-AIALAN 381
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
60-409 |
4.57e-20 |
|
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: 93.02 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 60 RQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIE-GERTRTANQLRLFAEVLRRGDFHGVRidrgqPGRTPP 138
Cdd:cd07139 55 PRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERR-----PGSGGG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 139 RPDLRQwriglGPVAVFGAS---NFPLafSTAGGDSAAALAAGCPVVVKAhgghmaTAECVADAIL--QAAADSGMPDGV 213
Cdd:cd07139 130 HVLVRR-----EPVGVVAAIvpwNAPL--FLAALKIAPALAAGCTVVLKP------SPETPLDAYLlaEAAEEAGLPPGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 214 FNMVYGS-GVGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEALRRRgrqVAEELAASV 292
Cdd:cd07139 197 VNVVPADrEVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA--RVTLELGGKSAAIVLDDADLDA---AVPGLVPAS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 293 TLGCGQFCTKPGLVLGLRSPgFDAFVAALGEALAARPAQSMLNAGTL---------RSYVEGLQRLERHPGIRRLAGApq 363
Cdd:cd07139 272 LMNNGQVCVALTRILVPRSR-YDEVVEALAAAVAALKVGDPLDPATQigplasarqRERVEGYIAKGRAEGARLVTGG-- 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15596450 364 eGRQAH--------PQLFkADVgllLEGDELLQEEVFGPATVVVEAADEEQLAR 409
Cdd:cd07139 349 -GRPAGldrgwfvePTLF-ADV---DNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
60-327 |
7.36e-20 |
|
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: 92.25 E-value: 7.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 60 RQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDFHGVRIDR--------G 131
Cdd:cd07082 56 PTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWfpgtkgkiA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 132 QPGRTPprpdlrqwrigLGPVAVFGASNFPL--AFSTAggdsAAALAAGCPVVVKAhgghmATAECVADA-ILQAAADSG 208
Cdd:cd07082 136 QVRREP-----------LGVVLAIGPFNYPLnlTVSKL----IPALIMGNTVVFKP-----ATQGVLLGIpLAEAFHDAG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 209 MPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAArpqpIPVFAEMSSINPLVVLPEA-Lrrrgrqva 285
Cdd:cd07082 196 FPKGVVNVVTGRGreIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM----KRLVLELGGKDPAIVLPDAdL-------- 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15596450 286 eELAAS-VTLGC----GQFCTKPGLVLGLRSPgFDAFVAALGEALAA 327
Cdd:cd07082 264 -ELAAKeIVKGAlsysGQRCTAIKRVLVHESV-ADELVELLKEEVAK 308
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
56-303 |
9.90e-20 |
|
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: 91.80 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALP---AARIEGERTrtANQLRLFAEVLRRGDFhgvridRGQ 132
Cdd:cd07138 49 FPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPitlARAAQVGLG--IGHLRAAADALKDFEF------EER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 133 PGRTpprpdlrqwRIGLGPVAVFGAS---NFPLAFSTAggDSAAALAAGCPVVVK----AHGGHMATAECVADAilqaaa 205
Cdd:cd07138 121 RGNS---------LVVREPIGVCGLItpwNWPLNQIVL--KVAPALAAGCTVVLKpsevAPLSAIILAEILDEA------ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 206 dsGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAA---RpqpipVFAEMSSINPLVVLPEAlrrr 280
Cdd:cd07138 184 --GLPAGVFNLVNGDGpvVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADtvkR-----VALELGGKSANIILDDA---- 252
|
250 260 270
....*....|....*....|....*....|
gi 15596450 281 grqvaeELAASVTLG-------CGQFCTKP 303
Cdd:cd07138 253 ------DLEKAVPRGvaacfanSGQSCNAP 276
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
57-324 |
1.42e-19 |
|
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: 91.46 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 57 PHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDfhgvridrgqpGRT 136
Cdd:cd07114 35 GAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIE-----------GAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 137 PP--RPDLRQW--RIGLGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDG 212
Cdd:cd07114 104 IPvdKGDYLNFtrREPLGVVAAITPWNSPLLLLA--KKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEA----GFPPG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 213 VFNMV--YGSGVGEALVRHPAIRAVGFTGSLKGGRALCDLAAARpqPIPVFAEMSSINPLVVLPEALRRRGrqvAEELAA 290
Cdd:cd07114 178 VVNVVtgFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN--LAPVTLELGGKSPNIVFDDADLDAA---VNGVVA 252
|
250 260 270
....*....|....*....|....*....|....*...
gi 15596450 291 SVTLGCGQFCtkpglVLGLR----SPGFDAFVAALGEA 324
Cdd:cd07114 253 GIFAAAGQTC-----VAGSRllvqRSIYDEFVERLVAR 285
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
51-326 |
1.68e-19 |
|
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: 90.79 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 51 AAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQ--LRLFAEVLRRGDfhgVRI 128
Cdd:cd07095 8 AARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKidISIKAYHERTGE---RAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 129 DRGQ-PGRTPPRPdlrqwrigLGPVAVFGASNFPLAFstAGGDSAAALAAGCPVVVKAHgghmATAECVADAILQAAADS 207
Cdd:cd07095 85 PMAQgRAVLRHRP--------HGVMAVFGPFNFPGHL--PNGHIVPALLAGNTVVFKPS----ELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 208 GMPDGVFNMVYGSG-VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVFaEMSSINPLVVLPEALRrrgRQVAE 286
Cdd:cd07095 151 GLPPGVLNLVQGGReTGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILAL-EMGGNNPLVVWDVADI---DAAAY 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15596450 287 ELAASVTLGCGQFCTKPGLVLGLRSPGFDAFVAALGEALA 326
Cdd:cd07095 227 LIVQSAFLTAGQRCTCARRLIVPDGAVGDAFLERLVEAAK 266
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
8-301 |
7.32e-19 |
|
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: 89.16 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 8 NYVGGARSAAGNLTLRSLDADSGEALpYAFVQATEAEVDAAARAAERAYPHYRQLSATRRAGFL----EAIASRLDALGd 83
Cdd:cd07086 1 GVIGGEWVGSGGETFTSRNPANGEPI-ARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVrqigEALRKKKEALG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 84 dfvALVRRETALPAARIEGERTrtanqlrlfaEVLRRGDFhGVRIDRGQPGRTPP--RPD---LRQWRiGLGPVAVFGAS 158
Cdd:cd07086 79 ---RLVSLEMGKILPEGLGEVQ----------EMIDICDY-AVGLSRMLYGLTIPseRPGhrlMEQWN-PLGVVGVITAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 159 NFPLAfsTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAAADSGMPDGVFNMVYGSG-VGEALVRHPAIRAVGF 237
Cdd:cd07086 144 NFPVA--VPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGdGGELLVHDPRVPLVSF 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596450 238 TGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEAlrrrgrqvAEELAA-SVTLGC----GQFCT 301
Cdd:cd07086 222 TGSTEVGRRVGETVARRFG--RVLLELGGNNAIIVMDDA--------DLDLAVrAVLFAAvgtaGQRCT 280
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
60-276 |
1.41e-18 |
|
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: 88.43 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 60 RQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFA----EVLRRGDFHGVRIDRGQPGR 135
Cdd:cd07099 35 AALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAArnapRVLAPRKVPTGLLMPNKKAT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 136 TPPRPdlrqwrigLGPVAVFGASNFPLAfsTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAIlqaaADSGMPDGVFN 215
Cdd:cd07099 115 VEYRP--------YGVVGVISPWNYPLL--TPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAW----AAAGPPQGVLQ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596450 216 MVYGSG-VGEALVRHPaIRAVGFTGSLKGGRALCDLAAARpqPIPVFAEMSSINPLVVLPEA 276
Cdd:cd07099 181 VVTGDGaTGAALIDAG-VDKVAFTGSVATGRKVMAAAAER--LIPVVLELGGKDPMIVLADA 239
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
56-300 |
1.83e-18 |
|
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: 87.97 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFA------EVLRRGDFHGVRID 129
Cdd:cd07106 32 FPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTAsldlpdEVIEDDDTRRVELR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 130 RgqpgrtppRPdlrqwrigLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVK-AHGGHMATAECVAdaILQAAadsg 208
Cdd:cd07106 112 R--------KP--------LGVVAAIVPWNFPL--LLAAWKIAPALLAGNTVVLKpSPFTPLCTLKLGE--LAQEV---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 209 MPDGVFNMVYGSG-VGEALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEALRRRgrqVAEE 287
Cdd:cd07106 168 LPPGVLNVVSGGDeLGPALTSHPDIRKISFTGSTATGKKV--MASAAKTLKRVTLELGGNDAAIVLPDVDIDA---VAPK 242
|
250
....*....|...
gi 15596450 288 LAASVTLGCGQFC 300
Cdd:cd07106 243 LFWGAFINSGQVC 255
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
62-329 |
2.41e-17 |
|
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: 84.60 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 62 LSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRT-ANQLRLFAEVLRRGDFHGVRIDRGQPGRTPPRp 140
Cdd:cd07089 39 TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGpIGHLRYFADLADSFPWEFDLPVPALRGGPGRR- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 141 dlRQWRIGLGPVAVFGASNFPlaFSTAGGDSAAALAAGCPVVVKAhgghMATAECVADAILQAAADSGMPDGVFNMVYGS 220
Cdd:cd07089 118 --VVRREPVGVVAAITPWNFP--FFLNLAKLAPALAAGNTVVLKP----APDTPLSALLLGEIIAETDLPAGVVNVVTGS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 221 G--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEALrrrGRQVAEELAASVTLGCGQ 298
Cdd:cd07089 190 DnaVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLK--RVLLELGGKSANIVLDDAD---LAAAAPAAVGVCMHNAGQ 264
|
250 260 270
....*....|....*....|....*....|.
gi 15596450 299 FCTKPGLVLGLRSPgFDAFVAALGEALAARP 329
Cdd:cd07089 265 GCALTTRLLVPRSR-YDEVVEALAAAFEALP 294
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-327 |
2.48e-17 |
|
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: 84.35 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 39 QATEAEVDAAARAAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAevl 118
Cdd:cd07107 15 AASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFA--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 119 rrGDFHGVridRGQPGRTPPRPDLRQWRIGLGPVAVFGASNFPLAFstAGGDSAAALAAGCPVVVKAhgghmatAECVAD 198
Cdd:cd07107 92 --GLVTEL---KGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMF--AAAKIAAPLAAGNTVVVKP-------PEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 199 AILQAA--ADSGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLP 274
Cdd:cd07107 158 SALRLAelAREVLPPGVFNILPGDGatAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK--HVTLELGGKNALIVFP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15596450 275 EAlrrRGRQVAEELAASVTLG-CGQFCTKPGLVLGLRSPgFDAFVAALGEALAA 327
Cdd:cd07107 236 DA---DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESI-YDEVLARVVERVAA 285
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-416 |
2.84e-17 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 84.19 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 7 HNYVGGARSAAGNLTLRSLDADSGEALpYAFVQATEAEVDAAARAAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFV 86
Cdd:PRK13473 4 KLLINGELVAGEGEKQPVYNPATGEVL-AEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 87 ALVRRETALP-AARIEGERTRTANQLRLFAEVLRrgDFHGVRIDRGQPGRTPPrpdLRqwRIGLGPVAVFGASNFPLAFs 165
Cdd:PRK13473 83 RLESLNCGKPlHLALNDEIPAIVDVFRFFAGAAR--CLEGKAAGEYLEGHTSM---IR--RDPVGVVASIAPWNYPLMM- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 166 tAGGDSAAALAAGCPVVVKAHGGHMATAECVAdailQAAADSgMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKG 243
Cdd:PRK13473 155 -AAWKLAPALAAGNTVVLKPSEITPLTALKLA----ELAADI-LPPGVLNVVTGRGatVGDALVGHPKVRMVSLTGSIAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 244 GRALcdLAAARPQPIPVFAEMSSINPLVVLPEA-LrrrgRQVAEELAASVTLGCGQFCTKPGLVLGLRSPgFDAFVAALG 322
Cdd:PRK13473 229 GKHV--LSAAADSVKRTHLELGGKAPVIVFDDAdL----DAVVEGIRTFGYYNAGQDCTAACRIYAQRGI-YDDLVAKLA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 323 EALAA----RPAQSMLNAGTL-----RSYVEGL-QRLERHPGIRRLAG-APQEGRQAH--PQLFkADVgllLEGDELLQE 389
Cdd:PRK13473 302 AAVATlkvgDPDDEDTELGPLisaahRDRVAGFvERAKALGHIRVVTGgEAPDGKGYYyePTLL-AGA---RQDDEIVQR 377
|
410 420
....*....|....*....|....*...
gi 15596450 390 EVFGPATVVVEAADEEQ-LARALDNLHG 416
Cdd:PRK13473 378 EVFGPVVSVTPFDDEDQaVRWANDSDYG 405
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
56-276 |
5.03e-17 |
|
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: 83.40 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDfhGVRIDRGQPGR 135
Cdd:cd07105 13 FPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQII--GGSIPSDKPGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 136 TPprpdlRQWRIGLGPVAVFGASNFPLAFSTAGgdSAAALAAGCPVVVKAHgghmATAECVADAILQAAADSGMPDGVFN 215
Cdd:cd07105 91 LA-----MVVKEPVGVVLGIAPWNAPVILGTRA--IAYPLAAGNTVVLKAS----ELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596450 216 MVYGS-----GVGEALVRHPAIRAVGFTGSLKGGRALCDLAAArpQPIPVFAEMSSINPLVVLPEA 276
Cdd:cd07105 160 VVTHSpedapEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK--HLKPVLLELGGKAPAIVLEDA 223
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
62-339 |
8.00e-17 |
|
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: 82.79 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 62 LSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDFHGVRIDRGQPGR-----T 136
Cdd:cd07146 37 LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFSCDLTANGKarkifT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 137 PPRPdlrqwrigLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFNM 216
Cdd:cd07146 117 LREP--------LGVVLAITPFNHPL--NQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEA----GLPPDMLSV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 217 VYG--SGVGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIpvfaEMSSINPLVVLPEALRRRGRQVAeelAASVTL 294
Cdd:cd07146 183 VTGepGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLL----ELGGNDPLIVMDDADLERAATLA---VAGSYA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15596450 295 GCGQFCTKPGLVLGLRSPgFDAFVAALGEALAAR----PAQSMLNAGTL 339
Cdd:cd07146 256 NSGQRCTAVKRILVHESV-ADEFVDLLVEKSAALvvgdPMDPATDMGTV 303
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-323 |
1.29e-16 |
|
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: 82.40 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 57 PHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLR--RGDFhgVRIDRGQPG 134
Cdd:cd07145 35 DVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKvlRGET--IPVDAYEYN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 135 RTPPRPDLRQwriglgPVAVFGAS---NFPLAFSTAggDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPD 211
Cdd:cd07145 113 ERRIAFTVRE------PIGVVGAItpfNFPANLFAH--KIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEA----GLPP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 212 GVFNMV--YGSGVGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVfaEMSSINPLVVLPEA-LRRrgrqVAEEL 288
Cdd:cd07145 181 GVINVVtgYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVAL--ELGGSDPMIVLKDAdLER----AVSIA 254
|
250 260 270
....*....|....*....|....*....|....*
gi 15596450 289 AASVTLGCGQFCTKPGLVLgLRSPGFDAFVAALGE 323
Cdd:cd07145 255 VRGRFENAGQVCNAVKRIL-VEEEVYDKFLKLLVE 288
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
56-300 |
2.55e-16 |
|
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: 81.47 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETA--LPAARIEgerTRTA-NQLRLFAEVLRRgDFHGVRIdrgq 132
Cdd:cd07125 82 FAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGktLADADAE---VREAiDFCRYYAAQARE-LFSDPEL---- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 133 PGRTPPRPDLrQWRiGLGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVKAhgghmatAE---CVADAILQAAADSGM 209
Cdd:cd07125 154 PGPTGELNGL-ELH-GRGVFVCISPWNFPLAIFT--GQIAAALAAGNTVIAKP-------AEqtpLIAARAVELLHEAGV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 210 PDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPI-PVFAEMSSINPLVVLPEALRrrgRQVAE 286
Cdd:cd07125 223 PRDVLQLVPGDGeeIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPIlPLIAETGGKNAMIVDSTALP---EQAVK 299
|
250
....*....|....
gi 15596450 287 ELAASVTLGCGQFC 300
Cdd:cd07125 300 DVVQSAFGSAGQRC 313
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
56-253 |
2.69e-16 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 81.66 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRR--GDFhgvridrgqp 133
Cdd:PLN02278 75 FPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRvyGDI---------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 134 gRTPPRPD-----LRQwriglgPVAVFGAS---NFPLAFSTAggDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaa 205
Cdd:PLN02278 145 -IPSPFPDrrllvLKQ------PVGVVGAItpwNFPLAMITR--KVGPALAAGCTVVVKPSELTPLTALAAAELALQA-- 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596450 206 dsGMPDGVFNMVYG--SGVGEALVRHPAIRAVGFTGSLKGGRALCDLAAA 253
Cdd:PLN02278 214 --GIPPGVLNVVMGdaPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA 261
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
61-409 |
8.59e-16 |
|
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: 79.66 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 61 QLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIDRGQPGRTPprp 140
Cdd:cd07151 50 ATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLR--MEGRILPSDVPGKEN--- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 141 dlRQWRIGLGPVAVFGASNFPLAFSTAGgdSAAALAAGCPVVVKAHGGHMATAECVADAILQAAadsGMPDGVFNMVYGS 220
Cdd:cd07151 125 --RVYREPLGVVGVISPWNFPLHLSMRS--VAPALALGNAVVLKPASDTPITGGLLLAKIFEEA---GLPKGVLNVVVGA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 221 G--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAArpqPIPVFA-EMSSINPLVVLPEAlrrRGRQVAEELAASVTLGCG 297
Cdd:cd07151 198 GseIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR---HLKKVAlELGGNNPFVVLEDA---DIDAAVNAAVFGKFLHQG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 298 QFCTKPGLVLgLRSPGFDAFVAALGEALAARPAQSMLNAGTL------RSYVEGLQ---RLERHPGIRRLAGAPQEGRQA 368
Cdd:cd07151 272 QICMAINRII-VHEDVYDEFVEKFVERVKALPYGDPSDPDTVvgplinESQVDGLLdkiEQAVEEGATLLVGGEAEGNVL 350
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15596450 369 HPQLFkADVGLLLEGDELLqeeVFGPATVVVEAADEEQLAR 409
Cdd:cd07151 351 EPTVL-SDVTNDMEIAREE---IFGPVAPIIKADDEEEALE 387
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
146-276 |
9.42e-16 |
|
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: 79.66 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 146 RIGLGPVAVFGASNFPlaFSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADaILQAAadsGMPDGVFNMVYGSG-VGE 224
Cdd:cd07090 114 REPLGVCAGIGAWNYP--IQIASWKSAPALACGNAMVYKPSPFTPLTALLLAE-ILTEA---GLPDGVFNVVQGGGeTGQ 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15596450 225 ALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEA 276
Cdd:cd07090 188 LLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIK--HVTLELGGKSPLIIFDDA 237
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
151-327 |
8.53e-15 |
|
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: 76.49 E-value: 8.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 151 PVAVFGAS---NFPLafSTAGGDSAAALAAGCPVVVKAHGGHMATAECVAdailQAAADSGMPDGVFNMVYGSG--VGEA 225
Cdd:cd07112 124 PLGVVGAVvpwNFPL--LMAAWKIAPALAAGNSVVLKPAEQSPLTALRLA----ELALEAGLPAGVLNVVPGFGhtAGEA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 226 LVRHPAIRAVGFTGSLKGGRALCDlAAARPQPIPVFAEMSSINPLVVLPEA--LRRrgrqVAEELAASVTLGCGQFCTKP 303
Cdd:cd07112 198 LGLHMDVDALAFTGSTEVGRRFLE-YSGQSNLKRVWLECGGKSPNIVFADApdLDA----AAEAAAAGIFWNQGEVCSAG 272
|
170 180
....*....|....*....|....
gi 15596450 304 GLVLgLRSPGFDAFVAALGEALAA 327
Cdd:cd07112 273 SRLL-VHESIKDEFLEKVVAAARE 295
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
70-300 |
1.01e-14 |
|
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: 76.52 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 70 FLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLrrgdfhgvridrgQPGRTPPRPDLRQW--RI 147
Cdd:cd07102 49 AVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEAL-------------ADIRVPEKDGFERYirRE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 148 GLGPVAVFGASNFPLAfsTAGGDSAAALAAGCPVVVKahggHMATAECVADAILQAAADSGMPDGVFNMVYGSG-VGEAL 226
Cdd:cd07102 116 PLGVVLIIAPWNYPYL--TAVNAVIPALLAGNAVILK----HSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHeTSAAL 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596450 227 VRHPAIRAVGFTGSLKGGRALCDLAAARpqPIPVFAEMSSINPLVVLPEAlrrRGRQVAEELAASVTLGCGQFC 300
Cdd:cd07102 190 IADPRIDHVSFTGSVAGGRAIQRAAAGR--FIKVGLELGGKDPAYVRPDA---DLDAAAESLVDGAFFNSGQSC 258
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
62-423 |
2.14e-14 |
|
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: 75.41 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 62 LSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGdfHGVrIDRGQPGRTPprpd 141
Cdd:cd07152 32 TPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQP--QGE-ILPSAPGRLS---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 142 lRQWRIGLGPVAVFGASNFPLAFSTAGgdSAAALAAGCPVVVKAHgghMATAECVADAILQAAADSGMPDGVFNMVYGSG 221
Cdd:cd07152 105 -LARRVPLGVVGVISPFNFPLILAMRS--VAPALALGNAVVLKPD---PRTPVSGGVVIARLFEEAGLPAGVLHVLPGGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 222 -VGEALVRHPAIRAVGFTGSLKGGRALCDLAAarPQPIPVFAEMSSINPLVVLPEAlrrrgrqvAEELAASVT-----LG 295
Cdd:cd07152 179 dAGEALVEDPNVAMISFTGSTAVGRKVGEAAG--RHLKKVSLELGGKNALIVLDDA--------DLDLAASNGawgafLH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 296 CGQFCTKPGLVLGLRSPgFDAFVAALGEALAARPAQS----------MLNAGTLRSyVEGLQRLERHPGIRRLAGAPQEG 365
Cdd:cd07152 249 QGQICMAAGRHLVHESV-ADAYTAKLAAKAKHLPVGDpatgqvalgpLINARQLDR-VHAIVDDSVAAGARLEAGGTYDG 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596450 366 RQAHPQLFkADVgllLEGDELLQEEVFGP-ATVVVEAADEEQLARALDNLHGqLSATLI 423
Cdd:cd07152 327 LFYRPTVL-SGV---KPGMPAFDEEIFGPvAPVTVFDSDEEAVALANDTEYG-LSAGII 380
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
56-409 |
2.33e-14 |
|
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: 75.17 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALP-AARIEGERTRTANQLRLFAEVLRRgdFHGVRIdrgqpg 134
Cdd:cd07115 32 FEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPiRAARRLDVPRAADTFRYYAGWADK--IEGEVI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 135 rtPPRPDLRQWRIgLGPVAVFGAS---NFPLAFstAGGDSAAALAAGCPVVVKAhgghMATAECVADAILQAAADSGMPD 211
Cdd:cd07115 104 --PVRGPFLNYTV-REPVGVVGAIvpwNFPLMF--AAWKVAPALAAGNTVVLKP----AELTPLSALRIAELMAEAGFPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 212 GVFNMV--YGSGVGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVfaEMSSINPLVVLPEALRRRGRQVAeelA 289
Cdd:cd07115 175 GVLNVVtgFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSL--ELGGKSANIVFADADLDAAVRAA---A 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 290 ASVTLGCGQFCTKPGLVLGLRSPgFDAFVaalgEALAAR-----------------PAQSMLNAGTLRSYVEglqrLERH 352
Cdd:cd07115 250 TGIFYNQGQMCTAGSRLLVHESI-YDEFL----ERFTSLarslrpgdpldpktqmgPLVSQAQFDRVLDYVD----VGRE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 353 PGIRRLAGAPQEGRQAH---PQLFKAdvglLLEGDELLQEEVFGPATVVVEAADEEQLAR 409
Cdd:cd07115 321 EGARLLTGGKRPGARGFfvePTIFAA----VPPEMRIAQEEIFGPVVSVMRFRDEEEALR 376
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
149-300 |
1.20e-13 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 73.85 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 149 LGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVK-AHGGHMATAECVAdaILQAAadsGMPDGVFNMVYGSG--VGEA 225
Cdd:PRK11809 769 LGPVVCISPWNFPLAIFT--GQVAAALAAGNSVLAKpAEQTPLIAAQAVR--ILLEA---GVPAGVVQLLPGRGetVGAA 841
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596450 226 LVRHPAIRAVGFTGSLKGGRALCDLAAAR--PQ--PIPVFAEMSSINPLVVLPEALrrrGRQVAEELAASVTLGCGQFC 300
Cdd:PRK11809 842 LVADARVRGVMFTGSTEVARLLQRNLAGRldPQgrPIPLIAETGGQNAMIVDSSAL---TEQVVADVLASAFDSAGQRC 917
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
59-413 |
1.70e-13 |
|
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: 72.73 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 59 YRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDfhgvridrgqpGRTPP 138
Cdd:cd07119 53 WPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKET-----------GEVYD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 139 RPDLRQWRIGLGPVAVFGAS---NFPLAfsTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFN 215
Cdd:cd07119 122 VPPHVISRTVREPVGVCGLItpwNYPLL--QAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEA----GLPAGVVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 216 MVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVfaEMSSINPLVVLPEAlrrrGRQVAEELA-ASV 292
Cdd:cd07119 196 LVTGSGatVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVAL--ELGGKNPNIVFADA----DFETAVDQAlNGV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 293 TLGCGQFCTKpGLVLGLRSPGFDAFVAALGEALAARPAQSMLNAGT---------LRSYVEGLQRLERHPGIRRLAG--A 361
Cdd:cd07119 270 FFNAGQVCSA-GSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTemgplvsaeHREKVLSYIQLGKEEGARLVCGgkR 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596450 362 PQEGRQAH-----PQLFkADVgllLEGDELLQEEVFGPaTVVVEAADEEQLARALDN 413
Cdd:cd07119 349 PTGDELAKgyfvePTIF-DDV---DRTMRIVQEEIFGP-VLTVERFDTEEEAIRLAN 400
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
57-276 |
1.98e-13 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 72.63 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 57 PHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRgdFHGVRIdrgqPGRt 136
Cdd:PRK11241 62 PAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKR--IYGDTI----PGH- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 137 ppRPDLRQWRIG--LGPVAVFGASNFPLAFSTAggDSAAALAAGCPVVVKAhgghMATAECVADAILQAAADSGMPDGVF 214
Cdd:PRK11241 135 --QADKRLIVIKqpIGVTAAITPWNFPAAMITR--KAGPALAAGCTMVLKP----ASQTPFSALALAELAIRAGIPAGVF 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596450 215 NMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVfaEMSSINPLVVLPEA 276
Cdd:PRK11241 207 NVVTGSAgaVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSL--ELGGNAPFIVFDDA 268
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
66-420 |
2.57e-13 |
|
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: 71.99 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 66 RRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEvlrrgdfhgvrIDRGQPGRT-PPRPD--- 141
Cdd:cd07120 43 LRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAG-----------LARTEAGRMiEPEPGsfs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 142 --LRQwriglgPVAVFGAS---NFPLAFSTAggDSAAALAAGCPVVVKAHGghmATAEcVADAILQAAAD-SGMPDGVFN 215
Cdd:cd07120 112 lvLRE------PMGVAGIIvpwNSPVVLLVR--SLAPALAAGCTVVVKPAG---QTAQ-INAAIIRILAEiPSLPAGVVN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 216 MVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEA-LRRrgrqVAEELAASV 292
Cdd:cd07120 180 LFTESGseGAAHLVASPDVDVISFTGSTATGRAI--MAAAAPTLKRLGLELGGKTPCIVFDDAdLDA----ALPKLERAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 293 TLGCGQFCTKPGLVLGLRSPgFDAFVAALGEALAARPAQSMLNAGTL---------RSYVEGLQRLERHPGIRRL--AGA 361
Cdd:cd07120 254 TIFAGQFCMAGSRVLVQRSI-ADEVRDRLAARLAAVKVGPGLDPASDmgplidranVDRVDRMVERAIAAGAEVVlrGGP 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 362 PQEGRQAHPQLFKADVGLLLEGDELLQEEVFGPATVVVEAADE-EQLARALDNLHGqLSA 420
Cdd:cd07120 333 VTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEaEAVALANDTDYG-LAA 391
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
126-276 |
2.95e-13 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 71.89 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 126 VRIDRGQPGRTPPRPDLRQWRIGLGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVKAhgghMATAECVADAILQAAA 205
Cdd:PRK03137 149 LKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMA--GMTLAAIVAGNTVLLKP----ASDTPVIAAKFVEVLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 206 DSGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGralCDL--AAARPQP-----IPVFAEMSSINPLVVLPEA 276
Cdd:PRK03137 223 EAGLPAGVVNFVPGSGseVGDYLVDHPKTRFITFTGSREVG---LRIyeRAAKVQPgqiwlKRVIAEMGGKDAIVVDEDA 299
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
59-276 |
3.63e-13 |
|
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: 71.60 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 59 YRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRlFAEVLRRGdFHGVRIDRGQPGRTPP 138
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWR-YAASLART-LHGDSYNNLGDDMLGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 139 RpdLRQwriGLGPVAVFGASNFPlaFSTAGGDSAAALAAGCPVVVKAHGGHMATAECVAdailQAAADSGMPDGVFNMVY 218
Cdd:cd07118 115 V--LRE---PIGVVGIITPWNFP--FLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLA----ELLIEAGLPAGVVNIVT 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 219 GSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVfaEMSSINPLVVLPEA 276
Cdd:cd07118 184 GYGatVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSL--ELGGKNPQIVFADA 241
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
6-449 |
8.41e-13 |
|
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: 70.55 E-value: 8.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 6 GHnYVGGARSAAGNLTLRSLDADSGEALPYAFVQATEAEVDAAARAAERAY-PHYRQLSATRRAGFLEAIASRLDALGDD 84
Cdd:cd07113 1 GH-FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 85 FVALvrrETALPAARIEGERT----RTANQLRLFAEVlrRGDFHGVRIDRGQPGRTPPRPDLRQWRIGLGPVAVFGASNF 160
Cdd:cd07113 80 LAQL---ETLCSGKSIHLSRAfevgQSANFLRYFAGW--ATKINGETLAPSIPSMQGERYTAFTRREPVGVVAGIVPWNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 161 PLAFstAGGDSAAALAAGCPVVVKAHGGHMATAECVAdailQAAADSGMPDGVFNMVYGSG-VGEALVRHPAIRAVGFTG 239
Cdd:cd07113 155 SVMI--AVWKIGAALATGCTIVIKPSEFTPLTLLRVA----ELAKEAGIPDGVLNVVNGKGaVGAQLISHPDVAKVSFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 240 SLKGGRALCDLAAARPQPIPVfaEMSSINPLVVLPEALRRRgrqVAEELAASVTLGCGQFCTKPGLVLgLRSPGFDAFVA 319
Cdd:cd07113 229 SVATGKKIGRQAASDLTRVTL--ELGGKNAAAFLKDADIDW---VVEGLLTAGFLHQGQVCAAPERFY-VHRSKFDELVT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 320 ALGEAL-AARPAQSM---------LNAGTLRSYVEGLQRlERHPGIRRLAGA---PQEGRQAHPQLfkadVGLLLEGDEL 386
Cdd:cd07113 303 KLKQALsSFQVGSPMdesvmfgplANQPHFDKVCSYLDD-ARAEGDEIVRGGealAGEGYFVQPTL----VLARSADSRL 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596450 387 LQEEVFGPATVVVEAADEEQLARALDNLHGQLSATLIGEadDLAAFAGLVPLLErkAGRLLFN 449
Cdd:cd07113 378 MREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTN--NLSKALRYIPRIE--AGTVWVN 436
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
149-301 |
8.63e-13 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 70.53 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 149 LGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVKAhgGHMATAECVADAilQAAADSGMPDGVFNMVYGSG--VGEAL 226
Cdd:PLN02467 152 LGVVGLITPWNYPLLMAT--WKVAPALAAGCTAVLKP--SELASVTCLELA--DICREVGLPPGVLNVVTGLGteAGAPL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 227 VRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEalrrrgrqVAEELAASVTL-GC----GQFCT 301
Cdd:PLN02467 226 ASHPGVDKIAFTGSTATGRKI--MTAAAQMVKPVSLELGGKSPIIVFDD--------VDLDKAVEWAMfGCfwtnGQICS 295
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
51-423 |
8.79e-13 |
|
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: 70.46 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 51 AAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRrgdfhgvRIDR 130
Cdd:cd07110 27 AARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAE-------QLDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 131 GQPGRTP-PRPDLRQwRIGLGPVAVFGAS---NFPLAfsTAGGDSAAALAAGCPVVVKAhgGHMATAECVadAILQAAAD 206
Cdd:cd07110 100 KAERAVPlPSEDFKA-RVRREPVGVVGLItpwNFPLL--MAAWKVAPALAAGCTVVLKP--SELTSLTEL--ELAEIAAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 207 SGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVfaEMSSINPLVVLPEAlrrrgrqv 284
Cdd:cd07110 173 AGLPPGVLNVVTGTGdeAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSL--ELGGKSPIIVFDDA-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 285 AEELAASVTL-GC----GQFCTKPGLVLgLRSPGFDAFVAALGEALAARPAQSMLNAGTL---------RSYVEGLQRLE 350
Cdd:cd07110 243 DLEKAVEWAMfGCfwnnGQICSATSRLL-VHESIADAFLERLATAAEAIRVGDPLEEGVRlgplvsqaqYEKVLSFIARG 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596450 351 RHPGIRRLAGA--PQEGRQAH---PQLFkADVgllLEGDELLQEEVFGPATVVVE-AADEEQLARALDNLHGqLSATLI 423
Cdd:cd07110 322 KEEGARLLCGGrrPAHLEKGYfiaPTVF-ADV---PTDSRIWREEIFGPVLCVRSfATEDEAIALANDSEYG-LAAAVI 395
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
151-253 |
1.26e-12 |
|
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: 69.93 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 151 PVAVFGAS---NFPL---AFSTAggdsaAALAAGCPVVVKahgghmaTAEC-------VADAILQAaadsGMPDGVFNMV 217
Cdd:cd07091 141 PIGVCGQIipwNFPLlmlAWKLA-----PALAAGNTVVLK-------PAEQtplsalyLAELIKEA----GFPPGVVNIV 204
|
90 100 110
....*....|....*....|....*....|....*...
gi 15596450 218 YGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAA 253
Cdd:cd07091 205 PGFGptAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
56-301 |
1.54e-12 |
|
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: 69.55 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETAlpaariegertRTANQLrlFAEVLRRGDFhgVRIDRGQPGR 135
Cdd:TIGR01238 87 FPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAG-----------KTIHNA--IAEVREAVDF--CRYYAKQVRD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 136 TPPRPDLRqwriGLGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVK-AHGGHMATAECVadAILQAAadsGMPDGVF 214
Cdd:TIGR01238 152 VLGEFSVE----SRGVFVCISPWNFPLAIFT--GQISAALAAGNTVIAKpAEQTSLIAYRAV--ELMQEA---GFPAGTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 215 NMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAAR-PQPIPVFAEMSSINPLVVLPEALrrrGRQVAEELAAS 291
Cdd:TIGR01238 221 QLLPGRGadVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQReDAPVPLIAETGGQNAMIVDSTAL---PEQVVRDVLRS 297
|
250
....*....|
gi 15596450 292 VTLGCGQFCT 301
Cdd:TIGR01238 298 AFDSAGQRCS 307
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
159-300 |
2.17e-12 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 69.84 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 159 NFPLAFSTagGDSAAALAAGCPVVVKAhgghmatAE---CVADAILQAAADSGMPDGVFNMVYGSG--VGEALVRHPAIR 233
Cdd:PRK11904 695 NFPLAIFL--GQVAAALAAGNTVIAKP-------AEqtpLIAAEAVKLLHEAGIPKDVLQLLPGDGatVGAALTADPRIA 765
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596450 234 AVGFTGSLKGGRALCDLAAARPQPI-PVFAEMSSINPLVV----LPEalrrrgrQVAEELAASVTLGCGQFC 300
Cdd:PRK11904 766 GVAFTGSTETARIINRTLAARDGPIvPLIAETGGQNAMIVdstaLPE-------QVVDDVVTSAFRSAGQRC 830
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
61-276 |
2.21e-12 |
|
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: 69.06 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 61 QLSATRRAGFLEAIASRLDALGDDFVALVRRETALP--AARIeGERTRTANQLRLFAEvlRRGDFHGVRIDRGQP--GRT 136
Cdd:cd07142 61 RMTGYERSRILLRFADLLEKHADELAALETWDNGKPyeQARY-AEVPLAARLFRYYAG--WADKIHGMTLPADGPhhVYT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 137 PPRPdlrqwrigLGPVAVFGASNFPLAFstAGGDSAAALAAGCPVVVKahgghmaTAECVA-DAILQA--AADSGMPDGV 213
Cdd:cd07142 138 LHEP--------IGVVGQIIPWNFPLLM--FAWKVGPALACGNTIVLK-------PAEQTPlSALLAAklAAEAGLPDGV 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596450 214 FNMV--YGSGVGEALVRHPAIRAVGFTGSLKGGRALCDLaAARPQPIPVFAEMSSINPLVVLPEA 276
Cdd:cd07142 201 LNIVtgFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL-AAKSNLKPVTLELGGKSPFIVCEDA 264
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
107-276 |
2.45e-12 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 69.08 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 107 TANQLRLFAEVLRRgdFHG--VRIDRGQPGRTPPRPdlrqwrigLGPVAVFGASNFP-LAFSTAggdSAAALAAGCPVVV 183
Cdd:PLN02766 125 AAGLLRYYAGAADK--IHGetLKMSRQLQGYTLKEP--------IGVVGHIIPWNFPsTMFFMK---VAPALAAGCTMVV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 184 KAhgghmatAECVADAIL---QAAADSGMPDGVFNMV--YGSGVGEALVRHPAIRAVGFTGSLKGGRALCDlAAARPQPI 258
Cdd:PLN02766 192 KP-------AEQTPLSALfyaHLAKLAGVPDGVINVVtgFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ-AAATSNLK 263
|
170
....*....|....*...
gi 15596450 259 PVFAEMSSINPLVVLPEA 276
Cdd:PLN02766 264 QVSLELGGKSPLLIFDDA 281
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
149-327 |
7.95e-12 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 67.29 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 149 LGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVKAHGGHMATAEcvadAILQAAADSGMPDGVFNMVYGS-GVGEALV 227
Cdd:PRK09457 135 HGVVAVFGPYNFPGHLPN--GHIVPALLAGNTVVFKPSELTPWVAE----LTVKLWQQAGLPAGVLNLVQGGrETGKALA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 228 RHPAIRAVGFTGSLKGGRALCDLAAARPQPIpVFAEMSSINPLVVlpealrrrgRQVAEELAA------SVTLGCGQFCT 301
Cdd:PRK09457 209 AHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-LALEMGGNNPLVI---------DEVADIDAAvhliiqSAFISAGQRCT 278
|
170 180
....*....|....*....|....*.
gi 15596450 302 KPGLVLGLRSPGFDAFVAALGEALAA 327
Cdd:PRK09457 279 CARRLLVPQGAQGDAFLARLVAVAKR 304
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
141-300 |
1.41e-11 |
|
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: 66.77 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 141 DLRQWRIGLGPVAVFGASNFPL--AFSTAggdsAAALAAGCPVVVKAhgghmatAE---CVADAILQAAADSGMPDGVFN 215
Cdd:cd07085 129 DTYSYRQPLGVVAGITPFNFPAmiPLWMF----PMAIACGNTFVLKP-------SErvpGAAMRLAELLQEAGLPDGVLN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 216 MVYGSG-VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEALRrrgRQVAEELAASVTL 294
Cdd:cd07085 198 VVHGGKeAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGK--RVQALGGAKNHAVVMPDADL---EQTANALVGAAFG 272
|
....*.
gi 15596450 295 GCGQFC 300
Cdd:cd07085 273 AAGQRC 278
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
56-275 |
1.48e-11 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 67.27 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETA--LPAAriegertrtanqlrlFAEV------LRrgdFHGVR 127
Cdd:COG4230 606 FPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGktLPDA---------------IAEVreavdfCR---YYAAQ 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 128 IDRGQPGRTPPRPdlrqwrigLGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVKAhgghmatAE------CVADAIL 201
Cdd:COG4230 668 ARRLFAAPTVLRG--------RGVFVCISPWNFPLAIFT--GQVAAALAAGNTVLAKP-------AEqtpliaARAVRLL 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 202 QAAadsGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARP-QPIPVFAEMSSINPLVV----LP 274
Cdd:COG4230 731 HEA---GVPADVLQLLPGDGetVGAALVADPRIAGVAFTGSTETARLINRTLAARDgPIVPLIAETGGQNAMIVdssaLP 807
|
.
gi 15596450 275 E 275
Cdd:COG4230 808 E 808
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
16-324 |
1.90e-11 |
|
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: 66.32 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 16 AAGNLTLRSLDADSGEALPYaFVQATEAEVDAAARAAERAYPHYRQLSATRRAGFLEAIASRLDAlGDDFVALVR----- 90
Cdd:cd07117 12 GSSGETIDSYNPANGETLSE-ITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDE-NKELLAMVEtldng 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 91 ---RETA---LPAAriegertrtANQLRLFAEVLRRGDFHGVRIDRGQPGRTpprpdLRQwriglgPVAVFGAS---NFP 161
Cdd:cd07117 90 kpiRETRavdIPLA---------ADHFRYFAGVIRAEEGSANMIDEDTLSIV-----LRE------PIGVVGQIipwNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 162 laFSTAGGDSAAALAAGCPVVVKAhgghmatAECVADAILQAAA--DSGMPDGVFNMVYGSG--VGEALVRHPAIRAVGF 237
Cdd:cd07117 150 --FLMAAWKLAPALAAGNTVVIKP-------SSTTSLSLLELAKiiQDVLPKGVVNIVTGKGskSGEYLLNHPGLDKLAF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 238 TGSLKGGRALCDLAAARpqPIPVFAEMSSINPLVVLPEA---LRRRGRQVAeelaasVTLGCGQFCTKpGLVLGLRSPGF 314
Cdd:cd07117 221 TGSTEVGRDVAIAAAKK--LIPATLELGGKSANIIFDDAnwdKALEGAQLG------ILFNQGQVCCA-GSRIFVQEGIY 291
|
330
....*....|
gi 15596450 315 DAFVAALGEA 324
Cdd:cd07117 292 DEFVAKLKEK 301
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
146-276 |
2.33e-11 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 66.06 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 146 RIGLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFNMVYGSG-VGE 224
Cdd:PRK13252 140 REPLGVCAGIGAWNYPI--QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEA----GLPDGVFNVVQGDGrVGA 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15596450 225 ALVRHPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEA 276
Cdd:PRK13252 214 WLTEHPDIAKVSFTGGVPTGKKV--MAAAAASLKEVTMELGGKSPLIVFDDA 263
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
56-327 |
3.55e-11 |
|
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: 65.17 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEvlrrgdfHGVRIDRGQPGR 135
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAE-------NAEAFLADEPIE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 136 TPP-------RPdlrqwrigLGPVavFGAS--NFPL--AFSTAggdsAAALAAGCPVVVKahggHmatAECV---ADAIL 201
Cdd:cd07100 85 TDAgkayvryEP--------LGVV--LGIMpwNFPFwqVFRFA----APNLMAGNTVLLK----H---ASNVpgcALAIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 202 QAAADSGMPDGVFNMVY-GSGVGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQpiPVFAEMSSINPLVVLPEA-Lrr 279
Cdd:cd07100 144 ELFREAGFPEGVFQNLLiDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLK--KSVLELGGSDPFIVLDDAdL-- 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15596450 280 rgRQVAEELAASVTLGCGQFCT--KPGLVLglrSPGFDAFVAALGEALAA 327
Cdd:cd07100 220 --DKAVKTAVKGRLQNAGQSCIaaKRFIVH---EDVYDEFLEKFVEAMAA 264
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
133-301 |
7.70e-11 |
|
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: 64.15 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 133 PGRTPP--RPD---LRQWRiGLGPVAVFGASNFPLAfsTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAAADS 207
Cdd:cd07130 113 YGLTIPseRPGhrmMEQWN-PLGVVGVITAFNFPVA--VWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 208 GMPDGVFNMVYGSG-VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARpqpipvFA----EMSSINPLVVLPEA-LRRRG 281
Cdd:cd07130 190 GLPGAIASLVCGGAdVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR------FGrsllELGGNNAIIVMEDAdLDLAV 263
|
170 180
....*....|....*....|
gi 15596450 282 RQVAeeLAASVTlgCGQFCT 301
Cdd:cd07130 264 RAVL--FAAVGT--AGQRCT 279
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
57-275 |
8.35e-11 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 64.89 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 57 PHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGErTRTA-NQLRLFAEVLRRGDfhgvridrgQPGR 135
Cdd:PRK11905 604 PEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE-VREAvDFLRYYAAQARRLL---------NGPG 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 136 TPPRpdlrqwriglGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVK--------AHgghmataecVADAILQAAads 207
Cdd:PRK11905 674 HKPL----------GPVVCISPWNFPLAIFT--GQIAAALVAGNTVLAKpaeqtpliAA---------RAVRLLHEA--- 729
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596450 208 GMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALC-DLAAARPQPIPVFAEMSSINPLVV----LPE 275
Cdd:PRK11905 730 GVPKDALQLLPGDGrtVGAALVADPRIAGVMFTGSTEVARLIQrTLAKRSGPPVPLIAETGGQNAMIVdssaLPE 804
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
51-276 |
1.37e-10 |
|
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: 63.42 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 51 AAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDfhgvriDR 130
Cdd:cd07147 29 AAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIY------GE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 131 GQPGRTPPRPDLRQW---RIGLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVKAhgghmATAECVADAIL-QAAAD 206
Cdd:cd07147 103 VLPLDISARGEGRQGlvrRFPIGPVSAITPFNFPL--NLVAHKVAPAIAAGCPFVLKP-----ASRTPLSALILgEVLAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596450 207 SGMPDGVFNMVYGSGVG-EALVRHPAIRAVGFTGSLKGGRALCDLAAARpqpiPVFAEMSSINPLVVLPEA 276
Cdd:cd07147 176 TGLPKGAFSVLPCSRDDaDLLVTDERIKLLSFTGSPAVGWDLKARAGKK----KVVLELGGNAAVIVDSDA 242
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
130-422 |
1.94e-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: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 130 RGQPGRTPPRPDLRQWRIGLGPVAVFGASNFPLAFSTAGgdSAAALAAGCPVVVKAHGGH---MATAECVADAILQAAAD 206
Cdd:cd07127 175 KPQGKHDPLAMEKTFTVVPRGVALVIGCSTFPTWNGYPG--LFASLATGNPVIVKPHPAAilpLAITVQVAREVLAEAGF 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 207 SgmPDGVFNMVY--GSGVGEALVRHPAIRAVGFTGSLKGGRALcDLAAARPQpipVFAEMSSINPLVVlpEALRRRgRQV 284
Cdd:cd07127 253 D--PNLVTLAADtpEEPIAQTLATRPEVRIIDFTGSNAFGDWL-EANARQAQ---VYTEKAGVNTVVV--DSTDDL-KAM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 285 AEELAASVTLGCGQFCTKPGLVL----GLRSP----GFDAFVAALGEA---LAARPAQSMLNAGTLRSYvEGLQRLERHP 353
Cdd:cd07127 324 LRNLAFSLSLYSGQMCTTPQNIYvprdGIQTDdgrkSFDEVAADLAAAidgLLADPARAAALLGAIQSP-DTLARIAEAR 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596450 354 GIRRLAGAPQEgrQAHPQLFKADV------GLLLEGDELLQEEVFGPATVVVEAADEE---QLARALDNLHGQLSATL 422
Cdd:cd07127 403 QLGEVLLASEA--VAHPEFPDARVrtplllKLDASDEAAYAEERFGPIAFVVATDSTDhsiELARESVREHGAMTVGV 478
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
71-327 |
2.31e-10 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 62.45 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 71 LEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDFHGVRIDRgqpgrtpPRPDLRQWRIGLG 150
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDR-------PGENILLFKRALG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 151 PVAVFGASNFPlaFSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFNMVYGSG--VGEALVR 228
Cdd:PRK10090 74 VTTGILPWNFP--FFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGRGetVGQELAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 229 HPAIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVVLPEAlrrrGRQVA-EELAASVTLGCGQFCTKPGLVL 307
Cdd:PRK10090 148 NPKVAMVSMTGSVSAGEKI--MAAAAKNITKVCLELGGKAPAIVMDDA----DLDLAvKAIVDSRVINSGQVCNCAERVY 221
|
250 260
....*....|....*....|
gi 15596450 308 GLRSPgFDAFVAALGEALAA 327
Cdd:PRK10090 222 VQKGI-YDQFVNRLGEAMQA 240
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
21-327 |
5.28e-10 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 61.68 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 21 TLRSLDADSGEALPYAFVQAteaevdaaaraaERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARI 100
Cdd:PRK09406 13 TVKTFTALTDDEVDAAIARA------------HARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 101 EGERTRTANQLRLFAEvlrrgdfHGVRIDRGQP------------GRTPPrpdlrqwrigLGPVAVFGASNFPLAfsTAG 168
Cdd:PRK09406 81 KAEALKCAKGFRYYAE-------HAEALLADEPadaaavgasrayVRYQP----------LGVVLAVMPWNFPLW--QVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 169 GDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVF-NMVYGSGVGEALVRHPAIRAVGFTGSLKGGRAL 247
Cdd:PRK09406 142 RFAAPALMAGNVGLLKHASNVPQTALYLADLFRRA----GFPDGCFqTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 248 CDLAAARPQPIPVfaEMSSINPLVVLPEAlrrrgrQVAEELAASVTLGC---GQFC--TKPGLVlglRSPGFDAFVAALG 322
Cdd:PRK09406 218 AAIAGDEIKKTVL--ELGGSDPFIVMPSA------DLDRAAETAVTARVqnnGQSCiaAKRFIV---HADVYDAFAEKFV 286
|
....*
gi 15596450 323 EALAA 327
Cdd:PRK09406 287 ARMAA 291
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
143-276 |
1.12e-09 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 60.66 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 143 RQWRIGLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFNMVYGSG- 221
Cdd:PRK09407 149 TELRQPKGVVGVISPWNYPL--TLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEA----GLPRDLWQVVTGPGp 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596450 222 -VGEALVRHpaIRAVGFTGSLKGGRALCDLAAARpqPIPVFAEMSSINPLVVLPEA 276
Cdd:PRK09407 223 vVGTALVDN--ADYLMFTGSTATGRVLAEQAGRR--LIGFSLELGGKNPMIVLDDA 274
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
151-420 |
2.09e-09 |
|
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: 59.85 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 151 PVAVFGAS---NFPLAFSTagGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFNMV--YGSGVGEA 225
Cdd:cd07143 144 PIGVCGQIipwNFPLLMCA--WKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVVsgYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 226 LVRHPAIRAVGFTGSLKGGRALCDlAAARPQPIPVFAEMSSINPLVVLPEAlrrRGRQVAEELAASVTLGCGQFCTKPGL 305
Cdd:cd07143 218 ISSHMDIDKVAFTGSTLVGRKVME-AAAKSNLKKVTLELGGKSPNIVFDDA---DLESAVVWTAYGIFFNHGQVCCAGSR 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 306 VLgLRSPGFDAFVAAL-------------GEALAARPAQSMLNAGTLRSYVEGlqrlERHPGIRRLAGAPQEGRQAH--- 369
Cdd:cd07143 294 IY-VQEGIYDKFVKRFkekakklkvgdpfAEDTFQGPQVSQIQYERIMSYIES----GKAEGATVETGGKRHGNEGYfie 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15596450 370 PQLFkADVgllLEGDELLQEEVFGPATVVVEAADEEQ-LARALDNLHGQLSA 420
Cdd:cd07143 369 PTIF-TDV---TEDMKIVKEEIFGPVVAVIKFKTEEEaIKRANDSTYGLAAA 416
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
149-327 |
2.55e-09 |
|
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: 59.46 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 149 LGPVAVFGASNFP--LAFSTAggdsAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsgMPDGVFNMVYGSG-VGEA 225
Cdd:cd07087 101 LGVVLIIGPWNYPlqLALAPL----IGAIAAGNTVVLKPSELAPATSALLAKLIPKY-----FDPEAVAVVEGGVeVATA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 226 LVRHP---AIravgFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVV-----LPEALRRrgrqvaeeLAASVTLGCG 297
Cdd:cd07087 172 LLAEPfdhIF----FTGSPAVGKIV--MEAAAKHLTPVTLELGGKSPCIVdkdanLEVAARR--------IAWGKFLNAG 237
|
170 180 190
....*....|....*....|....*....|
gi 15596450 298 QFCTKPGLVLGLRSPgFDAFVAALGEALAA 327
Cdd:cd07087 238 QTCIAPDYVLVHESI-KDELIEELKKAIKE 266
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
24-276 |
1.21e-08 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 57.18 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 24 SLDADSGEALPyAFVQATEAEVDAAARAAERAYPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGE 103
Cdd:PRK13968 11 SVNPATGEQLS-VLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 104 RTRTANQLRLFAEvlrrgdfHGVRIDRGQPGRTPPRPDLRQWRiGLGPVAVFGASNFPLAFSTAGgdSAAALAAGCPVVV 183
Cdd:PRK13968 90 VAKSANLCDWYAE-------HGPAMLKAEPTLVENQQAVIEYR-PLGTILAIMPWNFPLWQVMRG--AVPILLAGNGYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 184 KahggHMATAECVADAILQAAADSGMPDGVFNMVYGSGVG-EALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVfa 262
Cdd:PRK13968 160 K----HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGvSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVL-- 233
|
250
....*....|....
gi 15596450 263 EMSSINPLVVLPEA 276
Cdd:PRK13968 234 ELGGSDPFIVLNDA 247
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
151-486 |
1.24e-08 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 57.21 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 151 PVAVFGAS---NFPLAFstAGGDSAAALAAGCPVVVKAHGGHMATAECVAdailQAAADSGMPDGVFNMV--YGSGVGEA 225
Cdd:PRK09847 157 PVGVIAAIvpwNFPLLL--TCWKLGPALAAGNSVILKPSEKSPLSAIRLA----GLAKEAGLPDGVLNVVtgFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 226 LVRHPAIRAVGFTGSLKGGRALCD-----------LAAARPQPIPVFAEMSSINplvvlpealrrrgrQVAEELAASVTL 294
Cdd:PRK09847 231 LSRHNDIDAIAFTGSTRTGKQLLKdagdsnmkrvwLEAGGKSANIVFADCPDLQ--------------QAASATAAGIFY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 295 GCGQFCTKpGLVLGLRSPGFDAFVAAL-GEALAARPAQSMLNAGTLRSYVEGLQRLERHPGIRRLAGAPQ---EGR-QAH 369
Cdd:PRK09847 297 NQGQVCIA-GTRLLLEESIADEFLALLkQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQlllDGRnAGL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 370 PQLFKADVGLLL-EGDELLQEEVFGPATVVVEAADEEQ-LARALDNLHGQLSATLigeADDLAAFAGLVPLLerKAGRLL 447
Cdd:PRK09847 376 AAAIGPTIFVDVdPNASLSREEIFGPVLVVTRFTSEEQaLQLANDSQYGLGAAVW---TRDLSRAHRMSRRL--KAGSVF 450
|
330 340 350
....*....|....*....|....*....|....*....
gi 15596450 448 FNGYPTGvevcDAMVHGGPYPATSDARGTSVGtlAIERF 486
Cdd:PRK09847 451 VNNYNDG----DMTVPFGGYKQSGNGRDKSLH--ALEKF 483
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
130-412 |
3.60e-08 |
|
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: 56.05 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 130 RGQPGRTPPRP--DLRQWRIGLGPVAVFGASNFPLAFstAGGDSAAALAAGCPVVVKAhgghMATAECVADAILQAAADS 207
Cdd:cd07083 134 RYPAVEVVPYPgeDNESFYVGLGAGVVISPWNFPVAI--FTGMIVAPVAVGNTVIAKP----AEDAVVVGYKVFEIFHEA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 208 GMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGG----RALCDLAAARPQPIPVFAEMSSINPLVVLPEAlrrRG 281
Cdd:cd07083 208 GFPPGVVQFLPGVGeeVGAYLTEHERIRGINFTGSLETGkkiyEAAARLAPGQTWFKRLYVETGGKNAIIVDETA---DF 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 282 RQVAEELAASVTLGCGQFCTKPGLVL---GLRSPGFDAFVAALGEALAARPAQSMLNAG---------TLRSYVE-GLQR 348
Cdd:cd07083 285 ELVVEGVVVSAFGFQGQKCSAASRLIltqGAYEPVLERLLKRAERLSVGPPEENGTDLGpvidaeqeaKVLSYIEhGKNE 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596450 349 LERHPGIRRLAGapqEGRQAHPQLFKADvgllLEGDELLQEEVFGPATVVVEAADEEqLARALD 412
Cdd:cd07083 365 GQLVLGGKRLEG---EGYFVAPTVVEEV----PPKARIAQEEIFGPVLSVIRYKDDD-FAEALE 420
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
149-252 |
3.74e-08 |
|
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: 55.96 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 149 LGPVAVFGASNFPLAFstAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsGMPDGVFNMVYGSG--VGEAL 226
Cdd:cd07140 148 IGVCGIVIPWNYPLMM--LAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKA----GFPKGVINILPGSGslVGQRL 221
|
90 100
....*....|....*....|....*.
gi 15596450 227 VRHPAIRAVGFTGSLKGGRALCDLAA 252
Cdd:cd07140 222 SDHPDVRKLGFTGSTPIGKHIMKSCA 247
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
151-276 |
1.82e-07 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 53.66 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 151 PVAVFGAS---NFPL-AFSTAGGdsaAALAAGCPVVVKahgghmaTAECVADAILQAAA---DSGMPDGVFNMV--YGSG 221
Cdd:PLN02466 195 PIGVAGQIipwNFPLlMFAWKVG---PALACGNTIVLK-------TAEQTPLSALYAAKllhEAGLPPGVLNVVsgFGPT 264
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15596450 222 VGEALVRHPAIRAVGFTGSLKGGRALCDLaAARPQPIPVFAEMSSINPLVVLPEA 276
Cdd:PLN02466 265 AGAALASHMDVDKLAFTGSTDTGKIVLEL-AAKSNLKPVTLELGGKSPFIVCEDA 318
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
149-325 |
1.13e-06 |
|
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: 51.07 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 149 LGPVAVFGASNFP--LAFSTAggdsAAALAAGCPVVVKAHGGHMATAECVADAILQAaadsgMPDGVFNMVYGsGVGE-- 224
Cdd:cd07135 109 LGVVLIIGPWNYPvlLALSPL----VGAIAAGCTVVLKPSELTPHTAALLAELVPKY-----LDPDAFQVVQG-GVPEtt 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 225 ALVRHPaIRAVGFTGSLKGGRALCdlAAARPQPIPVFAEMSSINPLVV-----LPEALRRrgrqvaeeLAASVTLGCGQF 299
Cdd:cd07135 179 ALLEQK-FDKIFYTGSGRVGRIIA--EAAAKHLTPVTLELGGKSPVIVtknadLELAAKR--------ILWGKFGNAGQI 247
|
170 180
....*....|....*....|....*.
gi 15596450 300 CTKPGLVLGLRSPgFDAFVAALGEAL 325
Cdd:cd07135 248 CVAPDYVLVDPSV-YDEFVEELKKVL 272
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
149-327 |
5.40e-06 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 48.87 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 149 LGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAIlqaaaDSGMPDGVFNMVYG-SGVGEALV 227
Cdd:PTZ00381 110 LGVVLVIGAWNYPL--NLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-----TKYLDPSYVRVIEGgVEVTTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 228 RHPaIRAVGFTGSLKGGRALcdLAAARPQPIPVFAEMSSINPLVV-----LPEALRRrgrqvaeeLAASVTLGCGQFCTK 302
Cdd:PTZ00381 183 KEP-FDHIFFTGSPRVGKLV--MQAAAENLTPCTLELGGKSPVIVdkscnLKVAARR--------IAWGKFLNAGQTCVA 251
|
170 180
....*....|....*....|....*
gi 15596450 303 PGLVLGLRSPgFDAFVAALGEALAA 327
Cdd:PTZ00381 252 PDYVLVHRSI-KDKFIEALKEAIKE 275
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
57-447 |
8.38e-06 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 48.55 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 57 PHYRQLSATRRAGFLEAIASRLDALGDDFVAL-------VRRETALPaarIEGERTRTANQLRLFAEVlrrGDFHGVRI- 128
Cdd:PRK11903 55 AALRALTYAQRAALLAAIVKVLQANRDAYYDIatansgtTRNDSAVD---IDGGIFTLGYYAKLGAAL---GDARLLRDg 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 129 DRGQPGRTPprpdLRQWRIGLGP---VAVF-GASNFPlafstAGG---DSAAALAAGCPVVVK-AHGGHMATAECVADAI 200
Cdd:PRK11903 129 EAVQLGKDP----AFQGQHVLVPtrgVALFiNAFNFP-----AWGlweKAAPALLAGVPVIVKpATATAWLTQRMVKDVV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 201 lqaaaDSG-MPDGVFNMVYGSGVGeaLVRH-PAIRAVGFTGSLKGGRALCDLAAARPQPIPVFAEMSSINPLVVLP---- 274
Cdd:PRK11903 200 -----AAGiLPAGALSVVCGSSAG--LLDHlQPFDVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADSLNSALLGPdaap 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 275 --EALRRRGRQVAEELaasvTLGCGQFCTKPGLVL---GLRSPGFDAFVAALGEALAARPAQ------SMLNAGTLRSYV 343
Cdd:PRK11903 273 gsEAFDLFVKEVVREM----TVKSGQKCTAIRRIFvpeALYDAVAEALAARLAKTTVGNPRNdgvrmgPLVSRAQLAAVR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 344 EGLQRLERHP------GIRRLAGA-PQEGRQAHPQLFKADvgLLLEGDELLQEEVFGPATVVVEAADEEQLARALDNLHG 416
Cdd:PRK11903 349 AGLAALRAQAevlfdgGGFALVDAdPAVAACVGPTLLGAS--DPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQG 426
|
410 420 430
....*....|....*....|....*....|.
gi 15596450 417 QLSATLIGeaDDLAAFAGLVPLLERKAGRLL 447
Cdd:PRK11903 427 SLVASVYS--DDAAFLAAAALELADSHGRVH 455
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
149-300 |
1.11e-05 |
|
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: 48.06 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 149 LGPVAVFGASNFPlaFSTAGGDSAAALAAGCPVVVKAhGGHMATAECVADAILQAA-ADSGMPDGVFNMVYGSG-VGEAL 226
Cdd:cd07098 121 LGVVGAIVSWNYP--FHNLLGPIIAALFAGNAIVVKV-SEQVAWSSGFFLSIIREClAACGHDPDLVQLVTCLPeTAEAL 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596450 227 VRHPAIRAVGFTGSLKGGRALCdlAAARPQPIPVFAEMSSINPLVVLPEAlrrRGRQVAEELAASVTLGCGQFC 300
Cdd:cd07098 198 TSHPVIDHITFIGSPPVGKKVM--AAAAESLTPVVLELGGKDPAIVLDDA---DLDQIASIIMRGTFQSSGQNC 266
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
57-416 |
1.82e-05 |
|
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: 47.06 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 57 PHYRQLSATRRAGFLEAIASRLDAlGDDFVALVR--------RETA---LPAAriegertrtANQLRLFAEVLRRGDFHG 125
Cdd:cd07116 52 EAWGKTSVAERANILNKIADRMEA-NLEMLAVAEtwdngkpvRETLaadIPLA---------IDHFRYFAGCIRAQEGSI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 126 VRIDRGQPGRTPPRPdlrqwrigLGPVAVFGASNFPLAFSTagGDSAAALAAGCPVVVKAHGGHMAT----AECVADAIl 201
Cdd:cd07116 122 SEIDENTVAYHFHEP--------LGVVGQIIPWNFPLLMAT--WKLAPALAAGNCVVLKPAEQTPASilvlMELIGDLL- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 202 qaaadsgmPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGSLKGGRALCDLAAArpQPIPVFAEMSSINPLVVLPEALRR 279
Cdd:cd07116 191 --------PPGVVNVVNGFGleAGKPLASSKRIAKVAFTGETTTGRLIMQYASE--NIIPVTLELGGKSPNIFFADVMDA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 280 RGRQV--AEELAASVTLGCGQFCTKPGLVLgLRSPGFDAFVAALGEALAARPAQSMLNAGTLRSYVEGLQRLE------- 350
Cdd:cd07116 261 DDAFFdkALEGFVMFALNQGEVCTCPSRAL-IQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEkilsyid 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596450 351 --RHPGIRRLAG--APQEGRQAHPQLFKADVGLLLEGDELLQEEVFGPATVVVEAADEEQ-LARALDNLHG 416
Cdd:cd07116 340 igKEEGAEVLTGgeRNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFKDEEEaLEIANDTLYG 410
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
62-244 |
4.96e-05 |
|
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: 45.87 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 62 LSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLrrGDFHGVRIDRGQpgrTPPRPD 141
Cdd:cd07148 41 LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADEL--GQLGGREIPMGL---TPASAG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 142 LRQW--RIGLGPVAVFGASNFPLafSTAGGDSAAALAAGCPVVVK-AHGGHMATAECVadAILQAAadsGMPDGVFNMVY 218
Cdd:cd07148 116 RIAFttREPIGVVVAISAFNHPL--NLIVHQVAPAIAAGCPVIVKpALATPLSCLAFV--DLLHEA---GLPEGWCQAVP 188
|
170 180
....*....|....*....|....*..
gi 15596450 219 -GSGVGEALVRHPAIRAVGFTGSLKGG 244
Cdd:cd07148 189 cENAVAEKLVTDPRVAFFSFIGSARVG 215
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
56-526 |
6.42e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.02 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 56 YPHYRQLSATRRAGFLEAIASRLDALGDDFVALVRRETALPAARIEGERTRTANQLRLFAEVLRRGDFHGVRIDRGQPGR 135
Cdd:COG3321 866 YPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLAL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 136 TPPRPDLRQWRIGLGPVAVFGASNFPLAFSTAGGDSAAALAAGCPVVVKAHGGHMATAECVADAILQAAADSGMPDGVFN 215
Cdd:COG3321 946 AAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALA 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 216 MVYGSGVGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPVFAEMSSINPLVVLPEALRRRGRQVAEELAASVTLG 295
Cdd:COG3321 1026 ALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAA 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 296 CGQFCTKPGLVLGLRSPGFDAFVAALGEALAARPAQSMLNAGTLRSYVEGLQRLERHPGIRRLAGAPQEGRQAHPQLFKA 375
Cdd:COG3321 1106 LLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAAL 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 376 DVGLLLEGDELLQEEVFGPATVVVEAADEEQLARALDNLHGQLSATLIGEADDLAAFAGLVPLLERKAGRLLFNGYPTGV 455
Cdd:COG3321 1186 AAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALL 1265
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596450 456 EVCDAMVHGGPYPATSDARGTSVGTLAIERFLRPLCYQDYPDSLLPDALKNANPLGLLRLVDGRSTREALD 526
Cdd:COG3321 1266 AAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAA 1336
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
146-326 |
6.90e-05 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 45.52 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 146 RIGLGPVAVFGASNFP--LAFSTAggdsAAALAAGCPVVVKAhgghmATAECVAD-AILQAAADSGMPDGVFNMVYGSG- 221
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPvnLAVSKI----APALIAGNAVVLKP-----PTQGAVAAlHMVHCFHLAGFPKGLISCVTGKGs 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 222 -VGEALVRHPAIRAVGFTGSlKGGRALCDLAAArpqpIPVFAEMSSINPLVVLPEAlrrrgrqvAEELAASVTLG----- 295
Cdd:PLN00412 227 eIGDFLTMHPGVNCISFTGG-DTGIAISKKAGM----VPLQMELGGKDACIVLEDA--------DLDLAAANIIKggfsy 293
|
170 180 190
....*....|....*....|....*....|.
gi 15596450 296 CGQFCTKPGLVLGLRSPGfDAFVAALGEALA 326
Cdd:PLN00412 294 SGQRCTAVKVVLVMESVA-DALVEKVNAKVA 323
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
197-276 |
1.99e-04 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 43.97 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596450 197 ADAIL-QAAADSGMPDGVFNMVYGSG-VGEALVRHPAIRAVGFTGSLKGGRALCDLAAARPQPIPvfAEMSSINPLVVLP 274
Cdd:PLN02419 291 ASVILaELAMEAGLPDGVLNIVHGTNdTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQ--SNMGAKNHGLVLP 368
|
..
gi 15596450 275 EA 276
Cdd:PLN02419 369 DA 370
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
200-240 |
2.95e-04 |
|
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: 43.34 E-value: 2.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15596450 200 ILQAAadsGMPDGVFNMVYGSG--VGEALVRHPAIRAVGFTGS 240
Cdd:cd07123 218 ILEEA---GLPPGVINFVPGDGpvVGDTVLASPHLAGLHFTGS 257
|
|
| |
