|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
62-499 |
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: 629.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILRGDTFAARIDTALADRQPL 141
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREGSWLDARIDPADPDRQPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 142 PRPDLRQYQQALGPVAVFGASNFPLAFSTAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAVVRCGLPGGVFNMI 221
Cdd:cd07129 95 PRPDLRRMLVPLGPVAVFGASNFPLAFSVAGGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGLPAGVFSLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 222 FGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLFAEMSAINPLIILPQALQTRAEALANELVASFTLG 299
Cdd:cd07129 175 QGGgrEVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIPFYAELGSVNPVFILPGALAERGEAIAQGFVGSLTLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 300 GGQFCTRPGLILALRGAGLERFKSALCAAVAGSTPQVLLNAPTLQHYRQGVAALAVHPRIEKLASG-IAAGAGQAQTLLW 378
Cdd:cd07129 255 AGQFCTNPGLVLVPAGPAGDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEALAAAPGVRVLAGGaAAEGGNQAAPTLF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 379 QAQVEDLLAqDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLHAEADDGPLAASLLPLLCEKAGRVLFNGYPT 458
Cdd:cd07129 335 KVDAAAFLA-DPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDDLALARELLPVLERKAGRLLFNGWPT 413
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 915779292 459 GVEVCDAMVHGGPWPATTDARGTSVGSRAIERFLRPVCLQN 499
Cdd:cd07129 414 GVEVCPAMVHGGPYPATTDPRFTSVGTAAIERFLRPVCYQN 454
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
68-498 |
1.87e-59 |
|
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: 203.24 E-value: 1.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 68 QQRAHFLCAIADELDALGEPFFAIAGQETALPlARLQGERARTSGQLRMFADVILRGDTFAARIDTaladRQPLPRPDLR 147
Cdd:cd07084 21 PKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVIYSYRIPHEPGNH----LGQGLKQQSH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 148 QYQQALGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAVVrcgLPGGVFNMI-FGTDI 226
Cdd:cd07084 96 GYRWPYGPVLVIGAFNFPL--WIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LPPEDVTLInGDGKT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 227 GAELVRHPAIQAVGFTGSLAGGKALYQLAQQrpqpIPLFAEMSAINPLIILPQALQTraEALANELVASFTLGGGQFCTR 306
Cdd:cd07084 171 MQALLLHPNPKMVLFTGSSRVAEKLALDAKQ----ARIYLELAGFNWKVLGPDAQAV--DYVAWQCVQDMTACSGQKCTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 307 PGLILALRGAGLERFKSALCAAVAGSTPQVLLNAPTLQ-HYRQGVAALAVHPRIEKLASGIAA---------GAGQAQTL 376
Cdd:cd07084 245 QSMLFVPENWSKTPLVEKLKALLARRKLEDLLLGPVQTfTTLAMIAHMENLLGSVLLFSGKELknhsipsiyGACVASAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 377 LwqAQVEDLLAQDTLLQTEVFGPLSLLVEVDD--VAQLQAVVKALQGQLTATLHAEADdgpLAASLLPLLCEKAGRVLFN 454
Cdd:cd07084 325 F--VPIDEILKTYELVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSNDP---IFLQELIGNLWVAGRTYAI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 915779292 455 GY-PTGVEVcdAMVHGGPWPAttDARGTSVG-SRAIERFLRPVCLQ 498
Cdd:cd07084 400 LRgRTGVAP--NQNHGGGPAA--DPRGAGIGgPEAIKLVWRCHAEQ 441
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
57-494 |
2.00e-45 |
|
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: 165.07 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 57 QAFAVYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILR--GDTFAAridta 134
Cdd:cd07078 9 AAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRlhGEVIPS----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 135 ladrqPLPRPDLRQYQQALGPVAVFGASNFPLAFstAGGDTASALAAGCPVVVKAHPghmaTAELTAEAIVRAVVRCGLP 214
Cdd:cd07078 84 -----PDPGELAIVRREPLGVVGAITPWNFPLLL--AAWKLAPALAAGNTVVLKPSE----LTPLTALLLAELLAEAGLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 215 GGVFNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRpqPIPLFAEMSAINPLIILPQAlqtRAEALANEL 292
Cdd:cd07078 153 PGVLNVVtgDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEN--LKRVTLELGGKSPLIVFDDA---DLDAAVKGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 293 VASFTLGGGQFCTRPGLILALRGAgLERFKSALCAAVAGSTPQVLLNAPTLqhyrqgVAALAVHPRIEKLASGIAAGAGQ 372
Cdd:cd07078 228 VFGAFGNAGQVCTAASRLLVHESI-YDEFVERLVERVKALKVGNPLDPDTD------MGPLISAAQLDRVLAYIEDAKAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 373 AQTLLWQAQ--------------VEDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLHAEaDDGPLAA 438
Cdd:cd07078 301 GAKLLCGGKrleggkgyfvpptvLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTR-DLERALR 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 915779292 439 SLLPLlceKAGRVLFNGYPTGVEvcDAMVHGGpWPATTDARGTsvGSRAIERFLRP 494
Cdd:cd07078 380 VAERL---EAGTVWINDYSVGAE--PSAPFGG-VKQSGIGREG--GPYGLEEYTEP 427
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
62-494 |
7.48e-41 |
|
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: 151.23 E-value: 7.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVI--LRGDTFAAridtaladrq 139
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLAdkLGGPELPS---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 140 PLPRPDLRQYQQALGPVAVFGASNFPLAFstAGGDTASALAAGCPVVVKAHPghmaTAELTAEAIVRAVVRCGLPGGVFN 219
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLL--AAWKLAPALAAGNTVVLKPSE----LTPLTALALAELLQEAGLPPGVVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 220 MI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRpqPIPLFAEMSAINPLIILPQALQtraEALANELVASFT 297
Cdd:cd06534 154 VVpgGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAEN--LKPVTLELGGKSPVIVDEDADL---DAAVEGAVFGAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 298 LGGGQFCTRPGLILALRGAgLERFKSALCAAVAGSTPqvllnaptlqhyrqgvaalavhprieklasgiaagagqaqtll 377
Cdd:cd06534 229 FNAGQICTAASRLLVHESI-YDEFVEKLVTVLVDVDP------------------------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 378 wqaqvedllaQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLHAEaDDGPLAASLLPLlceKAGRVLFNGYP 457
Cdd:cd06534 265 ----------DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTR-DLNRALRVAERL---RAGTVYINDSS 330
|
410 420 430
....*....|....*....|....*....|....*..
gi 915779292 458 TGVEvcDAMVHGGPWPAttdARGTSVGSRAIERFLRP 494
Cdd:cd06534 331 IGVG--PEAPFGGVKNS---GIGREGGPYGLEEYTRT 362
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
10-494 |
2.78e-40 |
|
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: 151.82 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 10 RQFIAGRRI-ASGEATLLSLRAVDGEATGhRFYPASREEAALAAEAAQQAFAVYSQTTPQQRAHFLCAIADELDALGEPF 88
Cdd:COG1012 7 PLFIGGEWVaAASGETFDVINPATGEVLA-RVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 89 FAIAGQETALPLARLQGERARTSGQLRMFADVILRgdtfaaridtALADRQPLPRPDLRQY--QQALGPVAVFGASNFPL 166
Cdd:COG1012 86 AALLTLETGKPLAEARGEVDRAADFLRYYAGEARR----------LYGETIPSDAPGTRAYvrREPLGVVGAITPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 167 AfsTAGGDTASALAAGCPVVVKAHPghmaTAELTAEAIVRAVVRCGLPGGVFNMIFGT--DIGAELVRHPAIQAVGFTGS 244
Cdd:COG1012 156 A--LAAWKLAPALAAGNTVVLKPAE----QTPLSALLLAELLEEAGLPAGVLNVVTGDgsEVGAALVAHPDVDKISFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 245 LAGGKALYQLAQQRpqPIPLFAEMSAINPLIILPQAlqtRAEALANELVASFTLGGGQFCTRPGLILALRGAgLERFKSA 324
Cdd:COG1012 230 TAVGRRIAAAAAEN--LKRVTLELGGKNPAIVLDDA---DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESI-YDEFVER 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 325 LCAAVA------GSTPQVLLNAptLQHYRQgvaalavHPRIEKL-ASGIAAGA-----GQAQ----------TLLwqaqv 382
Cdd:COG1012 304 LVAAAKalkvgdPLDPGTDMGP--LISEAQ-------LERVLAYiEDAVAEGAelltgGRRPdgeggyfvepTVL----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 383 EDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLHAEadDGPLAASLLPLLceKAGRVLFNGYPTGVEv 462
Cdd:COG1012 370 ADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTR--DLARARRVARRL--EAGMVWINDGTTGAV- 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 915779292 463 cDAMVHGGPwpattdaRGTSVG----SRAIERFLRP 494
Cdd:COG1012 445 -PQAPFGGV-------KQSGIGreggREGLEEYTET 472
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
57-470 |
1.34e-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: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 57 QAFAVYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVI--LRGDTFAARID-T 133
Cdd:pfam00171 40 AAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLArrLDGETLPSDPGrL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 134 ALADRQPlprpdlrqyqqaLGPVAVFGASNFPLAfsTAGGDTASALAAGCPVVVKAHPghmaTAELTAEAIVRAVVRCGL 213
Cdd:pfam00171 120 AYTRREP------------LGVVGAITPWNFPLL--LPAWKIAPALAAGNTVVLKPSE----LTPLTALLLAELFEEAGL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 214 PGGVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALANE 291
Cdd:pfam00171 182 PAGVLNVVTGSgaEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTL--ELGGKNPLIVLEDA---DLDAAVEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 292 LVASFTLGGGQFCTRPGLILALRGAgLERFKSALCAAVAgstpQVLLNAPTLQHYRQGvaALAVHPRIEKLAS----GIA 367
Cdd:pfam00171 257 AVFGAFGNAGQVCTATSRLLVHESI-YDEFVEKLVEAAK----KLKVGDPLDPDTDMG--PLISKAQLERVLKyvedAKE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 368 AGA-----GQAQ---------TLLWqaqveDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLHAEaDD 433
Cdd:pfam00171 330 EGAklltgGEAGldngyfvepTVLA-----NVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTS-DL 403
|
410 420 430
....*....|....*....|....*....|....*..
gi 915779292 434 GPLAASLLPLlceKAGRVLFNGYPTGVEvcDAMVHGG 470
Cdd:pfam00171 404 ERALRVARRL---EAGMVWINDYTTGDA--DGLPFGG 435
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
62-408 |
1.73e-30 |
|
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: 124.28 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILR--GDTFAARidtaladrq 139
Cdd:cd07097 53 WRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRlsGETLPST--------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 140 plpRPDLRQY--QQALGPVAVFGASNFPLAfsTAGGDTASALAAGCPVVVKAHpghmATAELTAEAIVRAVVRCGLPGGV 217
Cdd:cd07097 124 ---RPGVEVEttREPLGVVGLITPWNFPIA--IPAWKIAPALAYGNTVVFKPA----ELTPASAWALVEILEEAGLPAGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 218 FNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAEALAnelVAS 295
Cdd:cd07097 195 FNLVMGSgsEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQL--EMGGKNPLVVLDDADLDLAVECA---VQG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 296 FTLGGGQFCTRPGLILALRGAGlERFKSALCAAVAGSTPQVLLNAPTlqhyrqGVAALAVHPRIEKLASGIAAGAGQAQT 375
Cdd:cd07097 270 AFFSTGQRCTASSRLIVTEGIH-DRFVEALVERTKALKVGDALDEGV------DIGPVVSERQLEKDLRYIEIARSEGAK 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 915779292 376 LLWQAQ---------------VEDLLAQDTLLQTEVFGPLSLLVEVDD 408
Cdd:cd07097 343 LVYGGErlkrpdegyylapalFAGVTNDMRIAREEIFGPVAAVIRVRD 390
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
59-411 |
6.64e-27 |
|
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: 113.30 E-value: 6.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 59 FAVYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILR--GDTFaaridtala 136
Cdd:cd07103 32 FKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARRiyGRTI--------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 137 drqPLPRPDLRQ--YQQALGPVAVFGASNFPLAFST--AGGdtasALAAGCPVVVKAhpghmatAE---LTAEAIVRAVV 209
Cdd:cd07103 103 ---PSPAPGKRIlvIKQPVGVVAAITPWNFPAAMITrkIAP----ALAAGCTVVLKP-------AEetpLSALALAELAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 210 RCGLPGGVFNMIFGTD--IGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEA 287
Cdd:cd07103 169 EAGLPAGVLNVVTGSPaeIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSL--ELGGNAPFIVFDDA---DLDK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 288 LANELVASFTLGGGQFCTRPGLILALRGAgLERFKSALCAAVA------GSTPQV----LLNAPTLqhyrQGVAALaVHP 357
Cdd:cd07103 244 AVDGAIASKFRNAGQTCVCANRIYVHESI-YDEFVEKLVERVKklkvgnGLDEGTdmgpLINERAV----EKVEAL-VED 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915779292 358 RIEKLASGIAAGAGQAQ-------TLLWQAQVEDLLAQDtllqtEVFGPLSLLVEVDDVAQ 411
Cdd:cd07103 318 AVAKGAKVLTGGKRLGLggyfyepTVLTDVTDDMLIMNE-----ETFGPVAPIIPFDTEDE 373
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
63-331 |
1.04e-23 |
|
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: 104.19 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 63 SQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQ-GERARTSGQLRMFADVIlRGDTFAARidtaladRQPL 141
Cdd:cd07139 55 PRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRrAQGPGPAALLRYYAALA-RDFPFEER-------RPGS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 142 PRPDLRQYQQALGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAvvrcGLPGGVFNMI 221
Cdd:cd07139 127 GGGHVLVRREPVGVVAAIVPWNAPL--FLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEA----GLPPGVVNVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 222 -FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALqtrAEALANELVASFTLGG 300
Cdd:cd07139 201 pADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTL--ELGGKSAAIVLDDAD---LDAAVPGLVPASLMNN 275
|
250 260 270
....*....|....*....|....*....|.
gi 915779292 301 GQFCTRPGLILALRgAGLERFKSALCAAVAG 331
Cdd:cd07139 276 GQVCVALTRILVPR-SRYDEVVEALAAAVAA 305
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
55-305 |
1.40e-23 |
|
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: 103.41 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 55 AQQAFAVYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQ-LRMFADVIL--RGDTFAARI 131
Cdd:cd07093 28 AKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAAnFRFFADYILqlDGESYPQDG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 132 DT-ALADRQPlprpdlrqyqqaLGPVAVFGASNFPLAFSTAggDTASALAAGCPVVVKahPGHMA--TAELTAEAIVRAv 208
Cdd:cd07093 108 GAlNYVLRQP------------VGVAGLITPWNLPLMLLTW--KIAPALAFGNTVVLK--PSEWTplTAWLLAELANEA- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 209 vrcGLPGGVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQqrPQPIPLFAEMSAINPLIILPQAlqTRAE 286
Cdd:cd07093 171 ---GLPPGVVNVVHGFgpEAGAALVAHPDVDLISFTGETATGRTIMRAAA--PNLKPVSLELGGKNPNIVFADA--DLDR 243
|
250
....*....|....*....
gi 915779292 287 ALANELVASFTLgGGQFCT 305
Cdd:cd07093 244 AVDAAVRSSFSN-NGEVCL 261
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
63-416 |
4.63e-22 |
|
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: 98.97 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 63 SQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILR--GDTFAARIDTALADRQ- 139
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRddGESFSCDLTANGKARKi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 140 -PLPRPdlrqyqqaLGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKahPGHMATaeLTAEAIVRAVVRCGLPGGVF 218
Cdd:cd07146 115 fTLREP--------LGVVLAITPFNHPL--NQVAHKIAPAIAANNRIVLK--PSEKTP--LSAIYLADLLYEAGLPPDML 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 219 NMIFG--TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIplfaEMSAINPLIILPQALQTRAEALAnelVASF 296
Cdd:cd07146 181 SVVTGepGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLL----ELGGNDPLIVMDDADLERAATLA---VAGS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 297 TLGGGQFCTRPGLILALRGAgLERFKSALCAAVAgstpQVLLNAPTLQHYRQGV-----AALAVHPRIEK-LASG--IAA 368
Cdd:cd07146 254 YANSGQRCTAVKRILVHESV-ADEFVDLLVEKSA----ALVVGDPMDPATDMGTvideeAAIQIENRVEEaIAQGarVLL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 915779292 369 GAGQAQTLLWQAQVEDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVV 416
Cdd:cd07146 329 GNQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAIS 376
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
141-416 |
8.21e-22 |
|
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: 98.57 E-value: 8.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 141 LPRPDLRQYQQALGPVAVFGASNFPLAFstAGGDTASALAAGCPVVVKahPGHMATAelTAEAIVRAVVRCGLPGGVFNM 220
Cdd:cd07131 124 LPNKDAMTRRQPIGVVALITPWNFPVAI--PSWKIFPALVCGNTVVFK--PAEDTPA--CALKLVELFAEAGLPPGVVNV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 221 I--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAE-ALANELVASFT 297
Cdd:cd07131 198 VhgRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVAL--EMGGKNPIIVMDDA---DLDlALEGALWSAFG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 298 LgGGQFCTRPGLILALRGAgLERFKSALCAAV------AGSTPQV----LLNAPTLQHYRQGVAALAVHPRIEKLASGIA 367
Cdd:cd07131 273 T-TGQRCTATSRLIVHESV-YDEFLKRFVERAkrlrvgDGLDEETdmgpLINEAQLEKVLNYNEIGKEEGATLLLGGERL 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 915779292 368 AGAGQAQTLLWQAQV-EDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVV 416
Cdd:cd07131 351 TGGGYEKGYFVEPTVfTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
65-411 |
1.52e-21 |
|
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: 97.64 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 65 TTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILRGDTfaariDTALADRQPLPRP 144
Cdd:cd07082 58 MPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDG-----DSLPGDWFPGTKG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 145 DLRQYQQA-LGPVAVFGASNFPL--AFSTaggdTASALAAGCPVVVKAhpghmATAE-LTAEAIVRAVVRCGLPGGVFNM 220
Cdd:cd07082 133 KIAQVRREpLGVVLAIGPFNYPLnlTVSK----LIPALIMGNTVVFKP-----ATQGvLLGIPLAEAFHDAGFPKGVVNV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 221 IF--GTDIGAELVRHPAIQAVGFTGSLAGGKalyQLAQQRPQpIPLFAEMSAINPLIILPQA-LqtraEALANELVA--- 294
Cdd:cd07082 204 VTgrGREIGDPLVTHGRIDVISFTGSTEVGN---RLKKQHPM-KRLVLELGGKDPAIVLPDAdL----ELAAKEIVKgal 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 295 SFTlggGQFCTRPGLILALRGAgLERFKSALCAAVAGS------------TPQVLLNAPTlqhYRQGVAALAVhpriEKL 362
Cdd:cd07082 276 SYS---GQRCTAIKRVLVHESV-ADELVELLKEEVAKLkvgmpwdngvdiTPLIDPKSAD---FVEGLIDDAV----AKG 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 915779292 363 ASGIAAGAGQAQTLLWQAQVEDLLAQDTLLQTEVFGPLSLLVEVDDVAQ 411
Cdd:cd07082 345 ATVLNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
65-409 |
2.10e-21 |
|
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: 97.12 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 65 TTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVI--LRGDTFAARIDTALADRQPLP 142
Cdd:cd07094 40 LPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAerIRGEEIPLDATQGSDNRLAWT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 143 RPDlrqyqqALGPVAVFGASNFPLAFSTAggDTASALAAGCPVVVKahPGhmATAELTAEAIVRAVVRCGLPGGVFNMIF 222
Cdd:cd07094 120 IRE------PVGVVLAITPFNFPLNLVAH--KLAPAIATGCPVVLK--PA--SKTPLSALELAKILVEAGVPEGVLQVVT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 223 GT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAqqrpqPIPLFA-EMSAINPLIILPQA-LQTRAEALANelvASFtL 298
Cdd:cd07094 188 GEreVLGDAFAADERVAMLSFTGSAAVGEALRANA-----GGKRIAlELGGNAPVIVDRDAdLDAAIEALAK---GGF-Y 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 299 GGGQFCTRPGLILALRGAGlERFKSALCAAVAgstpQVLLNAPTLQHYRQG-----VAALAVHPRIEKlasGIAAGA--- 370
Cdd:cd07094 259 HAGQVCISVQRIYVHEELY-DEFIEAFVAAVK----KLKVGDPLDEDTDVGpliseEAAERVERWVEE---AVEAGArll 330
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 915779292 371 --GQAQTLLWQAQVEDLLAQDTLLQT-EVFGPLSLLVEVDDV 409
Cdd:cd07094 331 cgGERDGALFKPTVLEDVPRDTKLSTeETFGPVVPIIRYDDF 372
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
62-305 |
1.12e-20 |
|
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: 95.02 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADvilrgdtFAARI--DTALADRq 139
Cdd:cd07088 51 WERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAE-------WARRIegEIIPSDR- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 140 plPRPDLRQYQQALGPVAVFGASNFPLAfsTAGGDTASALAAGCPVVVKahPGHMATaeLTAEAIVRAVVRCGLPGGVFN 219
Cdd:cd07088 123 --PNENIFIFKVPIGVVAGILPWNFPFF--LIARKLAPALVTGNTIVIK--PSEETP--LNALEFAELVDEAGLPAGVLN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 220 MIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAealANELVASFT 297
Cdd:cd07088 195 IVTGRgsVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL--ELGGKAPAIVMKDADLDLA---VKAIVDSRI 269
|
....*...
gi 915779292 298 LGGGQFCT 305
Cdd:cd07088 270 INCGQVCT 277
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
62-334 |
1.38e-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: 94.49 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPL---ARLQGERArtSGQLRMFADViLRGDTFAARIDTALADR 138
Cdd:cd07138 52 WSATSVEERAALLERIAEAYEARADELAQAITLEMGAPItlaRAAQVGLG--IGHLRAAADA-LKDFEFEERRGNSLVVR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 139 QPLprpdlrqyqqalGPVAVFGASNFPLAFSTAggDTASALAAGCPVVVKahPGHMA--TAELTAEAIVRAvvrcGLPGG 216
Cdd:cd07138 129 EPI------------GVCGLITPWNWPLNQIVL--KVAPALAAGCTVVLK--PSEVAplSAIILAEILDEA----GLPAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 217 VFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAEALAnelVA 294
Cdd:cd07138 189 VFNLVNGDgpVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVAL--ELGGKSANIILDDADLEKAVPRG---VA 263
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 915779292 295 SFTLGGGQFCTRPGLILALRGAgLERFKSALCAAVAGSTP 334
Cdd:cd07138 264 ACFANSGQSCNAPTRMLVPRSR-YAEAEEIAAAAAEAYVV 302
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
43-425 |
1.90e-20 |
|
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: 93.98 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 43 ASREEAALAAEAAQQAFAVYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVI- 121
Cdd:cd07107 16 ASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 122 -LRGDTFaaridtaladrqPLPRPDLR-QYQQALGPVAVFGASNFPLAFstAGGDTASALAAGCPVVVKAHPGHMATAEL 199
Cdd:cd07107 96 eLKGETI------------PVGGRNLHyTLREPYGVVARIVAFNHPLMF--AAAKIAAPLAAGNTVVVKPPEQAPLSALR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 200 TAEaivraVVRCGLPGGVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIIL 277
Cdd:cd07107 162 LAE-----LAREVLPPGVFNILPGDgaTAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTL--ELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 278 PQA-LQTRAEALANELVASFTlggGQFC---TRPGLILALRGAGLERFKSALCAAVAG--STPQVLLNA-PTLQHYRQGV 350
Cdd:cd07107 235 PDAdPEAAADAAVAGMNFTWC---GQSCgstSRLFVHESIYDEVLARVVERVAAIKVGdpTDPATTMGPlVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 351 AALAvhPRIEKLASgIAAGAGQAQTLLWQAQ--VE-----DLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQL 423
Cdd:cd07107 312 HYID--SAKREGAR-LVTGGGRPEGPALEGGfyVEptvfaDVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGL 388
|
..
gi 915779292 424 TA 425
Cdd:cd07107 389 TA 390
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
62-411 |
1.92e-20 |
|
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: 93.93 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLA-RLQGERARTSGQLRMFADvilrgdtfAARIDTALADRQP 140
Cdd:cd07092 35 WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHlVRDDELPGAVDNFRFFAG--------AARTLEGPAAGEY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 141 LPRPDLRQYQQALGPVAVFGASNFPLAFSTAggDTASALAAGCPVVVKAHPGHMATAELTAEAIVRavvrcGLPGGVFNM 220
Cdd:cd07092 107 LPGHTSMIRREPIGVVAQIAPWNYPLMMAAW--KIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-----VLPPGVVNV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 221 IFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALANELVASFTL 298
Cdd:cd07092 180 VCGGgaSAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHL--ELGGKAPVIVFDDA---DLDAAVAGIATAGYY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 299 GGGQFCTRPGLILALRGAgLERFKSALCAAVAgstpQVLLNAP-----------TLQHyRQGVAALavhprIEKLASGIA 367
Cdd:cd07092 255 NAGQDCTAACRVYVHESV-YDEFVAALVEAVS----AIRVGDPddedtemgplnSAAQ-RERVAGF-----VERAPAHAR 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 915779292 368 AGAGQAQT----LLWQAQVEDLLAQ-DTLLQTEVFGPLSLLVEVDDVAQ 411
Cdd:cd07092 324 VLTGGRRAegpgYFYEPTVVAGVAQdDEIVQEEIFGPVVTVQPFDDEDE 372
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-411 |
4.00e-20 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 93.05 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 7 MAGRQFIAGRRIASGEATLLSLRAVDGEATGHrfYP-ASREEAALAAEAAQQAFAVYSQTTPQQRAHFLCAIADELDALG 85
Cdd:PRK13473 1 MQTKLLINGELVAGEGEKQPVYNPATGEVLAE--IAeASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 86 EPFFAIAGQETALPL-ARLQGERARTSGQLRMFADvilrgdtfAARIDTALADRQPLP------RPDlrqyqqALGPVAV 158
Cdd:PRK13473 79 DEFARLESLNCGKPLhLALNDEIPAIVDVFRFFAG--------AARCLEGKAAGEYLEghtsmiRRD------PVGVVAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 159 FGASNFPLAFstAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAvvrcgLPGGVFNMIFGT--DIGAELVRHPAI 236
Cdd:PRK13473 145 IAPWNYPLMM--AAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-----LPPGVLNVVTGRgaTVGDALVGHPKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 237 QAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALANELVASFTLGGGQFCTRPGLILALRGA 316
Cdd:PRK13473 218 RMVSLTGSIATGKHVLSAAADSVKRTHL--ELGGKAPVIVFDDA---DLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 317 gLERFKSALCAAVAgstpQVLLNAP-----------TLQHyRQGVAAL----AVHPRIEKLASG-IAAGAGQ--AQTLlw 378
Cdd:PRK13473 293 -YDDLVAKLAAAVA----TLKVGDPddedtelgpliSAAH-RDRVAGFveraKALGHIRVVTGGeAPDGKGYyyEPTL-- 364
|
410 420 430
....*....|....*....|....*....|...
gi 915779292 379 qaqVEDLLAQDTLLQTEVFGPLSLLVEVDDVAQ 411
Cdd:PRK13473 365 ---LAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
62-411 |
1.15e-19 |
|
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: 91.90 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILRGDTFAAridtaladrQPL 141
Cdd:cd07124 85 WRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPV---------EMV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 142 PRPDLRQYQQALGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKahPghmatAELT---AEAIVRAVVRCGLPGGVF 218
Cdd:cd07124 156 PGEDNRYVYRPLGVGAVISPWNFPLAILA--GMTTAALVTGNTVVLK--P-----AEDTpviAAKLVEILEEAGLPPGVV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 219 NMIFGTD--IGAELVRHPAIQAVGFTGSLAGGKALYQLAqQRPQPI-----PLFAEMSAINPLIILPQA-LQTRAEALan 290
Cdd:cd07124 227 NFLPGPGeeVGDYLVEHPDVRFIAFTGSREVGLRIYERA-AKVQPGqkwlkRVIAEMGGKNAIIVDEDAdLDEAAEGI-- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 291 eLVASFTLgGGQFCTRPGLILALRG---AGLERFKSALCAAVAG--STPQVLL----NAPTLQHYRQgvaALAVHPRIEK 361
Cdd:cd07124 304 -VRSAFGF-QGQKCSACSRVIVHESvydEFLERLVERTKALKVGdpEDPEVYMgpviDKGARDRIRR---YIEIGKSEGR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 915779292 362 LASGIAAGAGQAQTLLWQ-AQVEDLLAQDTLLQTEVFGPLSLLVEVDDVAQ 411
Cdd:cd07124 379 LLLGGEVLELAAEGYFVQpTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
143-408 |
1.35e-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: 91.47 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 143 RPDLRQYQQA--LGPVAVFGASNFPLAfsTAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAVVRCGLPGGVFNM 220
Cdd:cd07086 122 RPGHRLMEQWnpLGVVGVITAFNFPVA--VPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 221 IFG-TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQA---LQTRAealanELVASF 296
Cdd:cd07086 200 VTGgGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLL--ELGGNNAIIVMDDAdldLAVRA-----VLFAAV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 297 -TlgGGQFCTRPG-LIL--ALRGAGLERFKSALCAAVAGStPqvlLNAPTLQ---HYRQGVaalavhpriEKLASGIAAG 369
Cdd:cd07086 273 gT--AGQRCTTTRrLIVheSVYDEFLERLVKAYKQVRIGD-P---LDEGTLVgplINQAAV---------EKYLNAIEIA 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 915779292 370 AGQAQTLLW---------------QAQVEDLLAQDTLLQTEVFGPLSLLVEVDD 408
Cdd:cd07086 338 KSQGGTVLTggkridggepgnyvePTIVTGVTDDARIVQEETFAPILYVIKFDS 391
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
65-331 |
1.38e-19 |
|
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: 91.27 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 65 TTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLaRLQ--GERARTSGQLRMFADVI--LRGDTFAaridtaladrqp 140
Cdd:cd07108 38 TPARERGKLLARIADALEARSEELARLLALETGNAL-RTQarPEAAVLADLFRYFGGLAgeLKGETLP------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 141 lPRPDLRQY--QQALGPVAVFGASNFPLAFSTAggDTASALAAGCPVVVKahpghmataelTAEAIVRAVVRCG------ 212
Cdd:cd07108 105 -FGPDVLTYtvREPLGVVGAILPWNAPLMLAAL--KIAPALVAGNTVVLK-----------AAEDAPLAVLLLAeilaqv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 213 LPGGVFNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAealAN 290
Cdd:cd07108 171 LPAGVLNVItgYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSL--ELGGKSPMIVFPDADLDDA---VD 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 915779292 291 ELVAS--FTLgGGQFCT---RPGLILALRGAGLERFKSALCAAVAG 331
Cdd:cd07108 246 GAIAGmrFTR-QGQSCTagsRLFVHEDIYDAFLEKLVAKLSKLKIG 290
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
69-305 |
1.76e-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: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 69 QRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLrmfaDVILRG-DTFAARIDTALADRQPLPRpdlr 147
Cdd:cd07095 23 ERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKI----DISIKAyHERTGERATPMAQGRAVLR---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 148 qyQQALGPVAVFGASNFPLAFstAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAvvrcGLPGGVFNMIFGT-DI 226
Cdd:cd07095 95 --HRPHGVMAVFGPFNFPGHL--PNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA----GLPPGVLNLVQGGrET 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915779292 227 GAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIpLFAEMSAINPLIILPQAlqtRAEALANELVASFTLGGGQFCT 305
Cdd:cd07095 167 GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-LALEMGGNNPLVVWDVA---DIDAAAYLIVQSAFLTAGQRCT 241
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
65-330 |
2.39e-19 |
|
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: 90.77 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 65 TTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGerartsgqlrMFADVILRGDTFAARIDTALADRQPLPRP 144
Cdd:cd07089 39 TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA----------MQVDGPIGHLRYFADLADSFPWEFDLPVP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 145 DLRQY-------QQALGPVAVFGASNFPlaFSTAGGDTASALAAGCPVVVKAHPghmaTAELTAEAIVRAVVRCGLPGGV 217
Cdd:cd07089 109 ALRGGpgrrvvrREPVGVVAAITPWNFP--FFLNLAKLAPALAAGNTVVLKPAP----DTPLSALLLGEIIAETDLPAGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 218 FNMIFGTD--IGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAEALAnelVAS 295
Cdd:cd07089 183 VNVVTGSDnaVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLL--ELGGKSANIVLDDADLAAAAPAA---VGV 257
|
250 260 270
....*....|....*....|....*....|....*
gi 915779292 296 FTLGGGQFCTRPGLILALRGAgLERFKSALCAAVA 330
Cdd:cd07089 258 CMHNAGQGCALTTRLLVPRSR-YDEVVEALAAAFE 291
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
63-398 |
7.32e-19 |
|
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: 89.33 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 63 SQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVilrgdtfAARIDTALADRQPLP 142
Cdd:cd07110 36 KKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADL-------AEQLDAKAERAVPLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 143 RPDL--RQYQQALGPVAVFGASNFPLAfsTAGGDTASALAAGCPVVVKahPGHMATaeLTAEAIVRAVVRCGLPGGVFNM 220
Cdd:cd07110 109 SEDFkaRVRREPVGVVGLITPWNFPLL--MAAWKVAPALAAGCTVVLK--PSELTS--LTELELAEIAAEAGLPPGVLNV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 221 I--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtraealANELVASFTL 298
Cdd:cd07110 183 VtgTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSL--ELGGKSPIIVFDDA--------DLEKAVEWAM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 299 GG-----GQFCTRPGLIL---ALRGAGLERFKSALCAAVAGS--TPQVLLNAPTLQHYRQGVAALavhpriekLASGIAA 368
Cdd:cd07110 253 FGcfwnnGQICSATSRLLvheSIADAFLERLATAAEAIRVGDplEEGVRLGPLVSQAQYEKVLSF--------IARGKEE 324
|
330 340 350
....*....|....*....|....*....|
gi 915779292 369 GAgqaqTLLWQAQVEDLLAQDTLLQTEVFG 398
Cdd:cd07110 325 GA----RLLCGGRRPAHLEKGYFIAPTVFA 350
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
67-418 |
2.32e-18 |
|
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: 87.78 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 67 PQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADvilrgdtfAARidtALADRQPLPRPD- 145
Cdd:cd07120 41 PRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAG--------LAR---TEAGRMIEPEPGs 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 146 ----LRQyqqALGPVAVFGASNFPLAFSTAggDTASALAAGCPVVVKAhPGHMAtaeLTAEAIVRAVVRC-GLPGGVFNM 220
Cdd:cd07120 110 fslvLRE---PMGVAGIIVPWNSPVVLLVR--SLAPALAAGCTVVVKP-AGQTA---QINAAIIRILAEIpSLPAGVVNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 221 IF--GTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALANELVASFTL 298
Cdd:cd07120 181 FTesGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGL--ELGGKTPCIVFDDA---DLDAALPKLERALTI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 299 GGGQFCTRPGLILALRGAgLERFKSALCAAVA------GSTPQVLLNAPTLQHYRQGV----------AALAVHpRIEKL 362
Cdd:cd07120 256 FAGQFCMAGSRVLVQRSI-ADEVRDRLAARLAavkvgpGLDPASDMGPLIDRANVDRVdrmveraiaaGAEVVL-RGGPV 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 915779292 363 ASGIAAGAGQAQTLLwqaqvEDLLAQDTLLQTEVFGPLSLLVEVDDVAqlQAVVKA 418
Cdd:cd07120 334 TEGLAKGAFLRPTLL-----EVDDPDADIVQEEIFGPVLTLETFDDEA--EAVALA 382
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
62-404 |
2.61e-18 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 87.82 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILRgdTFAARIDTALADRQPL 141
Cdd:PLN02278 78 WSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKR--VYGDIIPSPFPDRRLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 142 PrpdLRQyqqalgPVAVFGAS---NFPLAFSTAggDTASALAAGCPVVVKahPGHmaTAELTAEAIVRAVVRCGLPGGVF 218
Cdd:PLN02278 156 V---LKQ------PVGVVGAItpwNFPLAMITR--KVGPALAAGCTVVVK--PSE--LTPLTALAAAELALQAGIPPGVL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 219 NMIFG--TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALANELVASF 296
Cdd:PLN02278 221 NVVMGdaPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSL--ELGGNAPFIVFDDA---DLDVAVKGALASK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 297 TLGGGQFCTRPGLILALRGAgLERFKSALCAAV----------AGSTPQVLLNAPTLQHYRQGVAAlAVHPRIEKLASGI 366
Cdd:PLN02278 296 FRNSGQTCVCANRILVQEGI-YDKFAEAFSKAVqklvvgdgfeEGVTQGPLINEAAVQKVESHVQD-AVSKGAKVLLGGK 373
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 915779292 367 AAGAGQ---AQTLLWQAQVEDLLAqdtllQTEVFGPLSLLV 404
Cdd:PLN02278 374 RHSLGGtfyEPTVLGDVTEDMLIF-----REEVFGPVAPLT 409
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
63-304 |
2.95e-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: 87.20 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 63 SQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFA-----DVILRgDTFAARIDTAlad 137
Cdd:cd07106 36 SATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTAsldlpDEVIE-DDDTRRVELR--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 138 RQPlprpdlrqyqqaLGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHPghmaTAELTAEAIVRAVVRCgLPGGV 217
Cdd:cd07106 112 RKP------------LGVVAAIVPWNFPL--LLAAWKIAPALLAGNTVVLKPSP----FTPLCTLKLGELAQEV-LPPGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 218 FNMIFG-TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALqtrAEALANELVASF 296
Cdd:cd07106 173 LNVVSGgDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTL--ELGGNDAAIVLPDVD---IDAVAPKLFWGA 247
|
....*...
gi 915779292 297 TLGGGQFC 304
Cdd:cd07106 248 FINSGQVC 255
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
63-304 |
6.90e-18 |
|
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: 86.07 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 63 SQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVilrgdtfAARIDTALAdrqPLP 142
Cdd:cd07114 38 RKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGL-------ADKIEGAVI---PVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 143 RPDLRQYQQ--ALGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKahPGHMATAelTAEAIVRAVVRCGLPGGVFNM 220
Cdd:cd07114 108 KGDYLNFTRrePLGVVAAITPWNSPLLLLA--KKLAPALAAGNTVVLK--PSEHTPA--STLELAKLAEEAGFPPGVVNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 221 I--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAealANELVASFTL 298
Cdd:cd07114 182 VtgFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTL--ELGGKSPNIVFDDADLDAA---VNGVVAGIFA 256
|
....*.
gi 915779292 299 GGGQFC 304
Cdd:cd07114 257 AAGQTC 262
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
61-409 |
1.22e-17 |
|
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: 85.43 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 61 VYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLarlqgERARtsgqlrmfADVILRGDTFA--ARIDTALADR 138
Cdd:cd07090 34 EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-----EEAR--------VDIDSSADCLEyyAGLAPTLSGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 139 Q-PLPRPDLrQY--QQALGPVAVFGASNFPlaFSTAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAvvrcGLPG 215
Cdd:cd07090 101 HvPLPGGSF-AYtrREPLGVCAGIGAWNYP--IQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEA----GLPD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 216 GVFNMIFG-TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAEALAneLVA 294
Cdd:cd07090 174 GVFNVVQGgGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTL--ELGGKSPLIIFDDADLENAVNGA--MMA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 295 SFtLGGGQFCTRPGLILALRGAgLERFKSALCAavagSTPQVLLNAPTLQHYRQGvaALAVHPRIEKLASGIAAGAGQAQ 374
Cdd:cd07090 250 NF-LSQGQVCSNGTRVFVQRSI-KDEFTERLVE----RTKKIRIGDPLDEDTQMG--ALISEEHLEKVLGYIESAKQEGA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 915779292 375 TLLW---QAQVEDLLA---------------QDTLLQTEVFGPLSLLVEVDDV 409
Cdd:cd07090 322 KVLCggeRVVPEDGLEngfyvspcvltdctdDMTIVREEIFGPVMSILPFDTE 374
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
43-408 |
1.36e-17 |
|
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: 85.07 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 43 ASREEAALAAEAAQQAFAVYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVI- 121
Cdd:cd07150 18 GSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 122 -LRGDT----FAARIDTALadRQPlprpdlrqyqqaLGPVAVFGASNFPLAFSTAggDTASALAAGCPVVVKAHPGHMAT 196
Cdd:cd07150 98 rVRGETlpsdSPGTVSMSV--RRP------------LGVVAGITPFNYPLILATK--KVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 197 AELTAEAIVRAvvrcGLPGGVFNMIF--GTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPL 274
Cdd:cd07150 162 GLKIAEIMEEA----GLPKGVFNVVTggGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITL--ELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 275 IILPQALQTRAEALAnelVASFTLGGGQFCTRPGLILaLRGAGLERFKSALCAAVAGST------PQVLLnAPTLQHyRQ 348
Cdd:cd07150 236 IVLADADLDYAVRAA---AFGAFMHQGQICMSASRII-VEEPVYDEFVKKFVARASKLKvgdprdPDTVI-GPLISP-RQ 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 915779292 349 gvaALAVHPRIEK-LASG--IAAGAGQAQTLLWQAQVEDLLAQDTLLQTEVFGPLSLLVEVDD 408
Cdd:cd07150 310 ---VERIKRQVEDaVAKGakLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKD 369
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
63-400 |
1.52e-17 |
|
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: 85.32 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 63 SQTTPQQRAHFLCAIADELDALGEPFFAIAGQET-------------ALPLARLQGERARtsgqlRMFADVILRGDTFAa 129
Cdd:cd07125 86 SATPVEERAEILEKAADLLEANRGELIALAAAEAgktladadaevreAIDFCRYYAAQAR-----ELFSDPELPGPTGE- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 130 ridtaladrqplprpdLRQYQ-QALGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKahPghmatAE---LTAEAIV 205
Cdd:cd07125 160 ----------------LNGLElHGRGVFVCISPWNFPLAIFT--GQIAAALAAGNTVIAK--P-----AEqtpLIAARAV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 206 RAVVRCGLPGGVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPI-PLFAEMSAINPLIILPQALq 282
Cdd:cd07125 215 ELLHEAGVPRDVLQLVPGDgeEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPIlPLIAETGGKNAMIVDSTAL- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 283 trAEALANELVASFTLGGGQFCTrpglilALRGAGL-----ERFKSALCAAVA----GStpqvllnaPTLQHYRQGvaal 353
Cdd:cd07125 294 --PEQAVKDVVQSAFGSAGQRCS------ALRLLYLqeeiaERFIEMLKGAMAslkvGD--------PWDLSTDVG---- 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915779292 354 avhPRIEK----LASGIAAGAGQAQTLLWQAQVEDL-----------LAQDTLLQTEVFGPL 400
Cdd:cd07125 354 ---PLIDKpagkLLRAHTELMRGEAWLIAPAPLDDGngyfvapgiieIVGIFDLTTEVFGPI 412
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
64-411 |
1.60e-16 |
|
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: 81.90 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 64 QTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVI--LRGDTFAARID-TALADRQP 140
Cdd:cd07109 38 RLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAAdkLHGETIPLGPGyFVYTVREP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 141 LprpdlrqyqqalGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKahpghmaTAE---LTAEAIVRAVVRCGLPGGV 217
Cdd:cd07109 118 H------------GVTGHIIPWNYPL--QITGRSVAPALAAGNAVVVK-------PAEdapLTALRLAELAEEAGLPAGA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 218 FNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALANELVAS 295
Cdd:cd07109 177 LNVVtgLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTL--ELGGKSPQIVFADA---DLEAALPVVVNA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 296 FTLGGGQFCTRPGLIL---ALRGAGLERFKSALCAAVAGSTPQVLLNAPTL-QHYRQGVA---ALAVHPRIEKLASGIAA 368
Cdd:cd07109 252 IIQNAGQTCSAGSRLLvhrSIYDEVLERLVERFRALRVGPGLEDPDLGPLIsAKQLDRVEgfvARARARGARIVAGGRIA 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 915779292 369 ------GAGQAQTLLwqaqvEDLLAQDTLLQTEVFGPLSLLVEVDDVAQ 411
Cdd:cd07109 332 egapagGYFVAPTLL-----DDVPPDSRLAQEEIFGPVLAVMPFDDEAE 375
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-417 |
2.08e-16 |
|
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: 81.47 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 57 QAFAVYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETalplarlqGERARTSGQLRMFADVILRGdtFAARIDTALA 136
Cdd:cd07105 11 AAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEET--------GATAAWAGFNVDLAAGMLRE--AASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 137 DRQPLPRPDLRQ--YQQALGPVAVFGASNFPLAFSTAGgdTASALAAGCPVVVKAHPghmaTAELTAEAIVRAVVRCGLP 214
Cdd:cd07105 81 GSIPSDKPGTLAmvVKEPVGVVLGIAPWNAPVILGTRA--IAYPLAAGNTVVLKASE----LSPRTHWLIGRVFHEAGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 215 GGVFNMIF-----GTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAealA 289
Cdd:cd07105 155 KGVLNVVThspedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLL--ELGGKAPAIVLEDADLDAA---A 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 290 NELVASFTLGGGQFCTRPGLILALRGAGlERFKSALCAAVAG-----STPQVLLNAPTLQHYRQGVA-ALAvhpRIEKLA 363
Cdd:cd07105 230 NAALFGAFLNSGQICMSTERIIVHESIA-DEFVEKLKAAAEKlfagpVVLGSLVSAAAADRVKELVDdALS---KGAKLV 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 915779292 364 SGiAAGAGQAQTLLWQAQVEDLLAQDTLL-QTEVFGPLSLLVEVDDVAQLQAVVK 417
Cdd:cd07105 306 VG-GLADESPSGTSMPPTILDNVTPDMDIySEESFGPVVSIIRVKDEEEAVRIAN 359
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
62-276 |
4.61e-16 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 80.93 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDalgEPFFAIAGQET---ALPLARLQGERARTSGQLRMFADvilRGDTFAARIDTALAdr 138
Cdd:PLN02467 66 WARTTGAVRAKYLRAIAAKIT---ERKSELAKLETldcGKPLDEAAWDMDDVAGCFEYYAD---LAEALDAKQKAPVS-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 139 qpLPRPDLRQY--QQALGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKahPGHMATaeLTAEAIVRAVVRCGLPGG 216
Cdd:PLN02467 138 --LPMETFKGYvlKEPLGVVGLITPWNYPLLMAT--WKVAPALAAGCTAVLK--PSELAS--VTCLELADICREVGLPPG 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915779292 217 VFNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLII 276
Cdd:PLN02467 210 VLNVVtgLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSL--ELGGKSPIIV 269
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
95-258 |
9.07e-16 |
|
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: 79.60 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 95 ETALPLARLQGErartsgqlrmFADVILRGDTFAARIDTALADRQPLPRPDLRQY--QQALGPVAVFGASNFPLAfsTAG 172
Cdd:cd07102 67 QMGRPIAQAGGE----------IRGMLERARYMISIAEEALADIRVPEKDGFERYirREPLGVVLIIAPWNYPYL--TAV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 173 GDTASALAAGCPVVVKahpgHMATAELTAEAIVRAVVRCGLPGGVFNMIFGTD-IGAELVRHPAIQAVGFTGSLAGGKAL 251
Cdd:cd07102 135 NAVIPALLAGNAVILK----HSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHeTSAALIADPRIDHVSFTGSVAGGRAI 210
|
....*..
gi 915779292 252 YQLAQQR 258
Cdd:cd07102 211 QRAAAGR 217
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
61-494 |
1.02e-15 |
|
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: 79.41 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 61 VYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPL-ARLQGERARTSGQLRMFADVI--LRGDTfaaridtalad 137
Cdd:cd07115 34 AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIrAARRLDVPRAADTFRYYAGWAdkIEGEV----------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 138 rqpLP-RPDLRQYQQaLGPVAVFGAS---NFPLAFstAGGDTASALAAGCPVVVKahPGHMATaeLTAEAIVRAVVRCGL 213
Cdd:cd07115 103 ---IPvRGPFLNYTV-REPVGVVGAIvpwNFPLMF--AAWKVAPALAAGNTVVLK--PAELTP--LSALRIAELMAEAGF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 214 PGGVFNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALANE 291
Cdd:cd07115 173 PAGVLNVVtgFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSL--ELGGKSANIVFADA---DLDAAVRA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 292 LVASFTLGGGQFCTRPGLILALRGAGlERFKSALCAAVAGSTPQVLLNAPTlqhyrqGVAALAVHPRIEKLASGIAAGAG 371
Cdd:cd07115 248 AATGIFYNQGQMCTAGSRLLVHESIY-DEFLERFTSLARSLRPGDPLDPKT------QMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 372 QAQTLLWQAQ-------------VEDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLHAeADDGPLAA 438
Cdd:cd07115 321 EGARLLTGGKrpgargffveptiFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWT-RDLGRAHR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 915779292 439 SLLPLlceKAGRVLFNGYptgvevcDAMVHGGPWPATTDAR-GTSVGSRAIERFLRP 494
Cdd:cd07115 400 VAAAL---KAGTVWINTY-------NRFDPGSPFGGYKQSGfGREMGREALDEYTEV 446
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
11-427 |
1.55e-15 |
|
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: 79.02 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 11 QFIAGRRIASGEATLLSLRAVDGEATGHRFYPASREEAALAAEAAQQAFAV-YSQTTPQQRAHFLCAIADELDALGEpff 89
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 90 AIAGQETALPLARLQGERARTSGQ----LRMFADVI--LRGDTFAARIdtaladrqplPRPDLRQYQ-----QALGPVAV 158
Cdd:cd07113 79 ELAQLETLCSGKSIHLSRAFEVGQsanfLRYFAGWAtkINGETLAPSI----------PSMQGERYTaftrrEPVGVVAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 159 FGASNFPLAFstAGGDTASALAAGCPVVVKahPGHMAT------AELTAEAivravvrcGLPGGVFNMIFGT-DIGAELV 231
Cdd:cd07113 149 IVPWNFSVMI--AVWKIGAALATGCTIVIK--PSEFTPltllrvAELAKEA--------GIPDGVLNVVNGKgAVGAQLI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 232 RHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqTRAEALANELVASFtLGGGQFCTRPGLIL 311
Cdd:cd07113 217 SHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL--ELGGKNAAAFLKDA--DIDWVVEGLLTAGF-LHQGQVCAAPERFY 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 312 ALRG---AGLERFKSALCAAVAGS--TPQVLLNaptlqhyrqgvaALAVHPRIEKLASGIAAGAGQAQTLLWQAQ----- 381
Cdd:cd07113 292 VHRSkfdELVTKLKQALSSFQVGSpmDESVMFG------------PLANQPHFDKVCSYLDDARAEGDEIVRGGEalage 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 915779292 382 ---VEDLL-----AQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATL 427
Cdd:cd07113 360 gyfVQPTLvlarsADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASV 413
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
62-280 |
8.28e-15 |
|
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: 76.61 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADV--ILRGDTFAARID--TALAD 137
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLarTLHGDSYNNLGDdmLGLVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 138 RQPLprpdlrqyqqalGPVAVFGASNFPlaFSTAGGDTASALAAGCPVVVKahPGHM--ATAELTAEAIVRAvvrcGLPG 215
Cdd:cd07118 117 REPI------------GVVGIITPWNFP--FLILSQKLPFALAAGCTVVVK--PSEFtsGTTLMLAELLIEA----GLPA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 915779292 216 GVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQA 280
Cdd:cd07118 177 GVVNIVTGYgaTVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSL--ELGGKNPQIVFADA 241
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
61-408 |
1.81e-14 |
|
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: 75.46 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 61 VYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADV--ILRGDTFaaRIDT----- 133
Cdd:cd07145 36 VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEakVLRGETI--PVDAyeyne 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 134 ---ALADRQPLprpdlrqyqqalGPVAVFGASNFPLAFSTAggDTASALAAGCPVVVkaHPGhmATAELTAEAIVRAVVR 210
Cdd:cd07145 114 rriAFTVREPI------------GVVGAITPFNFPANLFAH--KIAPAIAVGNSVVV--KPS--SNTPLTAIELAKILEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 211 CGLPGGVFNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAeal 288
Cdd:cd07145 176 AGLPPGVINVVtgYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVAL--ELGGSDPMIVLKDADLERA--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 289 ANELVASFTLGGGQFCTRPGLILaLRGAGLERFKSALCAAVAgstpQVLLNAPTLQHYRQGV-----AALAVHPRIEK-L 362
Cdd:cd07145 251 VSIAVRGRFENAGQVCNAVKRIL-VEEEVYDKFLKLLVEKVK----KLKVGDPLDESTDLGPlispeAVERMENLVNDaV 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 915779292 363 ASG---IAAGAGQAQTLLWQAQVEDLLAQDTLLQTEVFGPLSLLVEVDD 408
Cdd:cd07145 326 EKGgkiLYGGKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKD 374
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
152-428 |
2.92e-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: 75.02 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 152 ALGPVAVFGASNFPLAFSTAGgdTASALAAGCPVVVKAHP-----GHMATAELTAEAivravvrcGLPGGVFNMIFG-TD 225
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRS--VAPALALGNAVVLKPDPrtpvsGGVVIARLFEEA--------GLPAGVLHVLPGgAD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 226 IGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqTRAEALANELVASFtLGGGQFCT 305
Cdd:cd07152 180 AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL--ELGGKNALIVLDDA--DLDLAASNGAWGAF-LHQGQICM 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 306 RPGLILALRGAgLERFKSALCAAVA------GSTPQVLLNAPTLQHYRQGVAALavhpriekLASGIAAGA-----GQAQ 374
Cdd:cd07152 255 AAGRHLVHESV-ADAYTAKLAAKAKhlpvgdPATGQVALGPLINARQLDRVHAI--------VDDSVAAGArleagGTYD 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 915779292 375 TLLWQAQV-EDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLH 428
Cdd:cd07152 326 GLFYRPTVlSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGII 380
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
127-280 |
4.52e-14 |
|
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: 74.18 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 127 FAARIDTALADRQPLPRPD-----LRQYQQALGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKahPGHMATaeLTA 201
Cdd:cd07099 89 AARNAPRVLAPRKVPTGLLmpnkkATVEYRPYGVVGVISPWNYPL--LTPMGDIIPALAAGNAVVLK--PSEVTP--LVG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 202 EAIVRAVVRCGLPGGVFNMIFGT-DIGAELVRHPaIQAVGFTGSLAGGKALYQLAQQRpqPIPLFAEMSAINPLIILPQA 280
Cdd:cd07099 163 ELLAEAWAAAGPPQGVLQVVTGDgATGAALIDAG-VDKVAFTGSVATGRKVMAAAAER--LIPVVLELGGKDPMIVLADA 239
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
62-331 |
5.03e-14 |
|
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: 74.03 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADvilRGDTFaaridtaLADrQPL 141
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAE---NAEAF-------LAD-EPI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 142 PRPDLRQY--QQALGPVavFGAS--NFPL--AFSTAggdtASALAAGCPVVVKahpgHMATAELTAEAIVRAVVRCGLPG 215
Cdd:cd07100 84 ETDAGKAYvrYEPLGVV--LGIMpwNFPFwqVFRFA----APNLMAGNTVLLK----HASNVPGCALAIEELFREAGFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 216 GVFNMIF-GTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALANELVA 294
Cdd:cd07100 154 GVFQNLLiDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVL--ELGGSDPFIVLDDA---DLDKAVKTAVK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 915779292 295 SFTLGGGQFCT---RpgLIL--ALRGAGLERFKSALCAAVAG 331
Cdd:cd07100 229 GRLQNAGQSCIaakR--FIVheDVYDEFLEKFVEAMAALKVG 268
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
55-408 |
6.73e-14 |
|
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: 73.72 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 55 AQQAFAVYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILR--GDTFAARID 132
Cdd:cd07104 9 AAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRpeGEILPSDVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 133 --TALADRQPlprpdlrqyqqaLGPVAVFGASNFPLAFSTAGgdTASALAAGCPVVVKAHP-----GHMATAELTAEAiv 205
Cdd:cd07104 89 gkESMVRRVP------------LGVVGVISPFNFPLILAMRS--VAPALALGNAVVLKPDSrtpvtGGLLIAEIFEEA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 206 ravvrcGLPGGVFNMIFG--TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQT 283
Cdd:cd07104 153 ------GLPKGVLNVVPGggSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVAL--ELGGNNPLIVLDDADLD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 284 RAEALAneLVASFtLGGGQFCTRPGLILALRgAGLERFKSALCAAVAG------STPQVLLnAPTLQHyRQgvaALAVHP 357
Cdd:cd07104 225 LAVSAA--AFGAF-LHQGQICMAAGRILVHE-SVYDEFVEKLVAKAKAlpvgdpRDPDTVI-GPLINE-RQ---VDRVHA 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915779292 358 RIEKlasGIAAGAgqaqTLLWQAQVEDLLAQDTLL----------QTEVFGPLSLLVEVDD 408
Cdd:cd07104 296 IVED---AVAAGA----RLLTGGTYEGLFYQPTVLsdvtpdmpifREEIFGPVAPVIPFDD 349
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
143-305 |
9.05e-14 |
|
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: 73.39 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 143 RPDLRQYQQA--LGPVAVFGASNFPLAfsTAGGDTASALAAGCPVVVKAHPghmaTAELTAEA----IVRAVVRCGLPGG 216
Cdd:cd07130 121 RPGHRMMEQWnpLGVVGVITAFNFPVA--VWGWNAAIALVCGNVVVWKPSP----TTPLTAIAvtkiVARVLEKNGLPGA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 217 VFNMIFG-TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRpqpiplFA----EMSAINPLIILPQA---LQTRAEAL 288
Cdd:cd07130 195 IASLVCGgADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR------FGrsllELGGNNAIIVMEDAdldLAVRAVLF 268
|
170
....*....|....*..
gi 915779292 289 AnelvASFTlgGGQFCT 305
Cdd:cd07130 269 A----AVGT--AGQRCT 279
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
62-305 |
1.20e-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: 73.11 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVIlrgdtfaaridTALADRQpL 141
Cdd:cd07119 53 WPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLA-----------TKETGEV-Y 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 142 PRPDLRQYQQALGPVAVFGAS---NFPLAfsTAGGDTASALAAGCPVVVKahPGHMATaeLTAEAIVRAVVRCGLPGGVF 218
Cdd:cd07119 121 DVPPHVISRTVREPVGVCGLItpwNYPLL--QAAWKLAPALAAGNTVVIK--PSEVTP--LTTIALFELIEEAGLPAGVV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 219 NMIFG--TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQA-LQTraeALANELVAS 295
Cdd:cd07119 195 NLVTGsgATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVAL--ELGGKNPNIVFADAdFET---AVDQALNGV 269
|
250
....*....|
gi 915779292 296 FtLGGGQFCT 305
Cdd:cd07119 270 F-FNAGQVCS 278
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
176-471 |
2.71e-13 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 72.30 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 176 ASALAAGCPVVVKAHPghmATAELTaEAIVRAVVRCG-LPGGVFNMIFGTdiGAELVRHPAIQ-AVGFTGSLAGGKALYQ 253
Cdd:cd07128 166 APALLAGVPVIVKPAT---ATAYLT-EAVVKDIVESGlLPEGALQLICGS--VGDLLDHLGEQdVVAFTGSAATAAKLRA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 254 LAQQRPQPIPLFAEMSAINPLIILPQALQTRAE--ALANELVASFTLGGGQFCTRPGLILALRG---AGLERFKSALCAA 328
Cdd:cd07128 240 HPNIVARSIRFNAEADSLNAAILGPDATPGTPEfdLFVKEVAREMTVKAGQKCTAIRRAFVPEArvdAVIEALKARLAKV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 329 VAG--STPQV----LLNAPTLQHYRQGVAAL-----AVH---PRIEKLASGIAAGAGQAQTLLwqaQVEDLLAQDTLLQT 394
Cdd:cd07128 320 VVGdpRLEGVrmgpLVSREQREDVRAAVATLlaeaeVVFggpDRFEVVGADAEKGAFFPPTLL---LCDDPDAATAVHDV 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 395 EVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLHaeADDGPLAASLLPLLCEKAGRVLFNGYPTGVE------VCDAMVH 468
Cdd:cd07128 397 EAFGPVATLMPYDSLAEAIELAARGRGSLVASVV--TNDPAFARELVLGAAPYHGRLLVLNRDSAKEstghgsPLPQLVH 474
|
...
gi 915779292 469 GGP 471
Cdd:cd07128 475 GGP 477
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
155-411 |
3.56e-13 |
|
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: 71.48 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 155 PVAVFGAS---NFPLafSTAGGDTASALAAGCPVVVKahPGHMAT------AELTAEAivravvrcGLPGGVFNMI--FG 223
Cdd:cd07112 124 PLGVVGAVvpwNFPL--LMAAWKIAPALAAGNSVVLK--PAEQSPltalrlAELALEA--------GLPAGVLNVVpgFG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 224 TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPiPLFAEMSAINPLIILPQA--LQTRAEALANelvASFTlGGG 301
Cdd:cd07112 192 HTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLK-RVWLECGGKSPNIVFADApdLDAAAEAAAA---GIFW-NQG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 302 QFCTRPGLILALRGAgLERFKSALCAAVAGSTPQVLLNAPTlqhyrqGVAALAVHPRIEKLASGIAAGAGQAQTLLW--- 378
Cdd:cd07112 267 EVCSAGSRLLVHESI-KDEFLEKVVAAAREWKPGDPLDPAT------RMGALVSEAHFDKVLGYIESGKAEGARLVAggk 339
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 915779292 379 --QAQVEDLLAQDTLL----------QTEVFGPLSLLVEVDDVAQ 411
Cdd:cd07112 340 rvLTETGGFFVEPTVFdgvtpdmriaREEIFGPVLSVITFDSEEE 384
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
153-314 |
3.73e-13 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 72.31 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 153 LGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKAhpghmatAE---LTAEAIVRAVVRCGLPGGVFNMIFGT--DIG 227
Cdd:PRK11809 769 LGPVVCISPWNFPLAIFT--GQVAAALAAGNSVLAKP-------AEqtpLIAAQAVRILLEAGVPAGVVQLLPGRgeTVG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 228 AELVRHPAIQAVGFTGSLAGGKALYQLAQQR--PQ--PIPLFAEMSAINPLIILPQALqtrAEALANELVASFTLGGGQF 303
Cdd:PRK11809 840 AALVADARVRGVMFTGSTEVARLLQRNLAGRldPQgrPIPLIAETGGQNAMIVDSSAL---TEQVVADVLASAFDSAGQR 916
|
170
....*....|.
gi 915779292 304 CTrpglilALR 314
Cdd:PRK11809 917 CS------ALR 921
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
63-314 |
4.24e-13 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 72.20 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 63 SQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGErartsgqLRMFADvILRgdTFAARIDTALADRQPLP 142
Cdd:PRK11905 607 SATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE-------VREAVD-FLR--YYAAQARRLLNGPGHKP 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 143 RpdlrqyqqalGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKahPghmatAELT----AEAiVRAVVRCGLPGGVF 218
Cdd:PRK11905 677 L----------GPVVCISPWNFPLAIFT--GQIAAALVAGNTVLAK--P-----AEQTpliaARA-VRLLHEAGVPKDAL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 219 NMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALY-QLAQQRPQPIPLFAEMSAINPLIILPQALqtrAEALANELVAS 295
Cdd:PRK11905 737 QLLPGDgrTVGAALVADPRIAGVMFTGSTEVARLIQrTLAKRSGPPVPLIAETGGQNAMIVDSSAL---PEQVVADVIAS 813
|
250
....*....|....*....
gi 915779292 296 FTLGGGQFCTrpglilALR 314
Cdd:PRK11905 814 AFDSAGQRCS------ALR 826
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
153-305 |
4.28e-13 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 71.53 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 153 LGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKahPGHMATAelTAEAIVRAVVRCGLPGGVFNMIFG-TDIGAELV 231
Cdd:PRK09457 135 HGVVAVFGPYNFPGHLPN--GHIVPALLAGNTVVFK--PSELTPW--VAELTVKLWQQAGLPAGVLNLVQGgRETGKALA 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915779292 232 RHPAIQAVGFTGSLAGGKALYQLAQQRPQPIpLFAEMSAINPLIILPQALqtrAEALANELVASFTLGGGQFCT 305
Cdd:PRK09457 209 AHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-LALEMGGNNPLVIDEVAD---IDAAVHLIIQSAFISAGQRCT 278
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
151-305 |
4.81e-13 |
|
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: 71.48 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 151 QALGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKAhpghmatAELTAEAIVRAV---VRCGLPGGVFNMIFG--TD 225
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFT--GQISAALAAGNTVIAKP-------AEQTSLIAYRAVelmQEAGFPAGTIQLLPGrgAD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 226 IGAELVRHPAIQAVGFTGSLAGGKALYQ-LAQQRPQPIPLFAEMSAINPLIILPQALqtrAEALANELVASFTLGGGQFC 304
Cdd:TIGR01238 230 VGAALTSDPRIAGVAFTGSTEVAQLINQtLAQREDAPVPLIAETGGQNAMIVDSTAL---PEQVVRDVLRSAFDSAGQRC 306
|
.
gi 915779292 305 T 305
Cdd:TIGR01238 307 S 307
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
69-452 |
5.67e-13 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 71.27 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 69 QRAHFLCAIADELDALGEPFFAIAgqetalplarlqgerARTSGQLRMFADVILRGDTFA----ARIDTALADRQPLP-- 142
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIA---------------TANSGTTRNDSAVDIDGGIFTlgyyAKLGAALGDARLLRdg 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 143 ------RPDLRQYQQALGP---VAVF-GASNFPlafstAGG---DTASALAAGCPVVVKahPGhMATAELTAEaIVRAVV 209
Cdd:PRK11903 129 eavqlgKDPAFQGQHVLVPtrgVALFiNAFNFP-----AWGlweKAAPALLAGVPVIVK--PA-TATAWLTQR-MVKDVV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 210 RCG-LPGGVFNMIFGTdiGAELVRH-PAIQAVGFTGSLAGGKALYQLAQQRPQPIPLFAEMSAINPLIILPQALQTRAE- 286
Cdd:PRK11903 200 AAGiLPAGALSVVCGS--SAGLLDHlQPFDVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADSLNSALLGPDAAPGSEAf 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 287 -ALANELVASFTLGGGQFCTRPGLILALRGAgLERFKSALCAAVAGST---PQ-------VLLNAPTLQHYRQGVAALAV 355
Cdd:PRK11903 278 dLFVKEVVREMTVKSGQKCTAIRRIFVPEAL-YDAVAEALAARLAKTTvgnPRndgvrmgPLVSRAQLAAVRAGLAALRA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 356 HP-------RIEKLASGIAAGAGQAQTLLwqaQVEDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKALQGQLTATLH 428
Cdd:PRK11903 357 QAevlfdggGFALVDADPAVAACVGPTLL---GASDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVY 433
|
410 420
....*....|....*....|....
gi 915779292 429 aeADDGPLAASLLPLLCEKAGRVL 452
Cdd:PRK11903 434 --SDDAAFLAAAALELADSHGRVH 455
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
61-280 |
6.88e-13 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 70.90 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 61 VYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPL-ARLQGERARTSGQLRMF---ADVIlRGDTFAARIDT-AL 135
Cdd:cd07144 61 WWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYagwADKI-QGKTIPTSPNKlAY 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 136 ADRQPLprpdlrqyqqalGPVAVFGASNFPLAFstAGGDTASALAAGCPVVVKahpghmaTAELTAEAIV---RAVVRCG 212
Cdd:cd07144 140 TLHEPY------------GVCGQIIPWNYPLAM--AAWKLAPALAAGNTVVIK-------PAENTPLSLLyfaNLVKEAG 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 213 LPGGVFNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQA 280
Cdd:cd07144 199 FPPGVVNIIpgYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTL--ECGGKSPALVFEDA 266
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
95-429 |
1.11e-12 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 70.32 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 95 ETALPLARLQGERARTSGQLRMFADVILR--GDTFaaridtaladrqPLPRPDLRQY--QQALGPVAVFGASNFPLAFST 170
Cdd:PRK11241 97 EQGKPLAEAKGEISYAASFIEWFAEEGKRiyGDTI------------PGHQADKRLIviKQPIGVTAAITPWNFPAAMIT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 171 AggDTASALAAGCPVVVKAhpghMATAELTAEAIVRAVVRCGLPGGVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGG 248
Cdd:PRK11241 165 R--KAGPALAAGCTMVLKP----ASQTPFSALALAELAIRAGIPAGVFNVVTGSagAVGGELTSNPLVRKLSFTGSTEIG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 249 KALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAEALAnelVASFTLGGGQFCTRPGLILALRGAgLERFKSALCAA 328
Cdd:PRK11241 239 RQLMEQCAKDIKKVSL--ELGGNAPFIVFDDADLDKAVEGA---LASKFRNAGQTCVCANRLYVQDGV-YDRFAEKLQQA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 329 VA----------GSTPQVLLNAPTLQHYRQGVAalavhPRIEKLASGIAAGAGQAQ--TLLWQAQVEDLLAQDTLLQTEV 396
Cdd:PRK11241 313 VSklhigdglekGVTIGPLIDEKAVAKVEEHIA-----DALEKGARVVCGGKAHELggNFFQPTILVDVPANAKVAKEET 387
|
330 340 350
....*....|....*....|....*....|...
gi 915779292 397 FGPLSLLVEVDDVAQLQAVVKALQGQLTATLHA 429
Cdd:PRK11241 388 FGPLAPLFRFKDEADVIAQANDTEFGLAAYFYA 420
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
151-275 |
2.11e-12 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 69.97 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 151 QALGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKahPghmatAE---LTAEAIVRAVVRCGLPGGVFNMIFGT--D 225
Cdd:COG4230 679 RGRGVFVCISPWNFPLAIFT--GQVAAALAAGNTVLAK--P-----AEqtpLIAARAVRLLHEAGVPADVLQLLPGDgeT 749
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 915779292 226 IGAELVRHPAIQAVGFTGSLAGGKALY-QLAQQRPQPIPLFAEMSAINPLI 275
Cdd:COG4230 750 VGAALVADPRIAGVAFTGSTETARLINrTLAARDGPIVPLIAETGGQNAMI 800
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
135-314 |
6.44e-12 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 68.30 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 135 LADRQPLPRPDLRQYQQALGPVAVFGA-S--NFPLAFSTagGDTASALAAGCPVVVKahPghmatAE---LTAEAIVRAV 208
Cdd:PRK11904 664 FGAPEKLPGPTGESNELRLHGRGVFVCiSpwNFPLAIFL--GQVAAALAAGNTVIAK--P-----AEqtpLIAAEAVKLL 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 209 VRCGLPGGVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQ-LAQQRPQPIPLFAEMSAINPLIILPQALqtrA 285
Cdd:PRK11904 735 HEAGIPKDVLQLLPGDgaTVGAALTADPRIAGVAFTGSTETARIINRtLAARDGPIVPLIAETGGQNAMIVDSTAL---P 811
|
170 180 190
....*....|....*....|....*....|
gi 915779292 286 EALANELVAS-FTlGGGQFCTrpglilALR 314
Cdd:PRK11904 812 EQVVDDVVTSaFR-SAGQRCS------ALR 834
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
145-304 |
6.86e-12 |
|
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: 67.54 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 145 DLRQYQQALGPVAVFGASNFP----LAFstaggdTASALAAGCPVVVKAH---PG-HMATAELTAEAivravvrcGLPGG 216
Cdd:cd07085 129 DTYSYRQPLGVVAGITPFNFPamipLWM------FPMAIACGNTFVLKPServPGaAMRLAELLQEA--------GLPDG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 217 VFNMIFGT-DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQ---RPQpiplfAEMSAINPLIILPQAlqtRAEALANEL 292
Cdd:cd07085 195 VLNVVHGGkEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAngkRVQ-----ALGGAKNHAVVMPDA---DLEQTANAL 266
|
170
....*....|..
gi 915779292 293 VASFTLGGGQFC 304
Cdd:cd07085 267 VGAAFGAAGQRC 278
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
61-411 |
1.32e-11 |
|
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: 66.47 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 61 VYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILR--GDTF------AARID 132
Cdd:cd07149 36 EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKRlaGETIpfdaspGGEGR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 133 TALADRQPLprpdlrqyqqalGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHPghmaTAELTAEAIVRAVVRCG 212
Cdd:cd07149 116 IGFTIREPI------------GVVAAITPFNFPL--NLVAHKVGPAIAAGNAVVLKPAS----QTPLSALKLAELLLEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 213 LPGGVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRpqpiPLFAEMSAINPLIILPQA-LQTRAEALA 289
Cdd:cd07149 178 LPKGALNVVTGSgeTVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK----KVTLELGSNAAVIVDADAdLEKAVERCV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 290 NelvASFTlGGGQFCTRPGLIL---ALRGAGLERFKSALCAAVAGStpqvllnaPTLQHYRQG-VAALAVHPRIEK-LAS 364
Cdd:cd07149 254 S---GAFA-NAGQVCISVQRIFvheDIYDEFLERFVAATKKLVVGD--------PLDEDTDVGpMISEAEAERIEEwVEE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 915779292 365 GIAAGA-----GQAQ-TLLWQAQVEDLLAQDTLLQTEVFGPLSLLVEVDDVAQ 411
Cdd:cd07149 322 AVEGGArlltgGKRDgAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDE 374
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
147-408 |
1.46e-11 |
|
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: 66.56 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 147 RQYQQALGPVAVFGASNFPLAFSTAGgdTASALAAGCPVVVKAHP-----GHMATAELTAEAivravvrcGLPGGVFNMI 221
Cdd:cd07151 125 RVYREPLGVVGVISPWNFPLHLSMRS--VAPALALGNAVVLKPASdtpitGGLLLAKIFEEA--------GLPKGVLNVV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 222 FG--TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAEALAneLVASFtLG 299
Cdd:cd07151 195 VGagSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVAL--ELGGNNPFVVLEDADIDAAVNAA--VFGKF-LH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 300 GGQFCTRPGLIL---ALRGAGLERFKSALCAAVAG--STPQVLlnaptlqhyrqgVAALAVHPRIEKLASGIAAGAGQAQ 374
Cdd:cd07151 270 QGQICMAINRIIvheDVYDEFVEKFVERVKALPYGdpSDPDTV------------VGPLINESQVDGLLDKIEQAVEEGA 337
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 915779292 375 TLLWQAQVEDLLAQDTLL----------QTEVFGPLSLLVEVDD 408
Cdd:cd07151 338 TLLVGGEAEGNVLEPTVLsdvtndmeiaREEIFGPVAPIIKADD 381
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
154-254 |
2.93e-11 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 65.49 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 154 GPVAVFGA---SNFPLAFSTagGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAvvrcGLPGGVFNMIFGT-DIGAE 229
Cdd:cd07111 146 KPVGVVGQivpWNFPLLMLA--WKICPALAMGNTVVLKPAEYTPLTALLFAEICAEA----GLPPGVLNIVTGNgSFGSA 219
|
90 100
....*....|....*....|....*
gi 915779292 230 LVRHPAIQAVGFTGSLAGGKALYQL 254
Cdd:cd07111 220 LANHPGVDKVAFTGSTEVGRALRRA 244
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
155-257 |
4.69e-11 |
|
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: 64.92 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 155 PVAVFGAS---NFPL---AFSTAggdtaSALAAGCPVVVKahpghmaTAE---LTAEAIVRAVVRCGLPGGVFNMI--FG 223
Cdd:cd07091 141 PIGVCGQIipwNFPLlmlAWKLA-----PALAAGNTVVLK-------PAEqtpLSALYLAELIKEAGFPPGVVNIVpgFG 208
|
90 100 110
....*....|....*....|....*....|....
gi 915779292 224 TDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQ 257
Cdd:cd07091 209 PTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
62-255 |
5.47e-11 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 64.96 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILRgdtfaaridtaLADRQPL 141
Cdd:PRK03137 89 WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-----------LADGKPV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 142 -PRP--DLRQYQQALGPVAVFGASNFPLAFSTagGDTASALAAGCPVVVKahPGhmATAELTAEAIVRAVVRCGLPGGVF 218
Cdd:PRK03137 158 eSRPgeHNRYFYIPLGVGVVISPWNFPFAIMA--GMTLAAIVAGNTVLLK--PA--SDTPVIAAKFVEVLEEAGLPAGVV 231
|
170 180 190
....*....|....*....|....*....|....*....
gi 915779292 219 NMIFGTD--IGAELVRHPAIQAVGFTGSLAGGKALYQLA 255
Cdd:PRK03137 232 NFVPGSGseVGDYLVDHPKTRFITFTGSREVGLRIYERA 270
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
118-305 |
7.72e-11 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 64.52 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 118 ADVIlrgDTFAARIDTALADRQPLpRPDLRQY--QQALGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHP---- 191
Cdd:PRK13252 110 ADVL---EYYAGLAPALEGEQIPL-RGGSFVYtrREPLGVCAGIGAWNYPI--QIACWKSAPALAAGNAMIFKPSEvtpl 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 192 GHMATAELTAEAivravvrcGLPGGVFNMIFGT-DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSA 270
Cdd:PRK13252 184 TALKLAEIYTEA--------GLPDGVFNVVQGDgRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTM--ELGG 253
|
170 180 190
....*....|....*....|....*....|....*
gi 915779292 271 INPLIILPQALQTRAEALAneLVASFtLGGGQFCT 305
Cdd:PRK13252 254 KSPLIVFDDADLDRAADIA--MLANF-YSSGQVCT 285
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
158-411 |
1.63e-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: 63.65 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 158 VFGASNFPlAFSTAGGDTASaLAAGCPVVVKAHPGHMATAELTAEaIVRAVV-RCGL-PGGVFNMIF--GTDIGAELVRH 233
Cdd:cd07127 199 VIGCSTFP-TWNGYPGLFAS-LATGNPVIVKPHPAAILPLAITVQ-VAREVLaEAGFdPNLVTLAADtpEEPIAQTLATR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 234 PAIQAVGFTGSLAGGKALYQLAQQRpqpiPLFAEMSAINPLIIlpqALQTRAEALANELVASFTLGGGQFCTRPGLILAL 313
Cdd:cd07127 276 PEVRIIDFTGSNAFGDWLEANARQA----QVYTEKAGVNTVVV---DSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVP 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 314 RgAGLE-----RFKSALCAAVAGSTPQVLLNAPTLQHYRQGVAALAVHPRIEKLASG---IAAGAGQAQTLLWQAQVEDL 385
Cdd:cd07127 349 R-DGIQtddgrKSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLgevLLASEAVAHPEFPDARVRTP 427
|
250 260 270
....*....|....*....|....*....|..
gi 915779292 386 L------AQDTLLQTEVFGPLSLLVEVDDVAQ 411
Cdd:cd07127 428 LllkldaSDEAAYAEERFGPIAFVVATDSTDH 459
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-280 |
2.85e-10 |
|
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: 62.47 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 12 FIAGRRI-ASGEATLLSLRAVDGEATGHrFYPASREEAALAAEAAQQAFAVYSQTTPQQRAHFLCAIADELDALGEPFFA 90
Cdd:cd07117 4 FINGEWVkGSSGETIDSYNPANGETLSE-ITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 91 IAGQETALPLARLQG-ERARTSGQLRMFADVILRGDTFAARIDT---ALADRQPlprpdlrqyqqaLGPVAVFGASNFPl 166
Cdd:cd07117 83 VETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEdtlSIVLREP------------IGVVGQIIPWNFP- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 167 aFSTAGGDTASALAAGCPVVVkaHPGHMATAELTAEAIVRAVVrcgLPGGVFNMI--FGTDIGAELVRHPAIQAVGFTGS 244
Cdd:cd07117 150 -FLMAAWKLAPALAAGNTVVI--KPSSTTSLSLLELAKIIQDV---LPKGVVNIVtgKGSKSGEYLLNHPGLDKLAFTGS 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 915779292 245 LAGGKALYQLAQQRpqPIPLFAEMSAINPLIILPQA 280
Cdd:cd07117 224 TEVGRDVAIAAAKK--LIPATLELGGKSANIIFDDA 257
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
147-304 |
3.84e-10 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 61.94 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 147 RQYQQALGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHpghMATAeLTAEAIVRAVVRCGLPGGVFNMIFG--T 224
Cdd:cd07101 113 TVNRRPKGVVGVISPWNYPL--TLAVSDAIPALLAGNAVVLKPD---SQTA-LTALWAVELLIEAGLPRDLWQVVTGpgS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 225 DIGAELVRHpaIQAVGFTGSLAGGKALYQLAQQRpqPIPLFAEMSAINPLIILPQALQTRAEALAneLVASFTlGGGQFC 304
Cdd:cd07101 187 EVGGAIVDN--ADYVMFTGSTATGRVVAERAGRR--LIGCSLELGGKNPMIVLEDADLDKAAAGA--VRACFS-NAGQLC 259
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
63-416 |
5.82e-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: 61.49 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 63 SQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADVILRGDTFAARIDT--------A 134
Cdd:cd07147 38 RALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIYGEVLPLDIsargegrqG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 135 LADRQPLprpdlrqyqqalGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVRAvvrcGLP 214
Cdd:cd07147 118 LVRRFPI------------GPVSAITPFNFPL--NLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAET----GLP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 215 GGVFNMI-FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRpqpiPLFAEMSAINPLIILPQALQTRaeALANELV 293
Cdd:cd07147 180 KGAFSVLpCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK----KVVLELGGNAAVIVDSDADLDF--AAQRIIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 294 ASFTlGGGQFCTRPGLILALRgAGLERFKSALCAAVA----------GSTPQVLLNAPTLQHYRQGVAAlAVHPRIEKLA 363
Cdd:cd07147 254 GAFY-QAGQSCISVQRVLVHR-SVYDEFKSRLVARVKalktgdpkddATDVGPMISESEAERVEGWVNE-AVDAGAKLLT 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 915779292 364 SGIAAGAGQAQTLLwqaqvEDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVV 416
Cdd:cd07147 331 GGKRDGALLEPTIL-----EDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAV 378
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
62-304 |
9.68e-10 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 60.91 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 62 YSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLARLQGERARTSGQLRMFADvilRGDTFAARiDTALADRQPL 141
Cdd:PRK09406 39 YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAE---HAEALLAD-EPADAAAVGA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 142 PRPDLRqyQQALGPVAVFGASNFPLAfsTAGGDTASALAAGCPVVVKaHPGHMATAELTAEAIVRavvRCGLPGGVF-NM 220
Cdd:PRK09406 115 SRAYVR--YQPLGVVLAVMPWNFPLW--QVVRFAAPALMAGNVGLLK-HASNVPQTALYLADLFR---RAGFPDGCFqTL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 221 IFGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAEALAnelVASFTLGG 300
Cdd:PRK09406 187 LVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVL--ELGGSDPFIVMPSADLDRAAETA---VTARVQNN 261
|
....
gi 915779292 301 GQFC 304
Cdd:PRK09406 262 GQSC 265
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
151-417 |
1.30e-09 |
|
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: 60.31 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 151 QALGPVAVFGASNFPlaFSTAGGDTASALAAGCPVVVKahPGHMA--TAELTAEaIVR--------AVVRcglpGGV--- 217
Cdd:cd07135 107 EPLGVVLIIGPWNYP--VLLALSPLVGAIAAGCTVVLK--PSELTphTAALLAE-LVPkyldpdafQVVQ----GGVpet 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 218 -------FNMIFgtdigaelvrhpaiqavgFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALAN 290
Cdd:cd07135 178 talleqkFDKIF------------------YTGSGRVGRIIAEAAAKHLTPVTL--ELGGKSPVIVTKNA---DLELAAK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 291 ELVASFTLGGGQFCTRPGLILA---LRGAGLERFKSALCAAVagstPQVLLNAPTLQHyrqgvaalAVHP----RIEKLA 363
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVdpsVYDEFVEELKKVLDEFY----PGGANASPDYTR--------IVNPrhfnRLKSLL 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 364 SG-----IAAGAGQAQTLLWQAQ-VEDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVK 417
Cdd:cd07135 303 DTtkgkvVIGGEMDEATRFIPPTiVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVIN 362
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
147-304 |
3.28e-09 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 59.12 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 147 RQYQQALGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHPghmATAeLTAEAIVRAVVRCGLPGGVFNMIFG--T 224
Cdd:PRK09407 149 TELRQPKGVVGVISPWNYPL--TLAVSDAIPALLAGNAVVLKPDS---QTP-LTALAAVELLYEAGLPRDLWQVVTGpgP 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 225 DIGAELVRHpaIQAVGFTGSLAGGKALYQLAQQRpqPIPLFAEMSAINPLIILPQALQTRAEALAneLVASFTlGGGQFC 304
Cdd:PRK09407 223 VVGTALVDN--ADYLMFTGSTATGRVLAEQAGRR--LIGFSLELGGKNPMIVLDDADLDKAAAGA--VRACFS-NAGQLC 295
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
136-400 |
6.95e-09 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 57.82 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 136 ADRqplPRPDLRQYQQALGPVAVFGASNFPlaFSTAGGDTASALAAGCPVVVKAhpghmatAELT---AEAIVRAVVRCG 212
Cdd:PRK10090 58 SDR---PGENILLFKRALGVTTGILPWNFP--FFLIARKMAPALLTGNTIVIKP-------SEFTpnnAIAFAKIVDEIG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 213 LPGGVFNMIFGT--DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQAlqtRAEALAN 290
Cdd:PRK10090 126 LPKGVFNLVLGRgeTVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCL--ELGGKAPAIVMDDA---DLDLAVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 291 ELVASFTLGGGQFCT---RPGLILALRGAGLERFKSALCAAVAGSTPQ-------VLLNAPTLQHYRQGVA-ALAVHPRI 359
Cdd:PRK10090 201 AIVDSRVINSGQVCNcaeRVYVQKGIYDQFVNRLGEAMQAVQFGNPAErndiamgPLINAAALERVEQKVArAVEEGARV 280
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 915779292 360 EkLASGIAAGAGQ--AQTLLwqaqvEDLLAQDTLLQTEVFGPL 400
Cdd:PRK10090 281 A-LGGKAVEGKGYyyPPTLL-----LDVRQEMSIMHEETFGPV 317
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
153-408 |
1.51e-08 |
|
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: 56.77 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 153 LGPVAVFGASNFP--LAFSTAggdtASALAAGCPVVVKA--HPGHMAT--AELTAEAIVRAVVRCgLPGGVfnmifgtDI 226
Cdd:cd07087 101 LGVVLIIGPWNYPlqLALAPL----IGAIAAGNTVVLKPseLAPATSAllAKLIPKYFDPEAVAV-VEGGV-------EV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 227 GAELVRHPaIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAealANELVASFTLGGGQFCTR 306
Cdd:cd07087 169 ATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTL--ELGGKSPCIVDKDANLEVA---ARRIAWGKFLNAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 307 PGLILALRGAgLERFKSALCAAVA---GSTPQvllNAPTL------QHYRqgvaalavhpRIEKLASG--IAAGaGQ--- 372
Cdd:cd07087 243 PDYVLVHESI-KDELIEELKKAIKefyGEDPK---ESPDYgriineRHFD----------RLASLLDDgkVVIG-GQvdk 307
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 915779292 373 -----AQTLLWQAQVEDLLAQDtllqtEVFGPLSLLVEVDD 408
Cdd:cd07087 308 eeryiAPTILDDVSPDSPLMQE-----EIFGPILPILTYDD 343
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
147-304 |
1.84e-08 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 56.75 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 147 RQYQ-----QALGPVAVFGASNFP-LAFSTAggdTASALAAGCPVVVKAhpghmatAE---LTAEAIVRAVVRCGLPGGV 217
Cdd:PLN02766 148 RQLQgytlkEPIGVVGHIIPWNFPsTMFFMK---VAPALAAGCTMVVKP-------AEqtpLSALFYAHLAKLAGVPDGV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 218 FNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQlAQQRPQPIPLFAEMSAINPLIILPQALQTRAEALAneLVAS 295
Cdd:PLN02766 218 INVVtgFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ-AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLA--LLGI 294
|
....*....
gi 915779292 296 FTlGGGQFC 304
Cdd:PLN02766 295 FY-NKGEIC 302
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
155-255 |
2.34e-08 |
|
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: 56.38 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 155 PVAVFGAS---NFPLAFSTagGDTASALAAGCPVVVKahpghmaTAELT---AEAIVRAVVRCGLPGGVFNMI--FGTDI 226
Cdd:cd07143 144 PIGVCGQIipwNFPLLMCA--WKIAPALAAGNTIVLK-------PSELTplsALYMTKLIPEAGFPPGVINVVsgYGRTC 214
|
90 100
....*....|....*....|....*....
gi 915779292 227 GAELVRHPAIQAVGFTGSLAGGKALYQLA 255
Cdd:cd07143 215 GNAISSHMDIDKVAFTGSTLVGRKVMEAA 243
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
61-400 |
3.22e-08 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 56.06 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 61 VYSQTTPQQRAHFLCAIADELDALGEPFFAIAGQETALPLAR-LQGERARTSGQLRMFADVIlrgDTFAARIDT------ 133
Cdd:PRK09847 74 DWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHsLRDDIPGAARAIRWYAEAI---DKVYGEVATtsshel 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 134 ALADRQPLprpdlrqyqqalGPVAVFGASNFPLAFstAGGDTASALAAGCPVVVKAHpghmATAELTAEAIVRAVVRCGL 213
Cdd:PRK09847 151 AMIVREPV------------GVIAAIVPWNFPLLL--TCWKLGPALAAGNSVILKPS----EKSPLSAIRLAGLAKEAGL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 214 PGGVFNMI--FGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLA-QQRPQPIPLFAEMSAINPLIILPQALQTRAEALAn 290
Cdd:PRK09847 213 PDGVLNVVtgFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSANIVFADCPDLQQAASATA- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 291 elvASFTLGGGQFCTrPGLILALRGAGLERFKSALCAAVAGSTPQVLLNAPTLqhyrqgVAALAVHPRIEKLASGIAAGA 370
Cdd:PRK09847 292 ---AGIFYNQGQVCI-AGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT------MGTLIDCAHADSVHSFIREGE 361
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 915779292 371 GQAQTLL------WQAQV-----EDLLAQDTLLQTEVFGPL 400
Cdd:PRK09847 362 SKGQLLLdgrnagLAAAIgptifVDVDPNASLSREEIFGPV 402
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
150-276 |
7.50e-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: 54.81 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 150 QQALGPVAVFGASNFPLAFstAGGDTASALAAGCPVVVKahPGHmaTAELTAEAIVRAVVRCGLPGGVFNMI--FGTDIG 227
Cdd:cd07140 145 REPIGVCGIVIPWNYPLMM--LAWKMAACLAAGNTVVLK--PAQ--VTPLTALKFAELTVKAGFPKGVINILpgSGSLVG 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 915779292 228 AELVRHPAIQAVGFTGSLAGGKALYQ-LAQQRPQPIPLfaEMSAINPLII 276
Cdd:cd07140 219 QRLSDHPDVRKLGFTGSTPIGKHIMKsCAVSNLKKVSL--ELGGKSPLII 266
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
153-418 |
6.74e-07 |
|
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: 51.92 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 153 LGPVAVFGASNFPlaFSTAGGDTASALAAGCPVVVKAhpghmatAELTA------EAIVRAVVR-CGLPGGVFNMIFGT- 224
Cdd:cd07098 121 LGVVGAIVSWNYP--FHNLLGPIIAALFAGNAIVVKV-------SEQVAwssgffLSIIRECLAaCGHDPDLVQLVTCLp 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 225 DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQrpQPIPLFAEMSAINPLIILPQAlqtRAEALANELVASFTLGGGQFC 304
Cdd:cd07098 192 ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAE--SLTPVVLELGGKDPAIVLDDA---DLDQIASIIMRGTFQSSGQNC 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 305 trpglilalrgAGLERF------KSALCAAVAGSTPQVLLNAPTLQHYRQGvaALAVHPRIEKLASGIAAGAGQAQTLLW 378
Cdd:cd07098 267 -----------IGIERVivhekiYDKLLEILTDRVQALRQGPPLDGDVDVG--AMISPARFDRLEELVADAVEKGARLLA 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 915779292 379 -------QAQVEDLLAQDTLL----------QTEVFGPLSLLVEVDDVAQLQAVVKA 418
Cdd:cd07098 334 ggkryphPEYPQGHYFPPTLLvdvtpdmkiaQEEVFGPVMVVMKASDDEEAVEIANS 390
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
140-305 |
7.94e-06 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 48.29 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 140 PLPRPD--LRQYQQALGPVAVFGASNFPLAfsTAGGDTASALAAGCPVVVKAHPG----HMATAELTAEAIVRAvvrcGL 213
Cdd:PLN02315 140 PSERPNhmMMEVWNPLGIVGVITAFNFPCA--VLGWNACIALVCGNCVVWKGAPTtpliTIAMTKLVAEVLEKN----NL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 214 PGGVFN-MIFGTDIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQA-LQTRAEALANE 291
Cdd:PLN02315 214 PGAIFTsFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLL--ELSGNNAIIVMDDAdIQLAVRSVLFA 291
|
170
....*....|....
gi 915779292 292 LVASftlgGGQFCT 305
Cdd:PLN02315 292 AVGT----AGQRCT 301
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
153-417 |
1.66e-05 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 47.33 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 153 LGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKAHPGHMATAELTAEAIVR----AVVRCgLPGGVfnmifgtDIGA 228
Cdd:PTZ00381 110 LGVVLVIGAWNYPL--NLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKyldpSYVRV-IEGGV-------EVTT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 229 ELVRHPaIQAVGFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQALQTRAealANELVASFTLGGGQFCTRPG 308
Cdd:PTZ00381 180 ELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTL--ELGGKSPVIVDKSCNLKVA---ARRIAWGKFLNAGQTCVAPD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 309 LILaLRGAGLERFKSALCAAVA---GSTPQvllnapTLQHYRQGVAALAvhprIEKLASGIAAGAGQ------------- 372
Cdd:PTZ00381 254 YVL-VHRSIKDKFIEALKEAIKeffGEDPK------KSEDYSRIVNEFH----TKRLAELIKDHGGKvvyggevdienky 322
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 915779292 373 -AQTLLWQAQVEDLLAQDtllqtEVFGPLSLLVEVDDvaqLQAVVK 417
Cdd:PTZ00381 323 vAPTIIVNPDLDSPLMQE-----EIFGPILPILTYEN---IDEVLE 360
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
151-400 |
1.06e-04 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 44.78 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 151 QALGPVAVFGASNFPLAFSTAGgdTASALAAGCPVVVKahpghM-----ATAELTAEAIVR-------AVVRcglpGGVf 218
Cdd:cd07133 100 QPLGVVGIIVPWNYPLYLALGP--LIAALAAGNRVMIK-----PseftpRTSALLAELLAEyfdedevAVVT----GGA- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 219 nmifgtDIGAELVRHPAIQAVgFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQA-LQTRAEALAnelvASFT 297
Cdd:cd07133 168 ------DVAAAFSSLPFDHLL-FTGSTAVGRHVMRAAAENLTPVTL--ELGGKSPAIIAPDAdLAKAAERIA----FGKL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 298 LGGGQFCTRPGLILALRGAgLERFKSALCAAVAGSTPQVLLNaPT------------LQHY-----RQGVAALAVHPrie 360
Cdd:cd07133 235 LNAGQTCVAPDYVLVPEDK-LEEFVAAAKAAVAKMYPTLADN-PDytsiinerhyarLQGLledarAKGARVIELNP--- 309
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 915779292 361 klaSGIAAGAGQ--AQTLLWQAQVEDLLAQDtllqtEVFGPL 400
Cdd:cd07133 310 ---AGEDFAATRklPPTLVLNVTDDMRVMQE-----EIFGPI 343
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
197-304 |
4.17e-04 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 43.20 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 197 AELTAEAivravvrcGLPGGVFNMIFGT-DIGAELVRHPAIQAVGFTGSLAGGKALYQLAQQRPQPIPlfAEMSAINPLI 275
Cdd:PLN02419 296 AELAMEA--------GLPDGVLNIVHGTnDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQ--SNMGAKNHGL 365
|
90 100
....*....|....*....|....*....
gi 915779292 276 ILPQAlqtRAEALANELVASFTLGGGQFC 304
Cdd:PLN02419 366 VLPDA---NIDATLNALLAAGFGAAGQRC 391
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
153-341 |
4.43e-04 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 42.82 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 153 LGPVAVFGASNFP--LAFSTaggdTASALAAGCPVVVKAhPGHMATAELTaeaIVRAVVRCGLPGGVFNMIFG--TDIGA 228
Cdd:PLN00412 159 LGVVLAIPPFNYPvnLAVSK----IAPALIAGNAVVLKP-PTQGAVAALH---MVHCFHLAGFPKGLISCVTGkgSEIGD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 229 ELVRHPAIQAVGFTGSlAGGKALYQLAQQrpqpIPLFAEMSAINPLIILPQAlqtraealANELVASFTLGG-----GQF 303
Cdd:PLN00412 231 FLTMHPGVNCISFTGG-DTGIAISKKAGM----VPLQMELGGKDACIVLEDA--------DLDLAAANIIKGgfsysGQR 297
|
170 180 190
....*....|....*....|....*....|....*...
gi 915779292 304 CTRPGLILAlrgagLERFKSALCAAVAGSTPQVLLNAP 341
Cdd:PLN00412 298 CTAVKVVLV-----MESVADALVEKVNAKVAKLTVGPP 330
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
151-418 |
1.87e-03 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 40.67 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 151 QALGPVAVFGASNFPlaFSTAGGDTASALAAGCPVVVKahpghmaTAELT--AEAIVRAVVRCGLP--------GGV--- 217
Cdd:cd07134 99 EPKGVCLIISPWNYP--FNLAFGPLVSAIAAGNTAILK-------PSELTphTSAVIAKIIREAFDedevavfeGDAeva 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 218 -------FNMIFgtdigaelvrhpaiqavgFTGSLAGGKALYQLAQQRPQPIPLfaEMSAINPLIILPQA-LQTRAEALA 289
Cdd:cd07134 170 qallelpFDHIF------------------FTGSPAVGKIVMAAAAKHLASVTL--ELGGKSPTIVDETAdLKKAAKKIA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 290 nelVASFtLGGGQFCTRPGLILALRgAGLERFKSALCAAVA---GSTPQVLLNAptlqHYRQGVAALAvHPRIEKLAS-G 365
Cdd:cd07134 230 ---WGKF-LNAGQTCIAPDYVFVHE-SVKDAFVEHLKAEIEkfyGKDAARKASP----DLARIVNDRH-FDRLKGLLDdA 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 915779292 366 IAAGA-----GQ---AQTLLWQAQVEDLLAQDTLLQTEVFGPLSLLVEVDDVAQLQAVVKA 418
Cdd:cd07134 300 VAKGAkvefgGQfdaAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINA 360
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
150-244 |
4.40e-03 |
|
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: 39.71 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779292 150 QQALGPVAVFGASNFPLafSTAGGDTASALAAGCPVVVKahPGhmATAELTAEAIVRAVVRCGLPGGVFNMIFGTDIGAE 229
Cdd:cd07148 122 REPIGVVVAISAFNHPL--NLIVHQVAPAIAAGCPVIVK--PA--LATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAE 195
|
90
....*....|....*.
gi 915779292 230 -LVRHPAIQAVGFTGS 244
Cdd:cd07148 196 kLVTDPRVAFFSFIGS 211
|
|
| |
