|
Name |
Accession |
Description |
Interval |
E-value |
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
1-517 |
0e+00 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 909.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 1 MPAPSAEVFDRLRNLAAIKDVAARPTRTIDEVFTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRD 80
Cdd:PRK09407 8 MPAPSALTFERLRRLTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 81 LVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLLKPRKAQPLLPGIGKTTVCYQPKGVVGVISPWNYP 160
Cdd:PRK09407 88 LVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAPRRRAGALPVLTKTTELRQPKGVVGVISPWNYP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 161 MTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLMFTGSSATGSRL 240
Cdd:PRK09407 168 LTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNADYLMFTGSTATGRVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 241 AEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTA 320
Cdd:PRK09407 248 AEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 321 YDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADV 400
Cdd:PRK09407 328 YDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 401 DEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQT 480
Cdd:PRK09407 408 DEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQT 487
|
490 500 510
....*....|....*....|....*....|....*..
gi 57116903 481 IATARVFNLDPPFGIPATVWQKSLLPIVRTVMKLPGR 517
Cdd:PRK09407 488 IATQRVLPLAPPPGMPYEKYAKLMLTGLRLMKKLRGR 524
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
30-483 |
0e+00 |
|
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: 792.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 30 DEVFTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIV 109
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 110 DLIANANYYARVCVDLLKPRKAQPLLPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC 189
Cdd:cd07101 81 DVAIVARYYARRAERLLKPRRRRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 190 ALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANL 269
Cdd:cd07101 161 ALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 270 DKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAK 349
Cdd:cd07101 241 DKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 350 GAKVIAGGKARPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRI 429
Cdd:cd07101 321 GATVLAGGRARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 57116903 430 AARLRSGTVNVDEGYAFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIAT 483
Cdd:cd07101 401 AARLRAGTVNVNEGYAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
10-482 |
3.81e-178 |
|
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: 509.28 E-value: 3.81e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 10 DRLRNLAAIKDVAARPTRTIDEV--FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENRE 87
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVInpATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 88 FLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLLKPRKAQPLLPGIGKTTvcYQPKGVVGVISPWNYPMTLTVSD 167
Cdd:COG1012 84 ELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVR--REPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 168 SVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAG 245
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHpdVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 246 RRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSV 325
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 326 DMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVE 405
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57116903 406 KANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAwgSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIA 482
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA--VPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
60-481 |
2.00e-168 |
|
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: 482.86 E-value: 2.00e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLLKPRKAQPLLPGig 139
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 140 KTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGT 219
Cdd:cd07078 89 LAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 220 AITDNC--DYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVE 297
Cdd:cd07078 169 ALASHPrvDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 298 KDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGPLFYEPTVLTNVA 377
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTVLTDVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 378 PEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAwgSLSAPMGG 457
Cdd:cd07078 329 PDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA--EPSAPFGG 406
|
410 420
....*....|....*....|....
gi 57116903 458 MGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07078 407 VKQSGIGREGGPYGLEEYTEPKTV 430
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
26-481 |
1.32e-157 |
|
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: 456.61 E-value: 1.32e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 26 TRTIDEV--FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWA 103
Cdd:pfam00171 6 SETIEVInpATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 104 AQEEIVDLIANANYYARVCvDLLKPRKAqPLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPD 183
Cdd:pfam00171 86 ARGEVDRAIDVLRYYAGLA-RRLDGETL-PSDPGRLAYTR-REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 184 SQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPM 261
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHpdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 262 IVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSG 341
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 342 HVDDATAKGAKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAG 421
Cdd:pfam00171 323 YVEDAKEEGAKLLTGGEAGLDNG-YFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTS 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 422 STAEGQRIAARLRSGTVNVDEGYAFAWGSLsaPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:pfam00171 402 DLERALRVARRLEAGMVWINDYTTGDADGL--PFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
34-483 |
1.05e-155 |
|
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: 451.29 E-value: 1.05e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07099 5 TGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYARVCVDLLKPRKAQ--PLLPGIgKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCAL 191
Cdd:cd07099 85 AIDWAARNAPRVLAPRKVPtgLLMPNK-KATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 192 ACAELLYRAGLPRALYAIVPGPGSVvGTAITDN-CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLD 270
Cdd:cd07099 164 LLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAgVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 271 KVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKG 350
Cdd:cd07099 243 RAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 351 AKVIAGGKaRPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIA 430
Cdd:cd07099 323 AKALTGGA-RSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 57116903 431 ARLRSGTVNVDEGYAFAwGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIAT 483
Cdd:cd07099 402 RRLEAGAVSINDVLLTA-GIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
34-482 |
2.60e-129 |
|
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: 384.09 E-value: 2.60e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKArWA-AQEEIVDLI 112
Cdd:cd07103 6 TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKP-LAeARGEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYA----RVCVDLLKPRKAQpllpgiGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPY 188
Cdd:cd07103 85 SFLEWFAeearRIYGRTIPSPAPG------KRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 189 CALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDY--LMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARG 266
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVrkISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 267 ANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDA 346
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 347 TAKGAKVIAGGKaRPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEG 426
Cdd:cd07103 319 VAKGAKVLTGGK-RLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 57116903 427 QRIAARLRSGTVNVDEGyafAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIA 482
Cdd:cd07103 398 WRVAEALEAGMVGINTG---LISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
60-481 |
8.70e-128 |
|
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: 376.95 E-value: 8.70e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLLKPRkaQPLLPGIG 139
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPE--LPSPDPGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 140 KTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGT 219
Cdd:cd06534 85 EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 220 AITDNC--DYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVE 297
Cdd:cd06534 165 ALLSHPrvDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 298 KDIAEEFTRKFGdavrnmklgtaydfsvdmgsliseaqlktvsghvddatakgakviaggkarpdigplfyepTVLTNVA 377
Cdd:cd06534 245 ESIYDEFVEKLV-------------------------------------------------------------TVLVDVD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 378 PEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFawGSLSAPMGG 457
Cdd:cd06534 264 PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG--VGPEAPFGG 341
|
410 420
....*....|....*....|....
gi 57116903 458 MGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
60-481 |
1.99e-124 |
|
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: 370.71 E-value: 1.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAG----KARWAAQEEIVDLIANANYYARVCVDLLkprkaQPLL 135
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGstrpKAAFEVGAAIAILREAAGLPRRPEGEIL-----PSDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 136 PGigKTTVCY-QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC-ALACAELLYRAGLPRALYAIVPGP 213
Cdd:cd07104 88 PG--KESMVRrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 214 GSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISI 291
Cdd:cd07104 166 GSEIGDALVEHPRVRMisFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 292 ERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARpdiGpLFYEPT 371
Cdd:cd07104 246 GRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE---G-LFYQPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 372 VLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSG-------TVNvDEGY 444
Cdd:cd07104 322 VLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGmvhindqTVN-DEPH 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 57116903 445 afawgslsAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07104 401 --------VPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
60-481 |
5.90e-117 |
|
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: 351.38 E-value: 5.90e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEiVDLIAN-ANYYARVCVDLLKPrkaQPLLPGI 138
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAE-VEKCAWiCRYYAENAEAFLAD---EPIETDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 139 GKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVG 218
Cdd:cd07100 88 GKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 219 TAITDncDYLM---FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIY 295
Cdd:cd07100 168 AIIAD--PRVRgvtLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 296 VEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKaRPDIGPLFYEPTVLTN 375
Cdd:cd07100 246 VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK-RPDGPGAFYPPTVLTD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 376 VAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEgyaFAWGSLSAPM 455
Cdd:cd07100 325 VTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING---MVKSDPRLPF 401
|
410 420
....*....|....*....|....*.
gi 57116903 456 GGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07100 402 GGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
34-482 |
1.84e-115 |
|
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: 348.79 E-value: 1.84e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREflmDLLQAE---AGKARWAAQE-EIV 109
Cdd:cd07093 6 TGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARAD---ELALLEsldTGKPITLARTrDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 110 DLIANANYYARVCvdLLKPRKAQPLLPGIgKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC 189
Cdd:cd07093 83 RAAANFRFFADYI--LQLDGESYPQDGGA-LNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 190 ALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDY--LMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGA 267
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVdlISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 268 NLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDAT 347
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 348 AKGAKVIAGGKARPDI---GPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTA 424
Cdd:cd07093 320 AEGATILTGGGRPELPdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57116903 425 EGQRIAARLRSGTV-----NVDEgyafawgsLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIA 482
Cdd:cd07093 400 RAHRVARRLEAGTVwvncwLVRD--------LRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
34-482 |
6.93e-114 |
|
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: 344.31 E-value: 6.93e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI---VD 110
Cdd:cd07150 8 DGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETtftPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 111 LIANANYYARvcvdLLKPRKAQPLLPGIgKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCA 190
Cdd:cd07150 88 LLRAAAGECR----RVRGETLPSDSPGT-VSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 191 LACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGAN 268
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMvtFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 269 LDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATA 348
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 349 KGAKVIAGGKARpdiGPlFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQR 428
Cdd:cd07150 323 KGAKLLTGGKYD---GN-FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 429 IAARLRSGTVNV------DEGYafawgslsAPMGGMGLSGVGRRHGPEGLLKYTESQTIA 482
Cdd:cd07150 399 LAERLESGMVHIndptilDEAH--------VPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
34-481 |
3.39e-113 |
|
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: 343.09 E-value: 3.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07088 22 TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYA----RVCVDLLKP-RKAQPLLpgIGKttvcyQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPY 188
Cdd:cd07088 102 YIDYMAewarRIEGEIIPSdRPNENIF--IFK-----VPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 189 CALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARG 266
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMisLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 267 ANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDA 346
Cdd:cd07088 255 ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 347 TAKGAKVIAGGKaRPDIGP-LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAE 425
Cdd:cd07088 335 VEAGATLLTGGK-RPEGEKgYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNT 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 57116903 426 GQRIAARLRSGTVNVDEGYAFAWGSLSApmgGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07088 414 AMRATNELEFGETYINRENFEAMQGFHA---GWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
34-481 |
2.95e-111 |
|
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: 337.58 E-value: 2.95e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07106 6 TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYArvcvDLLKPRKAQPLLPGiGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALAC 193
Cdd:cd07106 86 WLRYTA----SLDLPDEVIEDDDT-RRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 194 AELLYRAgLPRALYAIVPGPGSVvGTAITDNCDY--LMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDK 271
Cdd:cd07106 161 GELAQEV-LPPGVLNVVSGGDEL-GPALTSHPDIrkISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 272 VAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGA 351
Cdd:cd07106 239 VAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 352 KVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAA 431
Cdd:cd07106 319 KVLAGGEPLDGPG-YFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVAR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 57116903 432 RLRSGTVNVDEGYAFawgSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07106 398 RLEAGTVWINTHGAL---DPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
33-481 |
7.39e-111 |
|
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: 336.83 E-value: 7.39e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 33 FTGKPLTTIPVGTAADVEAAFAEARAAQTD--WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVD 110
Cdd:cd07114 5 ATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 111 LIANANYYARVCvdllkpRKAQ-PLLPGIGKTTVCYQ---PKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQT 186
Cdd:cd07114 85 LAEWYRYYAGLA------DKIEgAVIPVDKGDYLNFTrrePLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 187 PYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVA 264
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKiaFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 265 RGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVD 344
Cdd:cd07114 239 DDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 345 DATAKGAKVIAGGKaRPDIGPL----FYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWA 420
Cdd:cd07114 319 RAREEGARVLTGGE-RPSGADLgagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57116903 421 GSTAEGQRIAARLRSGTVNVDEGYAFAWgslSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSP---SSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
21-482 |
1.11e-110 |
|
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: 336.78 E-value: 1.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 21 VAARPTRTIDeVF---TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEA 97
Cdd:cd07138 8 VAPAGTETID-VInpaTEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 98 GKARWAAQEEIVDL-IANANYYARVCvdllkprKAQPLLPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGN 176
Cdd:cd07138 87 GAPITLARAAQVGLgIGHLRAAADAL-------KDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 177 AVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAE 254
Cdd:cd07138 160 TVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMvsFTGSTRAGKRVAEAAADTVKRVALE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 255 LGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEA 334
Cdd:cd07138 240 LGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 335 QLKTVSGHVDDATAKGAKVIAGGKARPDiGP---LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTD 411
Cdd:cd07138 320 QFDRVQGYIQKGIEEGARLVAGGPGRPE-GLergYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTP 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57116903 412 YGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAfawgSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIA 482
Cdd:cd07138 399 YGLAGYVWSADPERARAVARRLRAGQVHINGAAF----NPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
11-477 |
7.25e-109 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 333.20 E-value: 7.25e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 11 RLRNLAAIKDVAARPTRTIdEVF---TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENRE 87
Cdd:PLN02278 24 RTQGLIGGKWTDAYDGKTF-PVYnpaTGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 88 FLMDLLQAEAGKARWAAQEEIVDLIANANYYA----RVCVDLLKPRKAQpllpgiGKTTVCYQPKGVVGVISPWNYPMTL 163
Cdd:PLN02278 103 DLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAeeakRVYGDIIPSPFPD------RRLLVLKQPVGVVGAITPWNFPLAM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 164 TVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLA 241
Cdd:PLN02278 177 ITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASpkVRKITFTGSTAVGKKLM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 242 EHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAY 321
Cdd:PLN02278 257 AGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 322 DFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKaRPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVD 401
Cdd:PLN02278 337 EEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGK-RHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57116903 402 EAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAfawGSLSAPMGGMGLSGVGRRHGPEGLLKYTE 477
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLI---STEVAPFGGVKQSGLGREGSKYGIDEYLE 488
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
34-482 |
1.09e-108 |
|
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: 331.51 E-value: 1.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAA--QTDWAkRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVD- 110
Cdd:cd07089 6 TEEVIGTAPDAGAADVDAAIAAARRAfdTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 111 LIANANYYARVC--VDLLKPRKAQPLLPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPY 188
Cdd:cd07089 85 PIGHLRYFADLAdsFPWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 189 CALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARG 266
Cdd:cd07089 165 SALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDprVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 267 ANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDA 346
Cdd:cd07089 245 ADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 347 TAKGAKVIAGGKaRPDIGP--LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTA 424
Cdd:cd07089 325 RDEGARLVTGGG-RPAGLDkgFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVD 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 57116903 425 EGQRIAARLRSGTVNVDEGyafAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIA 482
Cdd:cd07089 404 RAYRVARRIRTGSVGINGG---GGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-481 |
2.97e-108 |
|
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: 330.33 E-value: 2.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTD--WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVD 110
Cdd:cd07112 11 TGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPiSDALAVDVPS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 111 LIANANYYARVC---VDLLKPRKAQPLlpgigkTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTP 187
Cdd:cd07112 91 AANTFRWYAEAIdkvYGEVAPTGPDAL------ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 188 YCALACAELLYRAGLPRALYAIVPGPGSVVGTAIT--DNCDYLMFTGSSATGSRLAEHAGR-RLIGFSAELGGKNPMIV- 263
Cdd:cd07112 165 LTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGlhMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVf 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 264 ARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHV 343
Cdd:cd07112 245 ADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 344 DDATAKGAKVIAGGKA-RPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGS 422
Cdd:cd07112 325 ESGKAEGARLVAGGKRvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSD 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 57116903 423 TAEGQRIAARLRSGTVNVDegyAFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07112 405 LSRAHRVARRLRAGTVWVN---CFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-481 |
8.64e-107 |
|
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: 326.57 E-value: 8.64e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 26 TRTIDEV--FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWA 103
Cdd:cd07151 9 ERTIDVLnpYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 104 AQEEIVDLIA----NANYYARVCVDLLkprkaQPLLPGigKTTVCY-QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAV 178
Cdd:cd07151 89 ANIEWGAAMAitreAATFPLRMEGRIL-----PSDVPG--KENRVYrEPLGVVGVISPWNFPLHLSMRSVAPALALGNAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 179 VLKPDSQTPYCA-LACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAEL 255
Cdd:cd07151 162 VLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHpvPRLISFTGSTPVGRHIGELAGRHLKKVALEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 256 GGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQ 335
Cdd:cd07151 242 GGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 336 LKTVSGHVDDATAKGAKVIAGGKARpdigPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLN 415
Cdd:cd07151 322 VDGLLDKIEQAVEEGATLLVGGEAE----GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57116903 416 ASVWAGSTAEGQRIAARLRSGTVNV------DEGYafawgslsAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHIndqpvnDEPH--------VPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
34-482 |
1.75e-105 |
|
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: 323.03 E-value: 1.75e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAA-FAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLI 112
Cdd:cd07109 6 TGEVFARIARGGAADVDRAvQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYARVCvDLLKPRKAqPLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALA 192
Cdd:cd07109 86 RYFEYYGGAA-DKLHGETI-PLGPGYFVYTV-REPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 193 CAELLYRAGLPRALYAIVPGPGSVVGTAIT--DNCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLD 270
Cdd:cd07109 163 LAELAEEAGLPAGALNVVTGLGAEAGAALVahPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 271 KVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDfSVDMGSLISEAQLKTVSGHVDDATAKG 350
Cdd:cd07109 243 AALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARARARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 351 AKVIAGGKARPDI--GPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQR 428
Cdd:cd07109 322 ARIVAGGRIAEGApaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALR 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 57116903 429 IAARLRSGTVNVDEGyaFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIA 482
Cdd:cd07109 402 VARRLRAGQVFVNNY--GAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
21-481 |
1.77e-105 |
|
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: 323.37 E-value: 1.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 21 VAARPTRTIDEV--FTGKPLTTIPVGTAADVEAAFAEARAAQTD--WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAE 96
Cdd:cd07139 8 VAPSGSETIDVVspATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 97 AGKAR-WAAQEEIVDLIANANYYARVCVDLLKPRKAQPllPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAG 175
Cdd:cd07139 88 NGMPIsWSRRAQGPGPAALLRYYAALARDFPFEERRPG--SGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 176 NAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGpGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSA 253
Cdd:cd07139 166 CTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 254 ELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISE 333
Cdd:cd07139 245 ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 334 AQLKTVSGHVDDATAKGAKVIAGGKARPDIGP-LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDY 412
Cdd:cd07139 325 RQRERVEGYIAKGRAEGARLVTGGGRPAGLDRgWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDY 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57116903 413 GLNASVWAGSTAEGQRIAARLRSGTVNVDeGYAFAWGslsAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07139 405 GLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFG---APFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
33-438 |
3.23e-104 |
|
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: 319.58 E-value: 3.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 33 FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLI 112
Cdd:cd07102 4 IDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGML 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYARVCVDLLKPRKAQPllPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALA 192
Cdd:cd07102 84 ERARYMISIAEEALADIRVPE--KDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 193 CAELLYRAGLPRALYAIVPGPGSVVGTAITD-NCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDK 271
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 272 VAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGA 351
Cdd:cd07102 242 AAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 352 KVIAGGK--ARPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRI 429
Cdd:cd07102 322 RALIDGAlfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEAL 401
|
....*....
gi 57116903 430 AARLRSGTV 438
Cdd:cd07102 402 GEQLETGTV 410
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
34-481 |
1.19e-103 |
|
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: 319.15 E-value: 1.19e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAA--QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARW-AAQEEIVD 110
Cdd:cd07091 28 TEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEeSAKGDVAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 111 LIANANYYARVCvDllkprKAQPLLPGIGKTTVCY---QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTP 187
Cdd:cd07091 108 SIKCLRYYAGWA-D-----KIQGKTIPIDGNFLAYtrrEPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 188 YCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDY--LMFTGSSATGSRLAEHAGRR-LIGFSAELGGKNPMIVA 264
Cdd:cd07091 182 LSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVdkIAFTGSTAVGRTIMEAAAKSnLKKVTLELGGKSPNIVF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 265 RGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVD 344
Cdd:cd07091 262 DDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 345 DATAKGAKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTA 424
Cdd:cd07091 342 SGKKEGATLLTGGERHGSKG-YFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDIN 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 57116903 425 EGQRIAARLRSGTVNVDEGYAFawgSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07091 421 KALRVSRALKAGTVWVNTYNVF---DAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
35-479 |
3.99e-103 |
|
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: 316.54 E-value: 3.99e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 35 GKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIAn 114
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 115 anyYARVCVDLLKPRKAQPLLPGIGKTTVCYQ-PKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCA-LA 192
Cdd:cd07152 80 ---ELHEAAGLPTQPQGEILPSAPGRLSLARRvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 193 CAELLYRAGLPRALYAIVPGpGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLD 270
Cdd:cd07152 157 IARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMisFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 271 KVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKG 350
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 351 AKVIAGGKARpdigPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIA 430
Cdd:cd07152 316 ARLEAGGTYD----GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 57116903 431 ARLRSG-------TVNvDEGYafawgslsAPMGGMGLSGVGRRH-GPEGLLKYTESQ 479
Cdd:cd07152 392 DRLRTGmlhindqTVN-DEPH--------NPFGGMGASGNGSRFgGPANWEEFTQWQ 439
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
22-491 |
2.48e-102 |
|
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: 315.79 E-value: 2.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 22 AARPTRTIDEVFTGKPLTTIPVGTAADVEAAFAEARAA--QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGK 99
Cdd:cd07119 10 ASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 100 ARWAAQEEIVDLIANANYYARVCVdllKPRKAQPLLPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVV 179
Cdd:cd07119 90 TLRESEIDIDDVANCFRYYAGLAT---KETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 180 LKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGG 257
Cdd:cd07119 167 IKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESpdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 258 KNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLK 337
Cdd:cd07119 247 KNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHRE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 338 TVSGHVDDATAKGAKVIAGGKaRPDIGPL----FYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYG 413
Cdd:cd07119 327 KVLSYIQLGKEEGARLVCGGK-RPTGDELakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57116903 414 LNASVWAGSTAEGQRIAARLRSGTVNV-DEGYAFAwgslSAPMGGMGLSGVGRRHGPEGLLKYTESQTIATarvfNLDP 491
Cdd:cd07119 406 LAGAVWTKDIARANRVARRLRAGTVWInDYHPYFA----EAPWGGYKQSGIGRELGPTGLEEYQETKHINI----NLSP 476
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
34-481 |
2.75e-102 |
|
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: 314.66 E-value: 2.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTD--WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI--- 108
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIega 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 109 VDLIANANYYARVcvdllkprkaqplLPG-----IGKTT---VCYQPKGVVGVISPWNYPMtLTVSDSVP-ALVAGNAVV 179
Cdd:cd07118 86 ADLWRYAASLART-------------LHGdsynnLGDDMlglVLREPIGVVGIITPWNFPF-LILSQKLPfALAAGCTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 180 LKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITD--NCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGG 257
Cdd:cd07118 152 VKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEhpDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 258 KNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLK 337
Cdd:cd07118 232 KNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 338 TVSGHVDDATAKGAKVIAGGKARPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNAS 417
Cdd:cd07118 312 KITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57116903 418 VWAGSTAEGQRIAARLRSGTVNVDegyAFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07118 392 VWSKDIDTALTVARRIRAGTVWVN---TFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
34-482 |
3.75e-101 |
|
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: 311.98 E-value: 3.75e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI---VD 110
Cdd:cd07145 8 NGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVertIR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 111 LIANANYYARVCVDLLKPRKAQPLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCA 190
Cdd:cd07145 88 LFKLAAEEAKVLRGETIPVDAYEYNERRIAFTV-REPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 191 LACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGAN 268
Cdd:cd07145 167 IELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMisFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 269 LDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATA 348
Cdd:cd07145 247 LERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 349 KGAKVIAGGKArpdIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQR 428
Cdd:cd07145 327 KGGKILYGGKR---DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALK 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 57116903 429 IAARLRSGTVNVDEGYAFAWGSLsaPMGGMGLSGVGRRHGPEGLLKYTESQTIA 482
Cdd:cd07145 404 VARELEAGGVVINDSTRFRWDNL--PFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
34-481 |
5.81e-99 |
|
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: 306.87 E-value: 5.81e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07097 24 TSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYARVCVDLlKPRKAQPLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALAC 193
Cdd:cd07097 104 IFRYYAGEALRL-SGETLPSTRPGVEVETT-REPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 194 AELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDK 271
Cdd:cd07097 182 VEILEEAGLPAGVFNLVMGSGSEVGQALVEHpdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 272 VAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGA 351
Cdd:cd07097 262 AVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 352 KVIAGGKA--RPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRI 429
Cdd:cd07097 342 KLVYGGERlkRPDEG-YYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHF 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 57116903 430 AARLRSGTVNVDE---GYAFawgslSAPMGGMGLSGVG-RRHGPEGLLKYTESQTI 481
Cdd:cd07097 421 KRRVEAGVVMVNLptaGVDY-----HVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
34-481 |
1.62e-98 |
|
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: 305.13 E-value: 1.62e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVDLI 112
Cdd:cd07115 6 TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPiRAARRLDVPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYARVCVDLlkPRKAQPLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALA 192
Cdd:cd07115 86 DTFRYYAGWADKI--EGEVIPVRGPFLNYTV-REPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 193 CAELLYRAGLPRALYAIVPGPGSVVGTAITD--NCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLD 270
Cdd:cd07115 163 IAELMAEAGFPAGVLNVVTGFGEVAGAALVEhpDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 271 KVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKG 350
Cdd:cd07115 243 AAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 351 AKVIAGGKaRPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIA 430
Cdd:cd07115 323 ARLLTGGK-RPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 57116903 431 ARLRSGTVNVDEGYAFAWGSlsaPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07115 402 AALKAGTVWINTYNRFDPGS---PFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
34-477 |
3.03e-98 |
|
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: 304.27 E-value: 3.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07110 6 TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYARVCVDLlKPRKAQPL-LPGIGKTTVCY-QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCAL 191
Cdd:cd07110 86 CFEYYADLAEQL-DAKAERAVpLPSEDFKARVRrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 192 ACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANL 269
Cdd:cd07110 165 ELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHpgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 270 DKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAK 349
Cdd:cd07110 245 EKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 350 GAKVIAGGKaRPDIGP--LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQ 427
Cdd:cd07110 325 GARLLCGGR-RPAHLEkgYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCD 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 57116903 428 RIAARLRSGTVnvdegyafaWGSLS------APMGGMGLSGVGRRHGPEGLLKYTE 477
Cdd:cd07110 404 RVAEALEAGIV---------WINCSqpcfpqAPWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
34-476 |
4.91e-98 |
|
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: 303.48 E-value: 4.91e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARW-AAQEEIVDLI 112
Cdd:cd07092 6 TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHlVRDDELPGAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYARVCVDLLKPRkAQPLLPGIgKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALA 192
Cdd:cd07092 86 DNFRFFAGAARTLEGPA-AGEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 193 CAELLYRaGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLD 270
Cdd:cd07092 164 LAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMvsLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 271 KVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDAtAKG 350
Cdd:cd07092 243 AAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA-PAH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 351 AKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIA 430
Cdd:cd07092 322 ARVLTGGRRAEGPG-YFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 57116903 431 ARLRSGTVNVDEGYAFAwgsLSAPMGGMGLSGVGRRHGPEGLLKYT 476
Cdd:cd07092 401 ARLDFGTVWVNTHIPLA---AEMPHGGFKQSGYGKDLSIYALEDYT 443
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
33-481 |
3.69e-97 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 301.44 E-value: 3.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 33 FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIvdli 112
Cdd:cd07149 7 YDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ananyyARvCVDLLK------PRKAQPLLP------GIGKTTVCYQ-PKGVVGVISPWNYPMTLTVSDSVPALVAGNAVV 179
Cdd:cd07149 83 ------DR-AIETLRlsaeeaKRLAGETIPfdaspgGEGRIGFTIRePIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 180 LKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIgfSAELGG 257
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMisFTGSPAVGEAIARKAGLKKV--TLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 258 KNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLK 337
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 338 TVSGHVDDATAKGAKVIAGGKARPDIgplfYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNAS 417
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGKRDGAI----LEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57116903 418 VWAGSTAEGQRIAARLRSGTVNVDEGYAFAWGSLsaPMGGMGLSGVGRrhgpEGlLKY-----TESQTI 481
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINDSSTFRVDHM--PYGGVKESGTGR----EG-PRYaieemTEIKLV 451
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
34-481 |
6.00e-97 |
|
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: 301.20 E-value: 6.00e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVDLI 112
Cdd:cd07108 6 TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNAlRTQARPEAAVLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYARVCVDLlkprKAQ--PLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCA 190
Cdd:cd07108 86 DLFRYFGGLAGEL----KGEtlPFGPDVLTYTV-REPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 191 LACAELLYRAgLPRALYAIVPGPGSVVGTAITDNCDY--LMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGAN 268
Cdd:cd07108 161 LLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVdkVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 269 LDKVAK---AATRacFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDD 345
Cdd:cd07108 240 LDDAVDgaiAGMR--FTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 346 A-TAKGAKVIAGGKARPDiGPL----FYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWA 420
Cdd:cd07108 318 GlSTSGATVLRGGPLPGE-GPLadgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57116903 421 GSTAEGQRIAARLRSGTVNVDEGYAFAWGsLSapMGGMGLSGVGRRHGPEGLLK-YTESQTI 481
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPG-QS--YGGFKQSGLGREASLEGMLEhFTQKKTV 455
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
33-485 |
1.24e-96 |
|
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: 300.37 E-value: 1.24e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 33 FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARW-AAQEEIVDL 111
Cdd:cd07098 4 ATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVdASLGEILVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 112 IANANYYARVCVDLLKP-RKAQPLLPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQT---- 186
Cdd:cd07098 84 CEKIRWTLKHGEKALRPeSRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVawss 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 187 -PYCALAcAELLYRAGLPRALYAIVPGPGSVvGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIV 263
Cdd:cd07098 164 gFFLSII-RECLAACGHDPDLVQLVTCLPET-AEALTSHpvIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 264 ARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHV 343
Cdd:cd07098 242 LDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 344 DDATAKGAKVIAGGKARPdiGPL-----FYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASV 418
Cdd:cd07098 322 ADAVEKGARLLAGGKRYP--HPEypqghYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57116903 419 WAGSTAEGQRIAARLRSGTVNVDEgYAFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIATAR 485
Cdd:cd07098 400 FGKDIKRARRIASQLETGMVAIND-FGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR 465
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
33-481 |
3.36e-96 |
|
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: 298.96 E-value: 3.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 33 FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI---V 109
Cdd:cd07094 7 YDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVdraI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 110 DLIANANYYARVCVDLLKPRKAQPLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC 189
Cdd:cd07094 87 DTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTI-REPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 190 ALACAELLYRAGLPRALYAIVPGPGSVVGTAIT--DNCDYLMFTGSSATGSRLAEHAGRRLIGFsaELGGKNPMIVARGA 267
Cdd:cd07094 166 ALELAKILVEAGVPEGVLQVVTGEREVLGDAFAadERVAMLSFTGSAAVGEALRANAGGKRIAL--ELGGNAPVIVDRDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 268 NLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDAT 347
Cdd:cd07094 244 DLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 348 AKGAKVIAGGkaRPDiGPLFYePTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQ 427
Cdd:cd07094 324 EAGARLLCGG--ERD-GALFK-PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAF 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 57116903 428 RIAARLRSGTVNVDEGYAFAWGSLsaPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07094 400 KAAEKLEVGGVMVNDSSAFRTDWM--PFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-481 |
3.57e-96 |
|
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: 299.65 E-value: 3.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 2 PAPSAEVFDRlRNLAAIKDVAArptrtidevftgkpltTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDL 81
Cdd:cd07131 9 DSASGETFDS-RNPADLEEVVG----------------TFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 82 VIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARvcvdllKPRKAQpllpgiGKTTVC----------YQPKGVV 151
Cdd:cd07131 72 LKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAG------EGRRLF------GETVPSelpnkdamtrRQPIGVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 152 GVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLM 229
Cdd:cd07131 140 ALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHpdVDVVS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 230 FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFG 309
Cdd:cd07131 220 FTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 310 DAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGPL---FYEPTVLTNVAPEMECAANE 386
Cdd:cd07131 300 ERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEkgyFVEPTVFTDVTPDMRIAQEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 387 TFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAWGSLsaPMGGMGLSGVGRR 466
Cdd:cd07131 380 IFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL--PFGGVKKSGNGHR 457
|
490
....*....|....*.
gi 57116903 467 HGPEGLLK-YTESQTI 481
Cdd:cd07131 458 EAGTTALDaFTEWKAV 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
34-481 |
1.33e-95 |
|
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: 297.72 E-value: 1.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAA--QTDWAKRPVIeRAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDL 111
Cdd:cd07120 6 TGEVIGTYADGGVAEAEAAIAAARRAfdETDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEISGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 112 IANANYYARVCVDLlkPRKAQPLLPGIgKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCAL 191
Cdd:cd07120 85 ISELRYYAGLARTE--AGRMIEPEPGS-FSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 192 ACAELLYRA-GLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGAN 268
Cdd:cd07120 162 AIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASpdVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 269 LDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATA 348
Cdd:cd07120 242 LDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 349 KGAKVI-AGGKARPDIGP-LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEG 426
Cdd:cd07120 322 AGAEVVlRGGPVTEGLAKgAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 57116903 427 QRIAARLRSGTVNVDEgyafaWGSL--SAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07120 402 MRVARAIRAGTVWIND-----WNKLfaEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
34-481 |
2.74e-93 |
|
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: 291.59 E-value: 2.74e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07107 6 TGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYARVCVDLlkprKAQ--PLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCAL 191
Cdd:cd07107 86 LLDYFAGLVTEL----KGEtiPVGGRNLHYTL-REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 192 ACAELLyRAGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANL 269
Cdd:cd07107 161 RLAELA-REVLPPGVFNILPGDGATAGAALVRHPDVKRiaLIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 270 DKVAKAATRAC-FSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATA 348
Cdd:cd07107 240 EAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 349 KGAKVIAGGKARPDI---GPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAE 425
Cdd:cd07107 320 EGARLVTGGGRPEGPaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQ 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 57116903 426 GQRIAARLRSGTVNVDEGYAFAWGslsAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07107 400 AHRTARRVEAGYVWINGSSRHFLG---APFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
34-476 |
3.95e-91 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 286.42 E-value: 3.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEE----IV 109
Cdd:PRK13473 26 TGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDeipaIV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 110 DLI---ANAnyyARvcvdLLKPRKAQPLLPGiGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQT 186
Cdd:PRK13473 106 DVFrffAGA---AR----CLEGKAAGEYLEG-HTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEIT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 187 PYCALACAELLYRAgLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVA 264
Cdd:PRK13473 178 PLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMvsLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 265 RGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVD 344
Cdd:PRK13473 257 DDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 345 DATAKG-AKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGST 423
Cdd:PRK13473 337 RAKALGhIRVVTGGEAPDGKG-YYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDV 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 57116903 424 AEGQRIAARLRSGTVNVDEGYAFAwgsLSAPMGGMGLSGVGRRHGPEGLLKYT 476
Cdd:PRK13473 416 GRAHRVSARLQYGCTWVNTHFMLV---SEMPHGGQKQSGYGKDMSLYGLEDYT 465
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
34-488 |
1.19e-90 |
|
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: 285.23 E-value: 1.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKR-PVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLI 112
Cdd:cd07082 25 DGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 AnanyYARVCVDLLKPRKAQPLLPGI---GKTTVCY---QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQT 186
Cdd:cd07082 105 D----YIRDTIEELKRLDGDSLPGDWfpgTKGKIAQvrrEPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 187 PYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRrlIGFSAELGGKNPMIVA 264
Cdd:cd07082 181 VLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHgrIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 265 RGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVD 344
Cdd:cd07082 259 PDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLID 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 345 DATAKGAKVIAGGKARpdiGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTA 424
Cdd:cd07082 339 DAVAKGATVLNGGGRE---GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDIN 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57116903 425 EGQRIAARLRSGTVNVDEGYAFAWGSLsaPMGGMGLSGVGRrhgpEGLLKYTESQTIATARVFN 488
Cdd:cd07082 416 KARKLADALEVGTVNINSKCQRGPDHF--PFLGRKDSGIGT----QGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
33-468 |
3.69e-90 |
|
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: 283.48 E-value: 3.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 33 FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRpviERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLI 112
Cdd:cd07146 7 YTGEVVGTVPAGTEEALREALALAASYRSTLTRY---QRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYAR---------VCVDLLKPRKAQpllpgigKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPD 183
Cdd:cd07146 84 DVLRFAAAealrddgesFSCDLTANGKAR-------KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 184 SQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTA-ITD-NCDYLMFTGSSATGSRLAEHAG-RRLIgfsAELGGKNP 260
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDElITHpDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 261 MIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVS 340
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 341 GHVDDATAKGAKVIAGGKARpdiGPLfYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWA 420
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQRQ---GAL-YAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 57116903 421 GSTAEGQRIAARLRSGTVNVDEGYAFAwgSLSAPMGGMGLSGVGRRHG 468
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFR--SELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
62-481 |
8.52e-89 |
|
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: 279.08 E-value: 8.52e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 62 DWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAqEEIVDLIAN-----ANYYARVCVDLLKPRKaqpllP 136
Cdd:cd07105 15 AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWA-GFNVDLAAGmlreaASLITQIIGGSIPSDK-----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 137 GIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPralyaivPGPGSV 216
Cdd:cd07105 89 GTLAMVV-KEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLP-------KGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 217 VGTAITDNCDYLM------------FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNA 284
Cdd:cd07105 161 VTHSPEDAPEVVEaliahpavrkvnFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 285 GQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGtaydfSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIG 364
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 365 PLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNV---- 440
Cdd:cd07105 316 GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIngmt 395
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 57116903 441 --DEGyafawgslSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07105 396 vhDEP--------TLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
34-481 |
4.58e-86 |
|
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: 273.03 E-value: 4.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKArwaAQEEIVDLIA 113
Cdd:cd07090 6 TGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKP---IEEARVDIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NAN---YYARVCVDLLkprkAQPL-LPGigkTTVCY---QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQT 186
Cdd:cd07090 83 SADcleYYAGLAPTLS----GEHVpLPG---GSFAYtrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 187 PYCALACAELLYRAGLPRALYAIVPGPGSVvGTAITDNCDY--LMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVA 264
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 265 RGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVD 344
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 345 DATAKGAKVIAGGKARPDIGPL----FYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWA 420
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEDGLengfYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57116903 421 GSTAEGQRIAARLRSGTVnvdegYAFAWGSLSA--PMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTC-----WINTYNISPVevPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
63-481 |
6.79e-86 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 273.07 E-value: 6.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 63 WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANA-NYYARvCVDLLKPRkaqpLLPGIGKT 141
Cdd:cd07141 63 WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVlRYYAG-WADKIHGK----TIPMDGDF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 142 tVCY---QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVG 218
Cdd:cd07141 138 -FTYtrhEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 219 TAITDNCDY--LMFTGSSATGSRLAEHAGR-RLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIY 295
Cdd:cd07141 217 AAISSHPDIdkVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTF 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 296 VEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGpLFYEPTVLTN 375
Cdd:cd07141 297 VQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKG-YFIQPTVFSD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 376 VAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFawgSLSAPM 455
Cdd:cd07141 376 VTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVV---SPQAPF 452
|
410 420
....*....|....*....|....*.
gi 57116903 456 GGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07141 453 GGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
34-481 |
8.66e-86 |
|
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: 273.13 E-value: 8.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAA-QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWA-AQEEIVDL 111
Cdd:cd07144 32 TGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLDEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 112 IANANYYARVCvDLLKPrKAQPLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCAL 191
Cdd:cd07144 112 IAVIRYYAGWA-DKIQG-KTIPTSPNKLAYTL-HEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 192 ACAELLYRAGLPRALYAIVPGPGSVVGTAIT--DNCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANL 269
Cdd:cd07144 189 YFANLVKEAGFPPGVVNIIPGYGAVAGSALAehPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 270 DKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVR-NMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATA 348
Cdd:cd07144 269 DQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 349 KGAKVIAGGKARPDIGP--LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEG 426
Cdd:cd07144 349 EGAKLVYGGEKAPEGLGkgYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRA 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 57116903 427 QRIAARLRSGTVNV----DEGYafawgslSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07144 429 HRVARELEAGMVWInssnDSDV-------GVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
62-482 |
2.01e-85 |
|
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: 272.94 E-value: 2.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 62 DWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLlkprKAQPLLPGIG-K 140
Cdd:cd07124 84 TWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRL----RGFPVEMVPGeD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 141 TTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTA 220
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 221 ITDNCD--YLMFTGSSATGSRLAEHAGRRLIG------FSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIE 292
Cdd:cd07124 240 LVEHPDvrFIAFTGSREVGLRIYERAAKVQPGqkwlkrVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 293 RIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATaKGAKVIAGGKARPDIGPLFY-EPT 371
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELAAEGYFvQPT 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 372 VLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAWgSL 451
Cdd:cd07124 399 IFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGAL-VG 477
|
410 420 430
....*....|....*....|....*....|..
gi 57116903 452 SAPMGGMGLSGVGRRH-GPEGLLKYTESQTIA 482
Cdd:cd07124 478 RQPFGGFKMSGTGSKAgGPDYLLQFMQPKTVT 509
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
34-481 |
3.13e-84 |
|
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: 268.66 E-value: 3.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07086 22 NGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMID 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYArvcvdllkprkaqpllpGI-----GKTTVC----------YQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAV 178
Cdd:cd07086 102 ICDYAV-----------------GLsrmlyGLTIPSerpghrlmeqWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 179 VLKPDSQTPYCALACAELLYRA----GLPRALYAIVPGPGSVvGTAIT--DNCDYLMFTGSSATGSRLAEHAGRRLIGFS 252
Cdd:cd07086 165 VWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 253 AELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLIS 332
Cdd:cd07086 244 LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLIN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 333 EAQLKTVSGHVDDATAKGAKVIAGGKaRPDIGP--LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDT 410
Cdd:cd07086 324 QAAVEKYLNAIEIAKSQGGTVLTGGK-RIDGGEpgNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57116903 411 DYGLNASVWAGSTAEGQRIAARLRS--GTVNVDEGYAFAwgSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07086 403 PQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNIPTSGA--EIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
34-477 |
6.57e-83 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 265.62 E-value: 6.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:PRK11241 35 NGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAAS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYA----RVCVDLLKPRKAQPLLpgigktTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC 189
Cdd:PRK11241 115 FIEWFAeegkRIYGDTIPGHQADKRL------IVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 190 ALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGA 267
Cdd:PRK11241 189 ALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 268 NLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDAT 347
Cdd:PRK11241 269 DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADAL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 348 AKGAKVIAGGKARPdIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQ 427
Cdd:PRK11241 349 EKGARVVCGGKAHE-LGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVF 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 57116903 428 RIAARLRSGTVNVDEGYAfawGSLSAPMGGMGLSGVGRRHGPEGLLKYTE 477
Cdd:PRK11241 428 RVGEALEYGIVGINTGII---SNEVAPFGGIKASGLGREGSKYGIEDYLE 474
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
34-481 |
1.76e-81 |
|
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: 261.69 E-value: 1.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAA-QTDWAKR-PVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVD 110
Cdd:cd07143 31 TGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTfGTAKRVDVQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 111 LIANANYYArvcvDLLKPRKAQPLLPGIGKTTVC-YQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC 189
Cdd:cd07143 111 SADTFRYYG----GWADKIHGQVIETDIKKLTYTrHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 190 ALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGR-RLIGFSAELGGKNPMIVARG 266
Cdd:cd07143 187 ALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHmdIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 267 ANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDA 346
Cdd:cd07143 267 ADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 347 TAKGAKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEG 426
Cdd:cd07143 347 KAEGATVETGGKRHGNEG-YFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNA 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 57116903 427 QRIAARLRSGTVNVDegyAFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07143 426 IRVANALKAGTVWVN---CYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
72-481 |
2.87e-80 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 256.20 E-value: 2.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 72 AAVIRryrdlviENREFLMDLLQAEAGKARWAAQEEI------VDLIAN-ANYYARVCVDLLKPRKaqpllpgigKTTVC 144
Cdd:PRK10090 5 AAGIR-------ERASEISALIVEEGGKIQQLAEVEVaftadyIDYMAEwARRYEGEIIQSDRPGE---------NILLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 145 YQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN 224
Cdd:PRK10090 69 KRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 225 CDYLM--FTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAE 302
Cdd:PRK10090 149 PKVAMvsMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 303 EFTRKFGDAVRNMKLG-TAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGpLFYEPTVLTNVAPEME 381
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGnPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKG-YYYPPTLLLDVRQEMS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 382 CAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAWGSLSApmgGMGLS 461
Cdd:PRK10090 308 IMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHA---GWRKS 384
|
410 420
....*....|....*....|
gi 57116903 462 GVGRRHGPEGLLKYTESQTI 481
Cdd:PRK10090 385 GIGGADGKHGLHEYLQTQVV 404
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-481 |
5.05e-80 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 258.27 E-value: 5.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 21 VAARPTRTIDEVF--TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAG 98
Cdd:PRK13252 16 VEATSGETFEVINpaTGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 99 KArwaAQEEI-VDLIANAN---YYARVCVDLLKprKAQPLLPGIGKTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVA 174
Cdd:PRK13252 96 KP---IQETSvVDIVTGADvleYYAGLAPALEG--EQIPLRGGSFVYTR-REPLGVCAGIGAWNYPIQIACWKSAPALAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 175 GNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVvGTAITDNCDY--LMFTGSSATGSRLAEHAGRRLIGFS 252
Cdd:PRK13252 170 GNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIakVSFTGGVPTGKKVMAAAAASLKEVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 253 AELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLIS 332
Cdd:PRK13252 249 MELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 333 EAQLKTVSGHVDDATAKGAKVIAGGKARPDIGP---LFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKAND 409
Cdd:PRK13252 329 FAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFangAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARAND 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57116903 410 TDYGLNASVWAGSTAEGQRIAARLRSGT--VNvdegyafAWGSLSAPM--GGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:PRK13252 409 TEYGLAAGVFTADLSRAHRVIHQLEAGIcwIN-------TWGESPAEMpvGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
66-468 |
8.07e-80 |
|
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: 255.53 E-value: 8.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 66 RPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARW-AAQEEIVDLIANANYYARVCVDLLKPRKAQ-PLLPGIGKTTV 143
Cdd:cd07087 17 RSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAeAYLTEIAVVLGEIDHALKHLKKWMKPRRVSvPLLLQPAKAYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 144 CYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAgLPRALYAIVPGPGSvVGTAITD 223
Cdd:cd07087 97 IPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-VATALLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 224 NC-DYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAE 302
Cdd:cd07087 175 EPfDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 303 EFTRKFGDAVRNMkLGTAYDFSVDMGSLISEAQLKTVSGHVDDatakgAKVIAGGKArpDIGPLFYEPTVLTNVAPEMEC 382
Cdd:cd07087 255 ELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDD-----GKVVIGGQV--DKEERYIAPTILDDVSPDSPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 383 AANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAwGSLSAPMGGMGLSG 462
Cdd:cd07087 327 MQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHA-AIPNLPFGGVGNSG 405
|
....*.
gi 57116903 463 VGRRHG 468
Cdd:cd07087 406 MGAYHG 411
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
32-476 |
1.05e-79 |
|
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: 256.02 E-value: 1.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 32 VFTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDL 111
Cdd:cd07147 6 PYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 112 IANANYYARVCVdllkpRKAQPLLP------GIGKTTVCYQ-PKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDS 184
Cdd:cd07147 86 IDTFRIAAEEAT-----RIYGEVLPldisarGEGRQGLVRRfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 185 QTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN-CDYLMFTGSSATGSRLAEHAGRRLIGFsaELGGKNPMIV 263
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDErIKLLSFTGSPAVGWDLKARAGKKKVVL--ELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 264 ARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHV 343
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 344 DDATAKGAKVIAGGKARpdiGPLFyEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGST 423
Cdd:cd07147 319 NEAVDAGAKLLTGGKRD---GALL-EPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 57116903 424 AEGQRIAARLRSGTVNVDEgyAFAWGSLSAPMGGMGLSGVGRrhgpEGlLKYT 476
Cdd:cd07147 395 EKALRAWDELEVGGVVIND--VPTFRVDHMPYGGVKDSGIGR----EG-VRYA 440
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
34-484 |
1.47e-79 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 257.44 E-value: 1.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAA--QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKArwAAQEEIVDL 111
Cdd:PLN02766 45 TGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKL--FALGKAVDI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 112 IANAN---YYA----RVCVDLLK-PRKAQpllpgiGKTTvcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPD 183
Cdd:PLN02766 123 PAAAGllrYYAgaadKIHGETLKmSRQLQ------GYTL--KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 184 SQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLM--FTGSSATGSRLAEHAGR-RLIGFSAELGGKNP 260
Cdd:PLN02766 195 EQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKvsFTGSTEVGRKIMQAAATsNLKQVSLELGGKSP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 261 MIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVS 340
Cdd:PLN02766 275 LLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKIL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 341 GHVDDATAKGAKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWA 420
Cdd:PLN02766 355 SYIEHGKREGATLLTGGKPCGDKG-YYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVT 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57116903 421 GSTAEGQRIAARLRSGTVNVDEGYAFawgSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIATA 484
Cdd:PLN02766 434 KDLDVANTVSRSIRAGTIWVNCYFAF---DPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTP 494
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
34-475 |
8.27e-79 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 255.43 E-value: 8.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAE-----ARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI 108
Cdd:PLN02467 32 TEETIGDIPAATAEDVDAAVEAarkafKRNKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 109 VDLIANANYYARVCVDLLKPRKAQPLLPGIG-KTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTP 187
Cdd:PLN02467 112 DDVAGCFEYYADLAEALDAKQKAPVSLPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELAS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 188 YCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVAR 265
Cdd:PLN02467 192 VTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHpgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 266 GANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDD 345
Cdd:PLN02467 272 DVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFIST 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 346 ATAKGAKVIAGGKARPDIGPLFY-EPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTA 424
Cdd:PLN02467 352 AKSEGATILCGGKRPEHLKKGFFiEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLE 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 57116903 425 EGQRIAARLRSGTVnvdegyafaWGSLS------APMGGMGLSGVGRRHGPEGLLKY 475
Cdd:PLN02467 432 RCERVSEAFQAGIV---------WINCSqpcfcqAPWGGIKRSGFGRELGEWGLENY 479
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
34-481 |
1.46e-78 |
|
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: 254.34 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAA--QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDL 111
Cdd:cd07140 30 DGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKTHVGM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 112 -IANANYYARVCvDLLKPrKAQPLLPGIGKTTVCY---QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTP 187
Cdd:cd07140 110 sIQTFRYFAGWC-DKIQG-KTIPINQARPNRNLTLtkrEPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 188 YCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDY--LMFTGSSATGSRLAEH-AGRRLIGFSAELGGKNPMIVA 264
Cdd:cd07140 188 LTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVrkLGFTGSTPIGKHIMKScAVSNLKKVSLELGGKSPLIIF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 265 RGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVD 344
Cdd:cd07140 268 ADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 345 DATAKGAKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPV--VSIYPVADVDEAVEKANDTDYGLNASVWAGS 422
Cdd:cd07140 348 RGVKEGATLVYGGKQVDRPG-FFFEPTVFTDVEDHMFIAKEESFGPImiISKFDDGDVDGVLQRANDTEYGLASGVFTKD 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 57116903 423 TAEGQRIAARLRSGTVNVDegyAFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07140 427 INKALYVSDKLEAGTVFVN---TYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
34-465 |
3.44e-78 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 252.35 E-value: 3.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:PRK09406 10 TGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYARVCVDLLKPRKAQPLLPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALAC 193
Cdd:PRK09406 90 GFRYYAEHAEALLADEPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 194 AELLYRAGLPR-ALYAIVPGPGSVVGTAITDNCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKV 272
Cdd:PRK09406 170 ADLFRRAGFPDgCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 273 AKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAK 352
Cdd:PRK09406 250 AETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGAT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 353 VIAGGKaRPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAAR 432
Cdd:PRK09406 330 ILCGGK-RPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDD 408
|
410 420 430
....*....|....*....|....*....|...
gi 57116903 433 LRSGTVNVDeGYAFAWGSLsaPMGGMGLSGVGR 465
Cdd:PRK09406 409 LEAGQVFIN-GMTVSYPEL--PFGGVKRSGYGR 438
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
19-481 |
1.60e-77 |
|
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: 251.21 E-value: 1.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 19 KDVAARPTRTIDEV--FTGKPLTTIPVGTAADVEAAFAEARAA-QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQA 95
Cdd:cd07113 7 RPVAGQSEKRLDITnpATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 96 EAGKARWAAQEEIVDLIAN-ANYYA----RVCVDLLKPrkAQPLLPGIGKTTVCY-QPKGVVGVISPWNYPMTLTVSDSV 169
Cdd:cd07113 87 CSGKSIHLSRAFEVGQSANfLRYFAgwatKINGETLAP--SIPSMQGERYTAFTRrEPVGVVAGIVPWNFSVMIAVWKIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 170 PALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITD-NCDYLMFTGSSATGSRLAEHAGRRL 248
Cdd:cd07113 165 AALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHpDVAKVSFTGSVATGKKIGRQAASDL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 249 IGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMG 328
Cdd:cd07113 245 TRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 329 SLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKAN 408
Cdd:cd07113 325 PLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEG-YFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLIN 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57116903 409 DTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEgYAFAWGSLsaPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07113 404 DTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNM-HTFLDPAV--PFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
29-468 |
1.12e-76 |
|
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: 250.19 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 29 IDEVFTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI 108
Cdd:cd07125 51 IDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 109 VDLIANANYYArvcvDLLKPRKAQPLLPG-IGKT-TVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQT 186
Cdd:cd07125 131 REAIDFCRYYA----AQARELFSDPELPGpTGELnGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 187 PYCALACAELLYRAGLPRALYAIVPGPGSVVGTAIT--DNCDYLMFTGSSATGSR----LAEHAGRrLIGFSAELGGKNP 260
Cdd:cd07125 207 PLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVahPRIDGVIFTGSTETAKLinraLAERDGP-ILPLIAETGGKNA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 261 MIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVS 340
Cdd:cd07125 286 MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 341 GHVDDATAKgAKVIAGGKArPDIGPLFYEPTVLTNVAPemECAANETFGPVVSI--YPVADVDEAVEKANDTDYGLNASV 418
Cdd:cd07125 366 AHTELMRGE-AWLIAPAPL-DDGNGYFVAPGIIEIVGI--FDLTTEVFGPILHVirFKAEDLDEAIEDINATGYGLTLGI 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 57116903 419 WAGSTAEGQRIAARLRSGTVNVDEGYAfawGS--LSAPMGGMGLSGVGRRHG 468
Cdd:cd07125 442 HSRDEREIEYWRERVEAGNLYINRNIT---GAivGRQPFGGWGLSGTGPKAG 490
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
34-465 |
3.00e-76 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 248.03 E-value: 3.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVDLI 112
Cdd:cd07559 25 NGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPiRETLAADIPLAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYARVCvdllkpRKAQPLLPGIGKTTVCY---QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC 189
Cdd:cd07559 105 DHFRYFAGVI------RAQEGSLSEIDEDTLSYhfhEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 190 ALACAELLYRAgLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIV---- 263
Cdd:cd07559 179 ILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHprIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfdda 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 264 -ARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGH 342
Cdd:cd07559 258 mDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 343 VDDATAKGAKVIAGGKARPDIGPL---FYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVW 419
Cdd:cd07559 338 VDIGKEEGAEVLTGGERLTLGGLDkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVW 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 57116903 420 AGSTAEGQRIAARLRSGTVNVDEGYAFAWGslsAPMGGMGLSGVGR 465
Cdd:cd07559 418 TRDINRALRVARGIQTGRVWVNCYHQYPAH---APFGGYKKSGIGR 460
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
34-475 |
4.02e-76 |
|
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: 247.69 E-value: 4.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07111 46 TGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYARVCVDLLKPRkaqplLPGigkttvcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALAC 193
Cdd:cd07111 126 RHFYHHAGWAQLLDTE-----LAG-------WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 194 AELLYRAGLPRALYAIVPGPGSVvGTAITDN--CDYLMFTGSSATGS---RLAEHAGRRLigfSAELGGKNPMIVARGAN 268
Cdd:cd07111 194 AEICAEAGLPPGVLNIVTGNGSF-GSALANHpgVDKVAFTGSTEVGRalrRATAGTGKKL---SLELGGKSPFIVFDDAD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 269 LDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATA 348
Cdd:cd07111 270 LDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 349 KGAKVIAGGKARPDIGPlFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQR 428
Cdd:cd07111 350 EGADVFQPGADLPSKGP-FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 57116903 429 IAARLRSGTVNVDEGYAFawgSLSAPMGGMGLSGVGRRHGPEGLLKY 475
Cdd:cd07111 429 VALSLKAGVVWINGHNLF---DAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
34-481 |
1.65e-74 |
|
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: 243.52 E-value: 1.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVDLI 112
Cdd:cd07117 25 NGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPiRETRAVDIPLAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYARVCvdllkpRKAQPLLPGIGKTT---VCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC 189
Cdd:cd07117 105 DHFRYFAGVI------RAEEGSANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 190 ALACAELLYRAgLPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGA 267
Cdd:cd07117 179 LLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 268 NLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDAT 347
Cdd:cd07117 258 NWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 348 AKGAKVIAGGK----ARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGST 423
Cdd:cd07117 338 EEGAKILTGGHrlteNGLDKG-FFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDI 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 57116903 424 AEGQRIAARLRSGTVNVDEGYAFAWGslsAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07117 417 NRALRVARAVETGRVWVNTYNQIPAG---APFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
63-483 |
3.54e-74 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 242.40 E-value: 3.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 63 WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVDLIANANYYA-RVCvdllkprKAQPL-LPGIG 139
Cdd:cd07142 59 WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPyEQARYAEVPLAARLFRYYAgWAD-------KIHGMtLPADG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 140 KTTV--CYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVV 217
Cdd:cd07142 132 PHHVytLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 218 GTAITD--NCDYLMFTGSSATGSRLAEHAGR-RLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERI 294
Cdd:cd07142 212 GAAIAShmDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 295 YVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGpLFYEPTVLT 374
Cdd:cd07142 292 FVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKG-YYIQPTIFS 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 375 NVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFawgSLSAP 454
Cdd:cd07142 371 DVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVF---DASIP 447
|
410 420
....*....|....*....|....*....
gi 57116903 455 MGGMGLSGVGRRHGPEGLLKYTESQTIAT 483
Cdd:cd07142 448 FGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
81-483 |
1.62e-73 |
|
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: 239.43 E-value: 1.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 81 LVIENREFLMDLLQAEAGKAR--------WAAQEEIVDLIANANYYArvcvdllKPRKAQPLLPG--IGKTTVCYQPKGV 150
Cdd:cd07135 39 AVKDNEEAIVEALKKDLGRPPfetlltevSGVKNDILHMLKNLKKWA-------KDEKVKDGPLAfmFGKPRIRKEPLGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 151 VGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLyRAGLPRALYAIVPGPGSVVGTAITDNCDYLMF 230
Cdd:cd07135 112 VLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELV-PKYLDPDAFQVVQGGVPETTALLEQKFDKIFY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 231 TGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGD 310
Cdd:cd07135 191 TGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 311 AVRNMKLGTAYDfSVDMGSLISEAQLKTVSGHVDdaTAKGaKVIAGGKArpDIGPLFYEPTVLTNVAPE---MEcaaNET 387
Cdd:cd07135 271 VLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLD--TTKG-KVVIGGEM--DEATRFIPPTIVSDVSWDdslMS---EEL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 388 FGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYaFAWGSLSAPMGGMGLSGVGRRH 467
Cdd:cd07135 342 FGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTL-IHVGVDNAPFGGVGDSGYGAYH 420
|
410
....*....|....*.
gi 57116903 468 GPEGLLKYTESQTIAT 483
Cdd:cd07135 421 GKYGFDTFTHERTVVK 436
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
60-471 |
3.33e-73 |
|
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: 238.67 E-value: 3.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRP--VIERAAVIRRYRDLVIENREFLMDLLQAEAGKArwaAQE----EIVDLIANANYYARVCVDLLKPRKAQP 133
Cdd:cd07134 9 AHALALRAstAAERIAKLKRLKKAILARREEIIAALAADFRKP---AAEvdltEILPVLSEINHAIKHLKKWMKPKRVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 134 LLPGIG-KTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCAlACAELLYRAGLPRALYAIVPG 212
Cdd:cd07134 86 PLLLFGtKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTS-AVIAKIIREAFDEDEVAVFEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 213 pGSVVGTAITD-NCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISI 291
Cdd:cd07134 165 -DAEVAQALLElPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 292 ERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDF-SVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDigPLFYEP 370
Cdd:cd07134 244 DYVFVHESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAA--QRYIAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 371 TVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYA-FAWG 449
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhFLNP 401
|
410 420
....*....|....*....|..
gi 57116903 450 SLsaPMGGMGLSGVGRRHGPEG 471
Cdd:cd07134 402 NL--PFGGVNNSGIGSYHGVYG 421
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
70-481 |
3.48e-71 |
|
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: 233.53 E-value: 3.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 70 ERAAVIRRYRDLVIENREFLMDLLQAEAGkARwAAQE----EIVDLIANANYYARVCVDLLKP--RKAQPLLPGiGKTTV 143
Cdd:cd07133 21 ERRDRLDRLKALLLDNQDALAEAISADFG-HR-SRHEtllaEILPSIAGIKHARKHLKKWMKPsrRHVGLLFLP-AKAEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 144 CYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLyRAGLPRALYAIVPGpGSVVGTAITD 223
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELL-AEYFDEDEVAVVTG-GADVAAAFSS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 224 -NCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAE 302
Cdd:cd07133 176 lPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 303 EFTRKFGDAVRNMkLGTAYDfSVDMGSLISEAQLKTVSGHVDDATAKGAKVI-AGGKARPDIGPLFYEPTVLTNVAPEME 381
Cdd:cd07133 256 EFVAAAKAAVAKM-YPTLAD-NPDYTSIINERHYARLQGLLEDARAKGARVIeLNPAGEDFAATRKLPPTLVLNVTDDMR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 382 CAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSG--TVNvDEGYAFAWGSLsaPMGGMG 459
Cdd:cd07133 334 VMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGgvTIN-DTLLHVAQDDL--PFGGVG 410
|
410 420
....*....|....*....|..
gi 57116903 460 LSGVGRRHGPEGLLKYTESQTI 481
Cdd:cd07133 411 ASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
60-465 |
8.49e-71 |
|
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: 232.16 E-value: 8.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANyyarVCVDLLKPRKAQPLLPGIG 139
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID----ISIKAYHERTGERATPMAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 140 KTTVC-YQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGpGSVVG 218
Cdd:cd07095 89 GRAVLrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 219 TAITDN--CDYLMFTGSSATGSRLAEH-AGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIY 295
Cdd:cd07095 168 EALAAHegIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 296 VEKD-IAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKaRPDIGPLFYEPTVLt 374
Cdd:cd07095 248 VPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME-RLVAGTAFLSPGII- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 375 NVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAwgSLSAP 454
Cdd:cd07095 326 DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA--SSTAP 403
|
410
....*....|.
gi 57116903 455 MGGMGLSGVGR 465
Cdd:cd07095 404 FGGVGLSGNHR 414
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
63-482 |
2.15e-69 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 230.98 E-value: 2.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 63 WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKArWA-AQEEIVDLIANANYYARvcvDLLKPRKAQPLLPGIGKT 141
Cdd:PRK03137 89 WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKP-WAeADADTAEAIDFLEYYAR---QMLKLADGKPVESRPGEH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 142 -TVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTA 220
Cdd:PRK03137 165 nRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 221 ITDNCD--YLMFTGSSATGSRLAEHAGR---------RLIgfsAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCI 289
Cdd:PRK03137 245 LVDHPKtrFITFTGSREVGLRIYERAAKvqpgqiwlkRVI---AEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 290 SIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSvDMGSLISEAQLKTVSGHVDDATAKGaKVIAGGKARPDIGpLFYE 369
Cdd:PRK03137 322 ACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKG-YFIQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 370 PTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAfawG 449
Cdd:PRK03137 399 PTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCT---G 475
|
410 420 430
....*....|....*....|....*....|....*....
gi 57116903 450 SLSA--PMGGMGLSG----VGrrhGPEGLLKYTESQTIA 482
Cdd:PRK03137 476 AIVGyhPFGGFNMSGtdskAG---GPDYLLLFLQAKTVS 511
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
12-485 |
2.81e-69 |
|
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: 229.71 E-value: 2.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 12 LRNLAAIKDVAARPTRTIDeVF---TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREF 88
Cdd:cd07085 1 LKLFINGEWVESKTTEWLD-VYnpaTGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 89 LMDLLQAEAGKARWAAQEEI------VDLIANANYyarvcvdLLKPRKAQPLLPGIgKTTVCYQPKGVVGVISPWNYPMT 162
Cdd:cd07085 80 LARLITLEHGKTLADARGDVlrglevVEFACSIPH-------LLKGEYLENVARGI-DTYSYRQPLGVVAGITPFNFPAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 163 LTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVgTAITDNCDY--LMFTGSSATGSRL 240
Cdd:cd07085 152 IPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIkaVSFVGSTPVGEYI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 241 AEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTA 320
Cdd:cd07085 231 YERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 321 YDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKarpDIGPLFYE------PTVLTNVAPEMECAANETFGPVVSI 394
Cdd:cd07085 311 DDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGR---GVKVPGYEngnfvgPTILDNVTPDMKIYKEEIFGPVLSI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 395 YPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAfawgslsAPM-----GGMGLSGVGRRH-- 467
Cdd:cd07085 388 VRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIP-------VPLaffsfGGWKGSFFGDLHfy 460
|
490
....*....|....*...
gi 57116903 468 GPEGLLKYTESQTIaTAR 485
Cdd:cd07085 461 GKDGVRFYTQTKTV-TSR 477
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
33-481 |
2.03e-67 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 225.16 E-value: 2.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 33 FTGKPLTTIPVGTAADVEAAFAEARAA--QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIV 109
Cdd:PRK09847 43 VTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPiRHSLRDDIP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 110 DLIANANYYARVCVDL---LKPRKAQPLlpgigkTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQT 186
Cdd:PRK09847 123 GAARAIRWYAEAIDKVygeVATTSSHEL------AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 187 PYCALACAELLYRAGLPRALYAIVPGPGSVVGTAIT--DNCDYLMFTGSSATGSRLAEHAGR-RLIGFSAELGGKNPMIV 263
Cdd:PRK09847 197 PLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSrhNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 264 -ARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGH 342
Cdd:PRK09847 277 fADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 343 VDDATAKGAKVIAGgkaRPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGS 422
Cdd:PRK09847 357 IREGESKGQLLLDG---RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRD 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 57116903 423 TAEGQRIAARLRSGTVNVDEgyaFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTI 481
Cdd:PRK09847 434 LSRAHRMSRRLKAGSVFVNN---YNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
63-484 |
1.16e-66 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 224.30 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 63 WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVDLIANANYYA---------RVCVDllkprkaq 132
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPyEQSAKAELPMFARLFRYYAgwadkihglTVPAD-------- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 133 pllpGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPG 212
Cdd:PLN02466 185 ----GPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 213 PGSVVGTAITD--NCDYLMFTGSSATGSRLAEHAGR-RLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCI 289
Cdd:PLN02466 261 FGPTAGAALAShmDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCC 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 290 SIERIYVEKDIAEEFTRKfgDAVRNMK--LGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGpLF 367
Cdd:PLN02466 341 AGSRTFVHERVYDEFVEK--AKARALKrvVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKG-YY 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 368 YEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFa 447
Cdd:PLN02466 418 IQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVF- 496
|
410 420 430
....*....|....*....|....*....|....*..
gi 57116903 448 wgSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIATA 484
Cdd:PLN02466 497 --DAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTP 531
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
34-486 |
1.40e-64 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 217.04 E-value: 1.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:PRK13968 16 TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSAN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANYYARVCVDLLKPrkaQPLLPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALAC 193
Cdd:PRK13968 96 LCDWYAEHGPAMLKA---EPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 194 AELLYRAGLPRALYAIVPGPGSVVGTAITD-NCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKV 272
Cdd:PRK13968 173 AQVFKDAGIPQGVYGWLNADNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 273 AKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAK 352
Cdd:PRK13968 253 VKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGAR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 353 VIAGGKARPDIGPlFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAAR 432
Cdd:PRK13968 333 LLLGGEKIAGAGN-YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAAR 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 57116903 433 LRSGTVNVDeGYAFAWGSLSapMGGMGLSGVGRRHGPEGLLKYTESQTIATARV 486
Cdd:PRK13968 412 LECGGVFIN-GYCASDARVA--FGGVKKSGFGRELSHFGLHEFCNIQTVWKDRI 462
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
33-464 |
9.55e-64 |
|
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: 214.59 E-value: 9.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 33 FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKR-PVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDL 111
Cdd:cd07148 7 FDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 112 IANAnyyaRVCVDLLKPRKAQPLLPGIGKTT------VCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQ 185
Cdd:cd07148 87 IDGV----ELAADELGQLGGREIPMGLTPASagriafTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 186 TPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITD-NCDYLMFTGSSATG----SRLAehAGRRLigfSAELGGKNP 260
Cdd:cd07148 163 TPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDpRVAFFSFIGSARVGwmlrSKLA--PGTRC---ALEHGGAAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 261 MIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVS 340
Cdd:cd07148 238 VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 341 GHVDDATAKGAKVIAGGKArpdIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWA 420
Cdd:cd07148 318 EWVNEAVAAGARLLCGGKR---LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 57116903 421 GSTAEGQRIAARLRSGTVNVDEGYAFA--WgslsAPMGGMGLSGVG 464
Cdd:cd07148 395 KDLDVALKAVRRLDATAVMVNDHTAFRvdW----MPFAGRRQSGYG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
45-462 |
2.55e-63 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 214.05 E-value: 2.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 45 TAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANAN-----YYA 119
Cdd:PRK09457 35 TAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINKIAisiqaYHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 120 RVcvdllkPRKAQPlLPGiGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYR 199
Cdd:PRK09457 115 RT------GEKRSE-MAD-GAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 200 AGLPRALYAIVPGpGSVVGTAITDN--CDYLMFTGSSATGSRL-AEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAA 276
Cdd:PRK09457 187 AGLPAGVLNLVQG-GRETGKALAAHpdIDGLLFTGSANTGYLLhRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 277 TRACFSNAGQLCISIERIYVEKDI-AEEFTRKFGDAVRNMKLGtAYD-----FsvdMGSLISEAQLKTVSGHVDDATAKG 350
Cdd:PRK09457 266 IQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVG-RWDaepqpF---MGAVISEQAAQGLVAAQAQLLALG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 351 AKVIAGGKaRPDIGPLFYEPTVL--TNVApemECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQR 428
Cdd:PRK09457 342 GKSLLEMT-QLQAGTGLLTPGIIdvTGVA---ELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQ 417
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 57116903 429 IAARLRSGTVNvdegyafaW------GSLSAPMGGMGLSG 462
Cdd:PRK09457 418 FLLEIRAGIVN--------WnkpltgASSAAPFGGVGASG 449
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
63-482 |
3.10e-63 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 214.36 E-value: 3.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 63 WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLLKPRKAQPLLPGIGKTT 142
Cdd:cd07083 71 WKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNES 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 143 VcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAIT 222
Cdd:cd07083 151 F-YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 223 DN--CDYLMFTGSSATGSRLAEHAGRRLIGFS------AELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERI 294
Cdd:cd07083 230 EHerIRGINFTGSLETGKKIYEAAARLAPGQTwfkrlyVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 295 YVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGaKVIAGGKaRPDIGPLFYEPTVLT 374
Cdd:cd07083 310 ILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGK-RLEGEGYFVAPTVVE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 375 NVAPEMECAANETFGPVVSI--YPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAfawGSLS 452
Cdd:cd07083 388 EVPPKARIAQEEIFGPVLSVirYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKIT---GALV 464
|
410 420 430
....*....|....*....|....*....|...
gi 57116903 453 A--PMGGMGLSGVGRRHG-PEGLLKYTESQTIA 482
Cdd:cd07083 465 GvqPFGGFKLSGTNAKTGgPHYLRRFLEMKAVA 497
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
66-468 |
3.49e-60 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 206.03 E-value: 3.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 66 RPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQE-EIVDLIANANYYARVCVDLLKPRKA-QPLLPGIGKTTV 143
Cdd:PTZ00381 26 RPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMtEVLLTVAEIEHLLKHLDEYLKPEKVdTVGVFGPGKSYI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 144 CYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELL--YragLPRALYAIVPGpGSVVGTAI 221
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLtkY---LDPSYVRVIEG-GVEVTTEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 222 TDN-CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDI 300
Cdd:PTZ00381 182 LKEpFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 301 AEEFTRKFGDAVRNMkLGTAYDFSVDMGSLISEAQLKTVSGHVDDataKGAKVIAGGKArpDIGPLFYEPTVLTNVAPEM 380
Cdd:PTZ00381 262 KDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEV--DIENKYVAPTIIVNPDLDS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 381 ECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGyAFAWGSLSAPMGGMGL 460
Cdd:PTZ00381 336 PLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDC-VFHLLNPNLPFGGVGN 414
|
....*...
gi 57116903 461 SGVGRRHG 468
Cdd:PTZ00381 415 SGMGAYHG 422
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
34-465 |
4.16e-57 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 197.67 E-value: 4.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKA-RWAAQEEIVDLI 112
Cdd:cd07116 25 TGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPvRETLAADIPLAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 113 ANANYYARVCvdllkpRKAQPLLPGIGKTTVCY---QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYC 189
Cdd:cd07116 105 DHFRYFAGCI------RAQEGSISEIDENTVAYhfhEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPAS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 190 ALACAELLYRAgLPRALYAIVPGPGSVVGTAITDNCDY--LMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIV---- 263
Cdd:cd07116 179 ILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIakVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFfadv 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 264 --ARGANLDKVAKAATRACFsNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSG 341
Cdd:cd07116 258 mdADDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 342 HVDDATAKGAKVIAGGKAR---PDIGPLFYEPTVLTNvAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASV 418
Cdd:cd07116 337 YIDIGKEEGAEVLTGGERNelgGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGV 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 57116903 419 WAGSTAEGQRIAARLRSGTVNVDEGYAFAWGslsAPMGGMGLSGVGR 465
Cdd:cd07116 416 WTRDGNTAYRMGRGIQAGRVWTNCYHLYPAH---AAFGGYKQSGIGR 459
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
45-492 |
4.29e-56 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 195.36 E-value: 4.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 45 TAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIV---DLIAnanYYARV 121
Cdd:PLN00412 51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVrsgDLIS---YTAEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 122 CVDLLKPRK--AQPLLPGIGKTTVCYQ---PKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAEL 196
Cdd:PLN00412 128 GVRILGEGKflVSDSFPGNERNKYCLTskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHC 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 197 LYRAGLPRALYAIVPGPGSVVGTAITD----NCdyLMFTGSSaTGSRLAEHAGrrLIGFSAELGGKNPMIVARGANLDKV 272
Cdd:PLN00412 208 FHLAGFPKGLISCVTGKGSEIGDFLTMhpgvNC--ISFTGGD-TGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 273 AKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDfSVDMGSLISEAQLKTVSGHVDDATAKGAK 352
Cdd:PLN00412 283 AANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGAT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 353 VIAGGKARpdiGPLFYePTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAAR 432
Cdd:PLN00412 362 FCQEWKRE---GNLIW-PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDA 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 433 LRSGTVNVDEgyAFAWGSLSAPMGGMGLSGVGRrhgpEGLLKYTESQTIATARVFNLDPP 492
Cdd:PLN00412 438 METGTVQINS--APARGPDHFPFQGLKDSGIGS----QGITNSINMMTKVKSTVINLPKP 491
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
45-464 |
1.49e-54 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 198.17 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 45 TAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI---VDLianANYYARV 121
Cdd:PRK11905 588 SAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVreaVDF---LRYYAAQ 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 122 CVDLLKPRKAQPLlpgigkttvcyqpkGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAG 201
Cdd:PRK11905 665 ARRLLNGPGHKPL--------------GPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 202 LPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSR----LAEHAGrRLIGFSAELGGKNPMIVARGANLDKVAKA 275
Cdd:PRK11905 731 VPKDALQLLPGDGRTVGAALVADprIAGVMFTGSTEVARLiqrtLAKRSG-PPVPLIAETGGQNAMIVDSSALPEQVVAD 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 276 ATRACFSNAGQLCiSIERI-YVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVI 354
Cdd:PRK11905 810 VIASAFDSAGQRC-SALRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVH 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 355 AGGKARPDIGPLFYEPTV--LTNVApEMEcaaNETFGPVVSI--YPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIA 430
Cdd:PRK11905 889 QLPLPAETEKGTFVAPTLieIDSIS-DLE---REVFGPVLHVvrFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVT 964
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 57116903 431 ARLRSGTVNVDE-------GyafawgslSAPMGGMGLSGVG 464
Cdd:PRK11905 965 SRIRAGNIYVNRniigavvG--------VQPFGGEGLSGTG 997
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
64-471 |
2.39e-53 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 186.56 E-value: 2.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 64 AKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKArwaAQE----EIVDLIANANYYARVCVDLLKPRKAQ-PLLPGI 138
Cdd:cd07136 15 ATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKS---EFEaymtEIGFVLSEINYAIKHLKKWMKPKRVKtPLLNFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 139 GKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLyRAGLPRALYAIVPGpGSVVG 218
Cdd:cd07136 92 SKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKII-EETFDEEYVAVVEG-GVEEN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 219 TAITDNC-DYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVE 297
Cdd:cd07136 170 QELLDQKfDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 298 KDIAEEFTRKFGDAVRNMkLGTAYDFSVDMGSLISEAQLKTVSGHVDDatakgAKVIAGGKARPDIgpLFYEPTVLTNVA 377
Cdd:cd07136 250 ESVKEKFIKELKEEIKKF-YGEDPLESPDYGRIINEKHFDRLAGLLDN-----GKIVFGGNTDRET--LYIEPTILDNVT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 378 PEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSG--TVNvDEGYAFAWGSLsaPM 455
Cdd:cd07136 322 WDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggCIN-DTIMHLANPYL--PF 398
|
410
....*....|....*.
gi 57116903 456 GGMGLSGVGRRHGPEG 471
Cdd:cd07136 399 GGVGNSGMGSYHGKYS 414
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
45-481 |
9.22e-52 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 189.64 E-value: 9.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 45 TAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI---VDLIanaNYYARV 121
Cdd:PRK11904 583 DAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVreaVDFC---RYYAAQ 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 122 CVDLLkprkAQP-LLPGI-GKT-TVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLY 198
Cdd:PRK11904 660 ARRLF----GAPeKLPGPtGESnELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLH 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 199 RAGLPRALYAIVPGPGSVVGTAIT--DNCDYLMFTGSSATGSR----LAEHAGrRLIGFSAELGGKNPMIVARGANLDKV 272
Cdd:PRK11904 736 EAGIPKDVLQLLPGDGATVGAALTadPRIAGVAFTGSTETARIinrtLAARDG-PIVPLIAETGGQNAMIVDSTALPEQV 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 273 AKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATaKGAK 352
Cdd:PRK11904 815 VDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMK-REAR 893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 353 VIAGGKARPDIGPLFYeptvltnVAP---EMECAA---NETFGPV--VSIYPVADVDEAVEKANDTDYGLNASVWA--GS 422
Cdd:PRK11904 894 LLAQLPLPAGTENGHF-------VAPtafEIDSISqleREVFGPIlhVIRYKASDLDKVIDAINATGYGLTLGIHSriEE 966
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57116903 423 TAEgqRIAARLRSGTVNVDE-------GyafawgslSAPMGGMGLSGVG-RRHGPEGLLKYTESQTI 481
Cdd:PRK11904 967 TAD--RIADRVRVGNVYVNRnqigavvG--------VQPFGGQGLSGTGpKAGGPHYLLRFATEKTV 1023
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
34-419 |
8.30e-50 |
|
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: 177.78 E-value: 8.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 34 TGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIA 113
Cdd:cd07130 21 NGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 114 NANY--------YARVcvdLLKPRKAQPLLPGigkttvcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQ 185
Cdd:cd07130 101 ICDFavglsrqlYGLT---IPSERPGHRMMEQ-------WNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 186 TPYCALAC----AELLYRAGLPRALYAIVPGpGSVVGTAITDNCDY--LMFTGSSATGSRLAEHAGRRLIGFSAELGGKN 259
Cdd:cd07130 171 TPLTAIAVtkivARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVplVSFTGSTAVGRQVGQAVAARFGRSLLELGGNN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 260 PMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTV 339
Cdd:cd07130 250 AIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 340 SGHVDDATAKGAKVIAGGKaRPDIGPLFYEPTVLTnVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVW 419
Cdd:cd07130 330 LAAIEEAKSQGGTVLFGGK-VIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIF 407
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
66-476 |
2.20e-49 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 175.87 E-value: 2.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 66 RPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQ-EEIVDLIANANYYARVCVDLLKPRKAQPLLPGIGKTTVC 144
Cdd:cd07132 17 RPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVlSEILLVKNEIKYAISNLPEWMKPEPVKKNLATLLDDVYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 145 Y-QPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELL--YragLPRALYAIVPGpGSVVGTAI 221
Cdd:cd07132 97 YkEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkY---LDKECYPVVLG-GVEETTEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 222 TDN-CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDI 300
Cdd:cd07132 173 LKQrFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 301 AEEFTRKFGDAVRNMkLGTAYDFSVDMGSLISEAQLKTVSGHVddataKGAKVIAGGkaRPDIGPLFYEPTVLTNVAPE- 379
Cdd:cd07132 253 QEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGG--QTDEKERYIAPTVLTDVKPSd 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 380 --MEcaaNETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAWGSlSAPMGG 457
Cdd:cd07132 325 pvMQ---EEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLD-SLPFGG 400
|
410
....*....|....*....
gi 57116903 458 MGLSGVGRRHGpegllKYT 476
Cdd:cd07132 401 VGNSGMGAYHG-----KYS 414
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
45-464 |
8.77e-49 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 181.29 E-value: 8.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 45 TAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI---VDLianANYYArv 121
Cdd:COG4230 591 TAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVreaVDF---CRYYA-- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 122 cvdllkpRKAQPLLPGigktTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAG 201
Cdd:COG4230 666 -------AQARRLFAA----PTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAG 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 202 LPRALYAIVPGPGSVVGTAITDN--CDYLMFTGSSATGSR----LAEHAGrRLIGFSAELGGKNPMIVARGANLDKVAKA 275
Cdd:COG4230 735 VPADVLQLLPGDGETVGAALVADprIAGVAFTGSTETARLinrtLAARDG-PIVPLIAETGGQNAMIVDSSALPEQVVDD 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 276 ATRACFSNAGQLCiSIERI-YVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVI 354
Cdd:COG4230 814 VLASAFDSAGQRC-SALRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVH 892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 355 AGGKARPDIGPLFYEPTV--LTNVApEMEcaaNETFGPVVSI--YPVADVDEAVEKANDTDYGLNASVWA--GSTAEgqR 428
Cdd:COG4230 893 QLPLPEECANGTFVAPTLieIDSIS-DLE---REVFGPVLHVvrYKADELDKVIDAINATGYGLTLGVHSriDETID--R 966
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 57116903 429 IAARLRSGTVNVDE-------GyafawgslSAPMGGMGLSGVG 464
Cdd:COG4230 967 VAARARVGNVYVNRniigavvG--------VQPFGGEGLSGTG 1001
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
63-479 |
4.11e-48 |
|
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: 173.94 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 63 WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLLKPRKAQPLlpgigktt 142
Cdd:TIGR01238 90 WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVESR-------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 143 vcyqpkGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAIT 222
Cdd:TIGR01238 162 ------GVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 223 DNCDY--LMFTGSSATGSRLAEHAGRRL---IGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVE 297
Cdd:TIGR01238 236 SDPRIagVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 298 KDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKV--IAGGKARPDIGPLFYEPTV--L 373
Cdd:TIGR01238 316 EDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqLTLDDSRACQHGTFVAPTLfeL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 374 TNVAPEMEcaanETFGPVVSI--YPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAWGSL 451
Cdd:TIGR01238 396 DDIAELSE----EVFGPVLHVvrYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGV 471
|
410 420
....*....|....*....|....*....
gi 57116903 452 SaPMGGMGLSGVG-RRHGPEGLLKYTESQ 479
Cdd:TIGR01238 472 Q-PFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
35-420 |
1.69e-42 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 158.52 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 35 GKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVieNREFLMDLLQAEA-GKARWAAQEEI---VD 110
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLL--SGKYRYELNAATMlGQGKNVWQAEIdaaCE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 111 LIANANYYARVCVDLLKprkAQPLLPGIG-KTTVCYQP-KGVVGVISPWNYPMTLTVSDSVPALVaGNAVVLKPDSQTPY 188
Cdd:cd07123 135 LIDFLRFNVKYAEELYA---QQPLSSPAGvWNRLEYRPlEGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 189 CALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDY--LMFTGSSATGSRL----AEHAGR-----RLIGfsaELGG 257
Cdd:cd07123 211 SNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLagLHFTGSTPTFKSLwkqiGENLDRyrtypRIVG---ETGG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 258 KNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLK 337
Cdd:cd07123 288 KNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 338 TVSGHVDDA-TAKGAKVIAGGKARPDIGpLFYEPTVLTNVAPEMECAANETFGPVVSI--YPVADVDEAVEKANDT-DYG 413
Cdd:cd07123 368 RIKGYIDHAkSDPEAEIIAGGKCDDSVG-YFVEPTVIETTDPKHKLMTEEIFGPVLTVyvYPDSDFEETLELVDTTsPYA 446
|
....*..
gi 57116903 414 LNASVWA 420
Cdd:cd07123 447 LTGAIFA 453
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
45-468 |
7.10e-39 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 151.66 E-value: 7.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 45 TAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKArwaaqeeivdlIANANYYARVCVD 124
Cdd:PRK11809 680 TPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKT-----------FSNAIAEVREAVD 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 125 LLKPRKAQpLLPGIGKTTvcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPR 204
Cdd:PRK11809 749 FLRYYAGQ-VRDDFDNDT--HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPA 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 205 ALYAIVPGPGSVVGTAIT--DNCDYLMFTGSSATGSRLAEH-AGR-----RLIGFSAELGGKNPMIVARGANLDKVAKAA 276
Cdd:PRK11809 826 GVVQLLPGRGETVGAALVadARVRGVMFTGSTEVARLLQRNlAGRldpqgRPIPLIAETGGQNAMIVDSSALTEQVVADV 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 277 TRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAG 356
Cdd:PRK11809 906 LASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQA 985
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 357 gkARPDIGPL----FYEPTV--LTNVApEMEcaaNETFGPVVSI--YPVADVDEAVEKANDTDYGLNASVWAGSTAEGQR 428
Cdd:PRK11809 986 --ARENSEDWqsgtFVPPTLieLDSFD-ELK---REVFGPVLHVvrYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQ 1059
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 57116903 429 IAARLRSGTVNVDEGYAFAWGSLSaPMGGMGLSGVGRRHG 468
Cdd:PRK11809 1060 VTGSAHVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTGPKAG 1098
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
66-468 |
7.46e-38 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 144.09 E-value: 7.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 66 RPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAA-QEEIVDLIANANYYARVCVDLLKPRKAQ-PLLPGIGKTTV 143
Cdd:cd07137 18 RSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKWMAPEKVKtPLTTFPAKAEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 144 CYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGsvVGTAITD 223
Cdd:cd07137 98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVP--ETTALLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 224 N-CDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACF-SNAGQLCISIERIYVEKDIA 301
Cdd:cd07137 176 QkWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 302 EEFTrkfgDAVRNMKL---GTAYDFSVDMGSLISEAQLKTVSGHVDDATAKgAKVIAGGkaRPDIGPLFYEPTVLTNVAP 378
Cdd:cd07137 256 PTLI----DALKNTLEkffGENPKESKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGG--ERDEKNLYIEPTILLDPPL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 379 EMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGyAFAWGSLSAPMGGM 458
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDT-VVQYAIDTLPFGGV 407
|
410
....*....|
gi 57116903 459 GLSGVGRRHG 468
Cdd:cd07137 408 GESGFGAYHG 417
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
11-441 |
6.77e-36 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 141.04 E-value: 6.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 11 RLRNLAAIKDVAARPTRTIDEV--FTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREF 88
Cdd:PLN02419 113 RVPNLIGGSFVESQSSSFIDVInpATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 89 LMDLLQAEAGKARWAAQEEI---VDLIANANYYARVcvdllkprKAQPLLPGIGKTTVCY---QPKGVVGVISPWNYPMT 162
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIfrgLEVVEHACGMATL--------QMGEYLPNVSNGVDTYsirEPLGVCAGICPFNFPAM 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 163 LTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVgTAITDNCDY--LMFTGSSATGSRL 240
Cdd:PLN02419 265 IPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIraVSFVGSNTAGMHI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 241 AEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDiAEEFTRKFGDAVRNMKLGTA 320
Cdd:PLN02419 344 YARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 321 YDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKarpDIGPLFYE------PTVLTNVAPEMECAANETFGPVVSI 394
Cdd:PLN02419 423 SEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGR---DIVVPGYEkgnfigPTILSGVTPDMECYKEEIFGPVLVC 499
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 57116903 395 YPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVD 441
Cdd:PLN02419 500 MQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
71-476 |
7.15e-36 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 139.48 E-value: 7.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 71 RAAVIRRYRDLVIENREFLMDLLQAEAGKARWAA-QEEIVDLIANANYYARVCVDLLKPRKAQ-PLLPGIGKTTVCYQPK 148
Cdd:PLN02203 30 RKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyRDEVGVLTKSANLALSNLKKWMAPKKAKlPLVAFPATAEVVPEPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 149 GVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGsvVGTAITD-NCDY 227
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEGGPA--VGEQLLQhKWDK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 228 LMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIV---ARGANLDKVAKAATRACFSN-AGQLCISIERIYVEkdiaEE 303
Cdd:PLN02203 188 IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVE----ER 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 304 FTRKFGDAVRNMK---LGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKgAKVIAGGKARPDigPLFYEPTVLTNVAPEM 380
Cdd:PLN02203 264 FAPILIELLKSTIkkfFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDEK--KLFIEPTILLNPPLDS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 381 ECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGyAFAWGSLSAPMGGMGL 460
Cdd:PLN02203 341 DIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDA-IIQYACDSLPFGGVGE 419
|
410
....*....|....*.
gi 57116903 461 SGVGRRHGpegllKYT 476
Cdd:PLN02203 420 SGFGRYHG-----KYS 430
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
63-419 |
4.19e-29 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 120.32 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 63 WAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGK---ARWAAQEEIVDLIANANYYARVCVDLLKPRKAqpllPGIG 139
Cdd:PLN02315 72 WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKilaEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSER----PNHM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 140 KTTVcYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALA----CAELLYRAGLPRALYAIVPGpGS 215
Cdd:PLN02315 148 MMEV-WNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCG-GA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 216 VVGTAITDNC--DYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIER 293
Cdd:PLN02315 226 EIGEAIAKDTriPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 294 IYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGPlFYEPTVL 373
Cdd:PLN02315 306 LLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGN-FVQPTIV 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 57116903 374 tNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVW 419
Cdd:PLN02315 385 -EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIF 429
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
126-468 |
7.83e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 116.30 E-value: 7.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 126 LKPRKAQPLLPGI-GKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPR 204
Cdd:PLN02174 90 MAPEKAKTSLTTFpASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 205 ALyAIVPGPGSVVGTAITDNCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAK---AATRACf 281
Cdd:PLN02174 170 AV-RVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRriiAGKWGC- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 282 sNAGQLCISIERIYVEKdiaeEFTRKFGDAVRnMKLGTAYDF----SVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGG 357
Cdd:PLN02174 248 -NNGQACISPDYILTTK----EYAPKVIDAMK-KELETFYGKnpmeSKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 358 KARPDigpLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGT 437
Cdd:PLN02174 322 KDREN---LKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGG 398
|
330 340 350
....*....|....*....|....*....|.
gi 57116903 438 VNVDEgYAFAWGSLSAPMGGMGLSGVGRRHG 468
Cdd:PLN02174 399 IVVND-IAVHLALHTLPFGGVGESGMGAYHG 428
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
147-418 |
2.28e-23 |
|
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: 103.12 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 147 PKGVVGV-ISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAG-LPR-ALYAIVPGPGSVVGTaiTD 223
Cdd:cd07128 143 PRRGVAVhINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEgALQLICGSVGDLLDH--LG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 224 NCDYLMFTGSSATGSRLAEHAG--RRLIGFSAELGGKNPMIVARGAN-----LDKVAKAATRACFSNAGQLCISIERIYV 296
Cdd:cd07128 221 EQDVVAFTGSAATAAKLRAHPNivARSIRFNAEADSLNAAILGPDATpgtpeFDLFVKEVAREMTVKAGQKCTAIRRAFV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 297 EKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAkGAKVIAGGKARPDIGPL------FYEP 370
Cdd:cd07128 301 PEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLA-EAEVVFGGPDRFEVVGAdaekgaFFPP 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 57116903 371 TVLTNVAPEMECAANET--FGPVVSIYPVADVDEAVEKANDTDYGLNASV 418
Cdd:cd07128 380 TLLLCDDPDAATAVHDVeaFGPVATLMPYDSLAEAIELAARGRGSLVASV 429
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
70-430 |
4.56e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.48 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 70 ERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLlkpRKAQPLLPG----IGKTT--- 142
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAAL---GDARLLRDGeavqLGKDPafq 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 143 ---VCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAG-LPRALYAIVPGPGSVVG 218
Cdd:PRK11903 141 gqhVLVPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 219 TAITDnCDYLMFTGSSATGSRLAEHAG--RRLIGFSAELGGKN-----PMIVARGANLDKVAKAATRACFSNAGQLCISI 291
Cdd:PRK11903 221 DHLQP-FDVVSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNsallgPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 292 ERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDdATAKGAKVIAGGKARPDIGP-----L 366
Cdd:PRK11903 300 RRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDAdpavaA 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57116903 367 FYEPTVLTNVAPEMECAANET--FGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIA 430
Cdd:PRK11903 379 CVGPTLLGASDPDAATAVHDVevFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
147-471 |
5.47e-22 |
|
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: 98.46 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 147 PKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAG-LPRALYAIVPGPGSvVGTAITD-- 223
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGK-TMQALLLhp 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 224 NCDYLMFTGSSATGSRLAEHAgrRLIGFSAELGGKNPMIVARGAN-LDKVAKAATRACFSNAGQLCISIERIYVEKDIAe 302
Cdd:cd07084 179 NPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWS- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 303 efTRKFGDAVRNmKLGTaydfSVDMGSLISEAQLKTVSGHVDDATAK-GAKVIAGGKARPDIG-PLFYEPTVLTNVApeM 380
Cdd:cd07084 256 --KTPLVEKLKA-LLAR----RKLEDLLLGPVQTFTTLAMIAHMENLlGSVLLFSGKELKNHSiPSIYGACVASALF--V 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 381 ECAAN---------ETFGPVVSIYPVADVDEA--VEKANDTDYGLNASVWAGSTAEGQRIAARL-RSGTVnvdegYAFAW 448
Cdd:cd07084 327 PIDEIlktyelvteEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLwVAGRT-----YAILR 401
|
330 340
....*....|....*....|....*
gi 57116903 449 GslsaPMGG--MGLSGVGRRHGPEG 471
Cdd:cd07084 402 G----RTGVapNQNHGGGPAADPRG 422
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
55-434 |
1.22e-11 |
|
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: 66.80 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 55 EARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEI------VDLIANA---NYYARVCVDL 125
Cdd:cd07129 7 AAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELgrttgqLRLFADLvreGSWLDARIDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 126 LKPRKAQPLLPGIgktTVCYQPKGVVGVISPWNYPMTLTVS--DSVPALVAGNAVVLKPDSQTPYCALACAELLYRA--- 200
Cdd:cd07129 87 ADPDRQPLPRPDL---RRMLVPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAHPAHPGTSELVARAIRAAlra 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 201 -GLPRALYAIVPGPGSVVGTAITDncDYLM----FTGSSATGSRLAEHAGRRL--IGFSAELGGKNPMIVARGA---NLD 270
Cdd:cd07129 164 tGLPAGVFSLLQGGGREVGVALVK--HPAIkavgFTGSRRGGRALFDAAAARPepIPFYAELGSVNPVFILPGAlaeRGE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 271 KVAKAATRACFSNAGQLCISIERIYVEKDIA-EEFTRKFGDAVRNMKLGTaydfsvdmgsLISEAQLKTVSGHVDD-ATA 348
Cdd:cd07129 242 AIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQT----------MLTPGIAEAYRQGVEAlAAA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 349 KGAKVIAGGKARPdiGPLFYEPTVL-TNVAPEMECAA--NETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWA--GST 423
Cdd:cd07129 312 PGVRVLAGGAAAE--GGNQAAPTLFkVDAAAFLADPAlqEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGeeDDL 389
|
410
....*....|.
gi 57116903 424 AEGQRIAARLR 434
Cdd:cd07129 390 ALARELLPVLE 400
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
71-407 |
1.44e-11 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 66.09 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 71 RAAVIRRYRDLVIENREFLMDLLQAEAGK------ARWAAQEEIVDLIANANYYARVCVDLLKPRKAQPLLPGIGKTTVC 144
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAyirsliANWIAMMGCSESKLYKNIDTERGITASVGHIQDVLLPDNGETYVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 145 YQPKGVVGVISPWNYPmTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRA---GLPRALYAIVPGPGSVVGTAI 221
Cdd:cd07077 98 AFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDELAEEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 222 T--DNCDYLMFTGSSATGSRLAEHA-GRRLIGFSAelgGKNPMIVARGANLDKVAKAATRACFSNaGQLCISIERIYVEK 298
Cdd:cd07077 177 LshPKIDLIVATGGRDAVDAAVKHSpHIPVIGFGA---GNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 299 DIAEEFTRKFGDAVRNMKLgtaydfsvdmgsliseaqlktvsghvddatakgaKVIAGGKarpdigPLFYEPTvltnvaP 378
Cdd:cd07077 253 DVLDPLYEEFKLKLVVEGL----------------------------------KVPQETK------PLSKETT------P 286
|
330 340
....*....|....*....|....*....
gi 57116903 379 EMECAANETFGPVVSIYPVADVDEAVEKA 407
Cdd:cd07077 287 SFDDEALESMTPLECQFRVLDVISAVENA 315
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
147-437 |
2.11e-11 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 65.98 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 147 PKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITD-NC 225
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEaNP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 226 DYLMFTGSSATGSRLA-EHAGRRLI---GFSAELGGKNPmivargANLDKVAKAATRACFSNAGQLCISIERIYVEKDIA 301
Cdd:cd07126 222 RMTLFTGSSKVAERLAlELHGKVKLedaGFDWKILGPDV------SDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 302 EE-FTRKFGDAVRNMKLGtayDFSVdmGSLISEAQlKTVSGHVDDATA-KGAKVIAGGK-----ARPDI-GPlfYEPTVL 373
Cdd:cd07126 296 QAgILDKLKALAEQRKLE---DLTI--GPVLTWTT-ERILDHVDKLLAiPGAKVLFGGKpltnhSIPSIyGA--YEPTAV 367
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57116903 374 -----TNVAPE-MECAANETFGP--VVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGT 437
Cdd:cd07126 368 fvpleEIAIEEnFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGT 439
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
60-407 |
2.14e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 62.67 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARwaAQEEIVDLIANANYYARVCVDLLKPRKAQPLLPGIg 139
Cdd:cd07081 12 QQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGR--VEDKVIKNHFAAEYIYNVYKDEKTCGVLTGDENGG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 140 kTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRA----GLPRALYAIVPGPGS 215
Cdd:cd07081 89 -TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 216 VVGTAITD--NCDYLMFTGSSATgSRLAEHAGRRLIGFSAelgGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIER 293
Cdd:cd07081 168 ELAQRLMKfpGIGLLLATGGPAV-VKAAYSSGKPAIGVGA---GNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 294 IYVEKDIAEEFTRKFGDAvrnmklgTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKV--IAGGKARPDIGPLFYEPT 371
Cdd:cd07081 244 VIVVDSVYDEVMRLFEGQ-------GAYKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIaaAAGLKVPQETRILIGEVT 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 57116903 372 VLTnvapEMECAANETFGPVVSIYPVADVDEAVEKA 407
Cdd:cd07081 317 SLA----EHEPFAHEKLSPVLAMYRAANFADADAKA 348
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
147-407 |
3.18e-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: 62.50 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 147 PKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPdSQTPYCALA-----CAELLYRAGLPRALYAIV---PGPGSVVG 218
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKP-HPAAILPLAitvqvAREVLAEAGFDPNLVTLAadtPEEPIAQT 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 219 TAITDNCDYLMFTGSSATGSRLAEHAGRRLIgfSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEK 298
Cdd:cd07127 272 LATRPEVRIIDFTGSNAFGDWLEANARQAQV--YTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPR 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 299 D-IAEEFTRKFGDAVRNmKLGTAYD-FSVD-------MGSLISEAQLKTVSghvddATAKGAKVIAGGKAR--PDI-GPL 366
Cdd:cd07127 350 DgIQTDDGRKSFDEVAA-DLAAAIDgLLADparaaalLGAIQSPDTLARIA-----EARQLGEVLLASEAVahPEFpDAR 423
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 57116903 367 FYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKA 407
Cdd:cd07127 424 VRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
60-407 |
5.22e-10 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 61.48 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQeeivdliananyyarvcvdLLKPRKAQPLLPGI- 138
Cdd:cd07121 17 QKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDK-------------------IAKNHLAAEKTPGTe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 139 -----------GKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELL----YRAGLP 203
Cdd:cd07121 78 dltttawsgdnGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELInkaiAEAGGP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 204 RALYAIVPGPGSVVGTAITDNCDYLMFTgssATGS----RLAEHAGRRLIGFSAelgGKNPMIVARGANLDKVAKAATRA 279
Cdd:cd07121 158 DNLVVTVEEPTIETTNELMAHPDINLLV---VTGGpavvKAALSSGKKAIGAGA---GNPPVVVDETADIEKAARDIVQG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 280 C-FSNaGQLCISIERIYVEKDIAEEFtrkfgdaVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDAT--AKGAKVI-- 354
Cdd:cd07121 232 AsFDN-NLPCIAEKEVIAVDSVADYL-------IAAMQRNGAYVLNDEQAEQLLEVVLLTNKGATPNKKwvGKDASKIlk 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 57116903 355 -AGGKARPDIGPLFYEptvltnVAPEMECAANETFGPVVSIYPVADVDEAVEKA 407
Cdd:cd07121 304 aAGIEVPADIRLIIVE------TDKDHPFVVEEQMMPILPVVRVKNFDEAIELA 351
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
60-407 |
3.72e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 55.68 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 60 QTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQeeivdliananyyarvcvdLLKPRKAQPLLPGI- 138
Cdd:PRK15398 49 QQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDK-------------------IAKNVAAAEKTPGVe 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 139 -----------GKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELL----YRAGLP 203
Cdd:PRK15398 110 dlttealtgdnGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLneaiVAAGGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 204 RALYAIVPGPGSVVGTAITDNCDYLMFTgssATGS----RLAEHAGRRLIGFSAelgGKNPMIVARGANLDKVAKAATRA 279
Cdd:PRK15398 190 ENLVVTVAEPTIETAQRLMKHPGIALLV---VTGGpavvKAAMKSGKKAIGAGA---GNPPVVVDETADIEKAARDIVKG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 280 C-FSNaGQLCISIERIYVEKDIAEEFtrkfgdaVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVI---A 355
Cdd:PRK15398 264 AsFDN-NLPCIAEKEVIVVDSVADEL-------MRLMEKNGAVLLTAEQAEKLQKVVLKNGGTVNKKWVGKDAAKIleaA 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 57116903 356 GGKARPDIGPLFYEptvltnVAPEMECAANETFGPVVSIYPVADVDEAVEKA 407
Cdd:PRK15398 336 GINVPKDTRLLIVE------TDANHPFVVTELMMPVLPVVRVKDVDEAIALA 381
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
145-314 |
3.72e-07 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 52.44 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 145 YQPKGVVGVISPWNYPMtLTVSDSVPALVAGNAVVLKPDSQTPYCALAC----AELLYRAGLPRALyAIVPGPGS--VVG 218
Cdd:pfam05893 86 AFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSSDPFTAAALlasfADLDPTHPLADSL-SVVYWDGGstQLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 219 TAITDNCDYLMFTGSSATGSRLAEHA--GRRLIGFSAELGgknPMIVARGANLDKVA-KAATRACFSNAgQLCISIERIY 295
Cdd:pfam05893 164 DLIVANADVVIAWGGEDAINAIRECLkpGKQWIDFGAKIS---FAVVDREAALDKAAeRAADDICVFDQ-QACLSPQTVF 239
|
170 180
....*....|....*....|..
gi 57116903 296 VEKD---IAEEFTRKFGDAVRN 314
Cdd:pfam05893 240 VESDdkiTPDEFAERLAAALAK 261
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
145-314 |
1.51e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 41.11 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 145 YQPKGVVGVISPWNYPmTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELL--YRAGLP--RALYAIV-PGPGSVVGT 219
Cdd:cd07080 110 AQPRGLVVHIIAGNVP-LLPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLadVDPNHPltDSISVVYwPGGDAELEE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57116903 220 AITDNCDYLMFTGSSAT----GSRLAEHAgrRLIGFSAELGGKnpmIVARGA----NLDKVAKAATR-ACFSNAgQLCIS 290
Cdd:cd07080 189 RILASADAVVAWGGEEAvkaiRSLLPPGC--RLIDFGPKYSFA---VIDREAleseKLAEVADALAEdICRYDQ-QACSS 262
|
170 180
....*....|....*....|....*..
gi 57116903 291 IERIYVEKDIAE---EFTRKFGDAVRN 314
Cdd:cd07080 263 PQVVFVEKDDDEelrEFAEALAAALER 289
|
|
| |
