|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
69-531 |
0e+00 |
|
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: 788.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEI 148
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTTCEKITWLLDEGEKWLKPEYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHAS 228
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 229 WSGCFYFRIIQAALAAVGAPDNLVHIITGFAETGQALVSSV--DKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFI 306
Cdd:cd07098 161 WSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPviDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 307 VCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNL 386
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 387 VNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVF 466
Cdd:cd07098 321 VADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286994 467 SGNQKRAIKIASQLHCGVAAINDFASSYMCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVVEDR 531
Cdd:cd07098 401 GKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTEDR 465
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
71-528 |
1.82e-163 |
|
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: 474.02 E-value: 1.82e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEIMT 150
Cdd:cd07099 3 PATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA-GLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TCEKITWLLDEGEKWLKPEYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWS 230
Cdd:cd07099 82 ALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 231 GCFyfriIQAALAAVGAPDNLVHIITGFAETGQALVSS-VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCE 309
Cdd:cd07099 162 GEL----LAEAWAAAGPPQGVLQVVTGDGATGAALIDAgVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 310 DVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVND 389
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 390 AVDKGAEIAGRGSFGHLGEdavdQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGN 469
Cdd:cd07099 318 AVAKGAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286994 470 QKRAIKIASQLHCGVAAINDFASSYMCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
92-529 |
1.90e-160 |
|
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: 465.53 E-value: 1.90e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 92 VAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTmVDASLGEIMTTCEKITWLLDEGEKWLKPEYR 171
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRLHGEVIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 172 ScgrSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNL 251
Cdd:cd07078 83 S---PDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA----GLPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 252 VHIITGFA-ETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSS 328
Cdd:cd07078 156 LNVVTGDGdEVGAALASHprVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 329 GQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGE 408
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 409 DAvdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIN 488
Cdd:cd07078 316 GY---FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1002286994 489 DFaSSYMCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVVE 529
Cdd:cd07078 393 DY-SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
61-527 |
2.06e-147 |
|
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: 433.50 E-value: 2.06e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 61 AQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTM 140
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 141 VDAsLGEIMTTCEKITWLLDEGEKwLKPEYRSCGRSMLhkkAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAV 220
Cdd:pfam00171 84 AEA-RGEVDRAIDVLRYYAGLARR-LDGETLPSDPGRL---AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 221 IKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTL 297
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEA----GLPAGVLNVVTGSgAEVGEALVEHpdVRKVSFTGSTAVGRHIAEAAAQNLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 298 ELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMI 377
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 378 EHSEKLQNLVNDAVDKGAEIAGRGSFGhlgeDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDS 457
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAG----LDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDT 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 458 KYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCqSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:pfam00171 391 EYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAD-GLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
71-531 |
5.66e-146 |
|
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: 430.32 E-value: 5.66e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEIMT 150
Cdd:COG1012 28 PATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA-RGEVDR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TCEKITWLLDEGEKwLKPEYRSCGRSmlHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWS 230
Cdd:COG1012 107 AADFLRYYAGEARR-LYGETIPSDAP--GTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 231 GCFYFRIIQAAlaavGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIV 307
Cdd:COG1012 184 ALLLAELLEEA----GLPAGVLNVVTGDgSEVGAALVAHpdVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 308 CEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLV 387
Cdd:COG1012 260 LDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 388 NDAVDKGAEI-AGrgsfGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVF 466
Cdd:COG1012 340 EDAVAEGAELlTG----GRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVF 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286994 467 SGNQKRAIKIASQLHCGVAAINDFASSYMCQsLPFGGVKDSGFGRFAGVEGLRACCLVKAVVEDR 531
Cdd:COG1012 416 TRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
95-529 |
6.63e-123 |
|
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: 367.32 E-value: 6.63e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 95 ARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVdASLGEIMTTCEKITWLLDEGEKWLKPEYRScg 174
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPELPS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 175 rSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHI 254
Cdd:cd06534 80 -PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA----GLPPGVVNV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 255 ITGFA-ETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQN 331
Cdd:cd06534 155 VPGGGdEVGAALLSHprVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 332 CAGAERFYVHKDIYSTFVSQVVkiiksisvgpplsgrydmgaicmiehseklqnlvndavdkgaeiagrgsfghlgedav 411
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEKLV---------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 412 dqffppTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFA 491
Cdd:cd06534 257 ------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSS 330
|
410 420 430
....*....|....*....|....*....|....*...
gi 1002286994 492 SSYMcQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVVE 529
Cdd:cd06534 331 IGVG-PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
71-527 |
1.21e-116 |
|
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: 354.05 E-value: 1.21e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEIMT 150
Cdd:cd07103 4 PATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RGEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TCEKITWLLDEGEkwlkpeyRSCGR----SMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEH 226
Cdd:cd07103 83 AASFLEWFAEEAR-------RIYGRtipsPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 227 ASWSGCFYFRIIQAAlaavGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKD 303
Cdd:cd07103 156 TPLSALALAELAEEA----GLPAGVLNVVTGSpAEIGEALCASprVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 304 AFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAicMIEHS--E 381
Cdd:cd07103 232 PFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGP--LINERavE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 382 KLQNLVNDAVDKGAEIAGRGSFGHLGedavDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGL 461
Cdd:cd07103 310 KVEALVEDAVAKGAKVLTGGKRLGLG----GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 462 GCAVFSGNQKRAIKIASQLHCGVAAINDFASSymCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07103 386 AAYVFTRDLARAWRVAEALEAGMVGINTGLIS--DAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
70-518 |
3.46e-107 |
|
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: 330.04 E-value: 3.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 70 EPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRqflRILLKY---ILEHQDLICEISSRDTGKTMVDAsLG 146
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERA---AVFLRFhdlVLERRDELLDLIQLETGKARRHA-FE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 147 EIMTTCEKITWLLDEGEKWLKPEYRSCGRSMLhKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEH 226
Cdd:cd07101 78 EVLDVAIVARYYARRAERLLKPRRRRGAIPVL-TRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 227 ASWSGCFYFRIIQAAlaavGAPDNLVHIITG-FAETGQALVSSVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAF 305
Cdd:cd07101 157 TALTALWAVELLIEA----GLPRDLWQVVTGpGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 306 IVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQN 385
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 386 LVNDAVDKGAE-IAGrgsfGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCA 464
Cdd:cd07101 313 HVDDAVAKGATvLAG----GRARPDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1002286994 465 VFSGNQKRAIKIASQLHCGVAAIND-FASSYMCQSLPFGGVKDSGFGRFAGVEGL 518
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNEgYAAAWASIDAPMGGMKDSGLGRRHGAEGL 443
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
71-528 |
1.33e-106 |
|
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: 328.74 E-value: 1.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKA--QKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTM--VDASLG 146
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIreTRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 147 EIMTT-------CEKItwlldEGEkWL---KPEYRSCGRSMlhkkakvefyPLGVIGAIVSWNYPFHNVFN---PMLAAi 213
Cdd:cd07114 84 YLAEWyryyaglADKI-----EGA-VIpvdKGDYLNFTRRE----------PLGVVAAITPWNSPLLLLAKklaPALAA- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 214 fsGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASD 290
Cdd:cd07114 147 --GNTVVLKPSEHTPASTLELAKLAEEA----GFPPGVVNVVTGFgPETGEALVEHplVAKIAFTGGTETGRHIARAAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 291 TLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYD 370
Cdd:cd07114 221 NLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 371 MGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEV 450
Cdd:cd07114 301 MGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEA 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286994 451 VKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDF-ASSYMcqsLPFGGVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:cd07114 381 IALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTYrALSPS---SPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
71-520 |
1.65e-106 |
|
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: 328.05 E-value: 1.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTmVDASLGEIMT 150
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP-IAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TCEKITWLLDEGEKWLKPeyrscgrSMLHKKAKVEFY----PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEH 226
Cdd:cd07102 82 MLERARYMISIAEEALAD-------IRVPEKDGFERYirrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 227 ASWSGCFyfriIQAALAAVGAPDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDA 304
Cdd:cd07102 155 TPLCGER----FAAAFAEAGLPEGVFQVLHLSHETSAALIADprIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 305 FIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQ 384
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 385 NLVNDAVDKGA--EIAGRGSFghlGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLG 462
Cdd:cd07102 311 AQIADAIAKGAraLIDGALFP---EDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLT 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 463 CAVFSGNQKRAIKIASQLHCGVAAIN--DFASSYmcqsLPFGGVKDSGFGRFAGVEGLRA 520
Cdd:cd07102 388 ASVWTKDIARAEALGEQLETGTVFMNrcDYLDPA----LAWTGVKDSGRGVTLSRLGYDQ 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
71-527 |
1.70e-105 |
|
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: 325.25 E-value: 1.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASlGEIMT 150
Cdd:cd07106 4 PATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEVGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TcekITWL------------LDEGEkwlkpeyrscgrsmlHKKAKVEFYPLGVIGAIVSWNYPFhnvfnpMLA------A 212
Cdd:cd07106 83 A---VAWLrytasldlpdevIEDDD---------------TRRVELRRKPLGVVAAIVPWNFPL------LLAawkiapA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 213 IFSGNAAVIKVSEHASWSGCFYFRIIQAALaavgaPDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGRMIMNRASD 290
Cdd:cd07106 139 LLAGNTVVLKPSPFTPLCTLKLGELAQEVL-----PPGVLNVVSGGDELGPALTSHpdIRKISFTGSTATGKKVMASAAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 291 TLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYD 370
Cdd:cd07106 214 TLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 371 MGAICMIEHSEKLQNLVNDAVDKGAEIAgrgsfghLGEDAVDQ---FFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSD 447
Cdd:cd07106 294 LGPVQNKMQYDKVKELVEDAKAKGAKVL-------AGGEPLDGpgyFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 448 EEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMcqSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07106 367 DEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDP--DAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
60-534 |
1.80e-104 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 325.29 E-value: 1.80e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 60 GAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRrqfLRILLKY---ILEHQDLICEISSRDT 136
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRER---AAVLLRFhdlVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 137 GKTMVDAsLGEIMTTCEKITWLLDEGEKWLKPEYRSCGRSMLhKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSG 216
Cdd:PRK09407 105 GKARRHA-FEEVLDVALTARYYARRAPKLLAPRRRAGALPVL-TKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 217 NAAVIKVSEHASWSgcfyfriiqaALAAV------GAPDNLVHIITG-FAETGQALVSSVDKIIFVGSPGVGRMIMNRAS 289
Cdd:PRK09407 183 NAVVLKPDSQTPLT----------ALAAVellyeaGLPRDLWQVVTGpGPVVGTALVDNADYLMFTGSTATGRVLAEQAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 290 DTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRY 369
Cdd:PRK09407 253 RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 370 DMGAICMIEHSEKLQNLVNDAVDKGAEI-AG---RGSFGHLgedavdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFN 445
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVlAGgkaRPDLGPL-------FYEPTVLTGVTPDMELAREETFGPVVSVYPVA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 446 SDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIND-FASSYMCQSLPFGGVKDSGFGRFAGVEGLRACCLV 524
Cdd:PRK09407 406 DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgYAAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTES 485
|
490
....*....|
gi 1002286994 525 KAVVEDRWWP 534
Cdd:PRK09407 486 QTIATQRVLP 495
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
88-528 |
1.09e-103 |
|
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: 320.18 E-value: 1.09e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 88 VKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEImttcEKITWLL----DEGE 163
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEV----EKCAWICryyaENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 164 KWLKPEYRSCGrsmlHKKAKVEFYPLGVIGAIVSWNYPFHNVFN---PMLAAifsGNAAVIKvseHAS-WSGCFyfRIIQ 239
Cdd:cd07100 76 AFLADEPIETD----AGKAYVRYEPLGVVLGIMPWNFPFWQVFRfaaPNLMA---GNTVLLK---HASnVPGCA--LAIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 240 AALAAVGAPDNLVhiITGFAETGQalvssVDKII---------FVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCED 310
Cdd:cd07100 144 ELFREAGFPEGVF--QNLLIDSDQ-----VEAIIadprvrgvtLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 311 VDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDA 390
Cdd:cd07100 217 ADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 391 VDKGAEIagrgsfgHLGEDAVDQ---FFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFS 467
Cdd:cd07100 297 VAAGATL-------LLGGKRPDGpgaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFT 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286994 468 GNQKRAIKIASQLHCGVAAINDFASSYmcQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:cd07100 370 TDLERAERVARRLEAGMVFINGMVKSD--PRLPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
69-527 |
1.60e-98 |
|
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: 307.57 E-value: 1.60e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEI 148
Cdd:cd07093 2 FNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTTCEKITWLLD-----EGEKWLKP-EYRSCGRSMlhkkakvefyPLGVIGAIVSWNYPFhnvfnpMLA------AIFSG 216
Cdd:cd07093 82 PRAAANFRFFADyilqlDGESYPQDgGALNYVLRQ----------PVGVAGLITPWNLPL------MLLtwkiapALAFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 217 NAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGF-AETGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLI 293
Cdd:cd07093 146 NTVVLKPSEWTPLTAWLLAELANEA----GLPPGVVNVVHGFgPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 294 PVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGA 373
Cdd:cd07093 222 PVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 374 ICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKL 453
Cdd:cd07093 302 LISKEHLEKVLGYVELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIEL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 454 ANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFassyMCQSL--PFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07093 382 ANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCW----LVRDLrtPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
52-488 |
1.06e-97 |
|
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: 306.11 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 52 YIPPRKGKgaqtdKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEI 131
Cdd:cd07088 6 FVPSSSGE-----TIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 132 SSRDTGKTMVDASlGEIMTTCEKITWLLD-----EGEkwLKPEYRSCGRSMLHKKakvefyPLGVIGAIVSWNYPFHNVF 206
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEwarriEGE--IIPSDRPNENIFIFKV------PIGVVAGILPWNFPFFLIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 207 NPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITG-FAETGQALVSS--VDKIIFVGSPGVGRM 283
Cdd:cd07088 152 RKLAPALVTGNTIVIKPSEETPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHpkVGMISLTGSTEAGQK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 284 IMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGP 363
Cdd:cd07088 228 IMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 364 PLSGRYDMGAIcmIEHSE--KLQNLVNDAVDKGAEIAGRGSFGHLGEdavDQFFPPTVLVNVNHTMKIMQEEAFGPILPI 441
Cdd:cd07088 308 PFDAATDMGPL--VNEAAldKVEEMVERAVEAGATLLTGGKRPEGEK---GYFYEPTVLTNVRQDMEIVQEEIFGPVLPV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1002286994 442 MKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIN 488
Cdd:cd07088 383 VKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
69-528 |
1.13e-96 |
|
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: 302.62 E-value: 1.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWA-KSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASlGE 147
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-AD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 148 IM----------TTCEKItwlldEGEKW-LKPEYRScgrSMLHKkakvefyPLGVIGAIVSWNYPFHNVFNPMLAAIFSG 216
Cdd:cd07109 81 VEaaaryfeyygGAADKL-----HGETIpLGPGYFV---YTVRE-------PHGVTGHIIPWNYPLQITGRSVAPALAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 217 NAAVIKVSEHASWSGCfyfRIIQAALAAvGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLI 293
Cdd:cd07109 146 NAVVVKPAEDAPLTAL---RLAELAEEA-GLPAGALNVVTGLgAEAGAALVAHpgVDHISFTGSVETGIAVMRAAAENVV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 294 PVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSgRYDMGA 373
Cdd:cd07109 222 PVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 374 ICMIEHSEKLQNLVNDAVDKGAEIAGRgsfGHLGEDAVDQ--FFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVV 451
Cdd:cd07109 301 LISAKQLDRVEGFVARARARGARIVAG---GRIAEGAPAGgyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAI 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286994 452 KLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIND-FASSYMcqSLPFGGVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:cd07109 378 ALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNyGAGGGI--ELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-514 |
1.13e-95 |
|
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: 299.45 E-value: 1.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 87 EVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASlGEIMTTC----EKITWLLDEG 162
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAA-FEVGAAIailrEAAGLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 163 EKWLKPEYRscGR-SMLHKKakvefyPLGVIGAIVSWNYPFH---NVFNPMLAAifsGNAAVIKVSEHASWSGCFYF-RI 237
Cdd:cd07104 80 GEILPSDVP--GKeSMVRRV------PLGVVGVISPFNFPLIlamRSVAPALAL---GNAVVLKPDSRTPVTGGLLIaEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 238 IQAAlaavGAPDNLVHIITG-FAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLP 314
Cdd:cd07104 149 FEEA----GLPKGVLNVVPGgGSEIGDALVEHprVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 315 SVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAIcmIEHS--EKLQNLVNDAVD 392
Cdd:cd07104 225 LAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPL--INERqvDRVHAIVEDAVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 393 KGAEIAgrgsfghLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKR 472
Cdd:cd07104 303 AGARLL-------TGGTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLER 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1002286994 473 AIKIASQLHCGVAAINDfassymcQSL------PFGGVKDSGFGRFAG 514
Cdd:cd07104 376 AMAFAERLETGMVHIND-------QTVndephvPFGGVKASGGGRFGG 416
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
67-527 |
7.68e-95 |
|
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: 298.36 E-value: 7.68e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 67 QCYEPATMKYLGYFPALTPDEVKEHVAQARKA--QKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAS 144
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 145 LGEIMTTCEKITW---LLDE--GEkwLKPeyrsCGRSMLhkkAKVEFYPLGVIGAIVSWNYPFHNV---FNPMLAAifsG 216
Cdd:cd07112 85 AVDVPSAANTFRWyaeAIDKvyGE--VAP----TGPDAL---ALITREPLGVVGAVVPWNFPLLMAawkIAPALAA---G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 217 NAAVIKVSEHASWSGcfyFRIIQAALAAvGAPDNLVHIITGFAET-GQALV--SSVDKIIFVGSPGVGRMIMNRASDT-L 292
Cdd:cd07112 153 NSVVLKPAEQSPLTA---LRLAELALEA-GLPAGVLNVVPGFGHTaGEALGlhMDVDALAFTGSTEVGRRFLEYSGQSnL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 293 IPVTLELGGKDAFIVCEDV-DLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDM 371
Cdd:cd07112 229 KRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 372 GAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHlgEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVV 451
Cdd:cd07112 309 GALVSEAHFDKVLGYIESGKAEGARLVAGGKRVL--TETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAV 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 452 KLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMcqSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07112 387 ALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDI--TTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
69-527 |
8.88e-95 |
|
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: 298.06 E-value: 8.88e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMvdaslgei 148
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 mttcEKITWLLDEGEKWLkpEYRSCGRSMLHKK---------AKVEFYPLGVIGAIVSWNYPFHNVF---NPMLAAifsG 216
Cdd:cd07090 74 ----EEARVDIDSSADCL--EYYAGLAPTLSGEhvplpggsfAYTRREPLGVCAGIGAWNYPIQIASwksAPALAC---G 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 217 NAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAETGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLIP 294
Cdd:cd07090 145 NAMVYKPSPFTPLTALLLAEILTEA----GLPDGVFNVVQGGGETGQLLCEhpDVAKVSFTGSVPTGKKVMSAAAKGIKH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 295 VTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAI 374
Cdd:cd07090 221 VTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 375 CMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLgEDAVD--QFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVK 452
Cdd:cd07090 301 ISEEHLEKVLGYIESAKQEGAKVLCGGERVVP-EDGLEngFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIR 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286994 453 LANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMcqSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07090 380 RANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPV--EVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
71-528 |
2.81e-93 |
|
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: 294.15 E-value: 2.81e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKS-SFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIM 149
Cdd:cd07089 4 PATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 150 TTCEKITWLLDEGEKWLKPEYRscGRSMLHKKA---KVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEH 226
Cdd:cd07089 84 GPIGHLRYFADLADSFPWEFDL--PVPALRGGPgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 227 ASWSGCFYFRIIqaalAAVGAPDNLVHIITG-FAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKD 303
Cdd:cd07089 162 TPLSALLLGEII----AETDLPAGVVNVVTGsDNAVGEALTTDprVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 304 AFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKL 383
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 384 QNLVNDAVDKGAEIA-GRGSFGHLgedAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLG 462
Cdd:cd07089 318 EGYIARGRDEGARLVtGGGRPAGL---DKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 463 CAVFSGNQKRAIKIASQLHCGVAAINDFAssYMCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:cd07089 395 GGVWSADVDRAYRVARRIRTGSVGINGGG--GYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
69-519 |
2.04e-92 |
|
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: 291.94 E-value: 2.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDaSLGEI 148
Cdd:cd07145 4 RNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ-SRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTTCEkITWLLDEGEKWLKPEY-RSCGRSMLHKK-AKVEFYPLGVIGAIVSWNYPFhNVFNPMLA-AIFSGNAAVIKVSE 225
Cdd:cd07145 83 ERTIR-LFKLAAEEAKVLRGETiPVDAYEYNERRiAFTVREPIGVVGAITPFNFPA-NLFAHKIApAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 226 HASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAET-GQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGK 302
Cdd:cd07145 161 NTPLTAIELAKILEEA----GLPPGVINVVTGYGSEvGDEIVTNpkVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 303 DAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEK 382
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 383 LQNLVNDAVDKGAEI--AGRGSFGHlgedavdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYG 460
Cdd:cd07145 317 MENLVNDAVEKGGKIlyGGKRDEGS--------FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286994 461 LGCAVFSGNQKRAIKIASQLHCGVAAINDfASSYMCQSLPFGGVKDSGFGRfagvEGLR 519
Cdd:cd07145 389 LQASVFTNDINRALKVARELEAGGVVIND-STRFRWDNLPFGGFKKSGIGR----EGVR 442
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
59-527 |
8.19e-91 |
|
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: 288.54 E-value: 8.19e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 59 KGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKA-QKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTG 137
Cdd:cd07144 18 KSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 138 KTMVDASLGEIMTTCEKITWLLDEGEKWLkpeyrscGRSMLHKKAKVEFY---PLGVIGAIVSWNYPFHNV---FNPMLA 211
Cdd:cd07144 98 KPYHSNALGDLDEIIAVIRYYAGWADKIQ-------GKTIPTSPNKLAYTlhePYGVCGQIIPWNYPLAMAawkLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 212 AifsGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRA 288
Cdd:cd07144 171 A---GNTVVIKPAENTPLSLLYFANLVKEA----GFPPGVVNIIPGYgAVAGSALAEHpdVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 289 SDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSIS-VGPPLSG 367
Cdd:cd07144 244 AQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 368 RYDMGAICMIEHSEKLQNLVNDAVDKGAEIAgRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSD 447
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLV-YGGEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 448 EEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINdfaSSYM-CQSLPFGGVKDSGFGRFAGVEGLRACCLVKA 526
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWIN---SSNDsDVGVPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
.
gi 1002286994 527 V 527
Cdd:cd07144 480 V 480
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
59-528 |
1.08e-90 |
|
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: 287.95 E-value: 1.08e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 59 KGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKI--WAKSSFKQRRQFLRILLKYILEHQDLICEISSRDT 136
Cdd:cd07091 14 DSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 137 GKTMVDASLGEIMTT----------CEKITwlldegekwlkpeyrscGRSMLHKKAKVEFY---PLGVIGAIVSWNYP-- 201
Cdd:cd07091 94 GKPLEESAKGDVALSikclryyagwADKIQ-----------------GKTIPIDGNFLAYTrrePIGVCGQIIPWNFPll 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 202 -FHNVFNPMLAAifsGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAET-GQALVSS--VDKIIFVGS 277
Cdd:cd07091 157 mLAWKLAPALAA---GNTVVLKPAEQTPLSALYLAELIKEA----GFPPGVVNIVPGFGPTaGAAISSHmdVDKIAFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 278 PGVGRMIMNRASDT-LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKII 356
Cdd:cd07091 230 TAVGRTIMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 357 KSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEI-AGRGSFGHLGedavdQFFPPTVLVNVNHTMKIMQEEAF 435
Cdd:cd07091 310 EKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLlTGGERHGSKG-----YFIQPTVFTDVKDDMKIAKEEIF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 436 GPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSymCQSLPFGGVKDSGFGRFAGV 515
Cdd:cd07091 385 GPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVF--DAAVPFGGFKQSGFGRELGE 462
|
490
....*....|...
gi 1002286994 516 EGLRACCLVKAVV 528
Cdd:cd07091 463 EGLEEYTQVKAVT 475
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
106-520 |
2.08e-89 |
|
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: 283.22 E-value: 2.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 106 SFKQRRQFLRILLKYILEHQDLICEISSRDTG-KTMVDASLGEIMTTCEKITWLLDEGEKWLKPEYRSCGRSMLHKKAKV 184
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHVGLLFLPAKAEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 185 EFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGcfyfRIIQAALAAVGAPDnLVHIITGFAETGQA 264
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTS----ALLAELLAEYFDED-EVAVVTGGADVAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 265 lVSSV--DKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHK 342
Cdd:cd07133 173 -FSSLpfDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 343 DIYSTFVSQVVKIIKSISvgPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAgrgSFGHLGEDAVD-QFFPPTVLV 421
Cdd:cd07133 252 DKLEEFVAAAKAAVAKMY--PTLADNPDYTSIINERHYARLQGLLEDARAKGARVI---ELNPAGEDFAAtRKLPPTLVL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 422 NVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCQSLPF 501
Cdd:cd07133 327 NVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPF 406
|
410
....*....|....*....
gi 1002286994 502 GGVKDSGFGRFAGVEGLRA 520
Cdd:cd07133 407 GGVGASGMGAYHGKEGFLT 425
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
71-527 |
1.77e-88 |
|
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: 281.64 E-value: 1.77e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMT 150
Cdd:cd07115 4 PATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 T----------CEKItwlldEGEKW-LKPEYRScgrsmlhkkaKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAA 219
Cdd:cd07115 84 AadtfryyagwADKI-----EGEVIpVRGPFLN----------YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 220 VIKVSEHASWSGcfyFRIIQAAlAAVGAPDNLVHIITGFAE-TGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLIPVT 296
Cdd:cd07115 149 VLKPAELTPLSA---LRIAELM-AEAGFPAGVLNVVTGFGEvAGAALVEhpDVDKITFTGSTAVGRKIMQGAAGNLKRVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 297 LELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICM 376
Cdd:cd07115 225 LELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 377 IEHSEKlqnlVNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLAND 456
Cdd:cd07115 305 QAQFDR----VLDYVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANG 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286994 457 SKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFasSYMCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07115 381 TEYGLAAGVWTRDLGRAHRVAAALKAGTVWINTY--NRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
63-528 |
4.70e-88 |
|
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: 280.93 E-value: 4.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 63 TDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTG----- 137
Cdd:cd07138 13 TETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGapitl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 138 --KTMVDASLGEIMTTCEkitwLLDEGEkWLKPEyrscGRSMLHKKakvefyPLGVIGAIVSWNYPFHNVFNPMLAAIFS 215
Cdd:cd07138 93 arAAQVGLGIGHLRAAAD----ALKDFE-FEERR----GNSLVVRE------PIGVCGLITPWNWPLNQIVLKVAPALAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 216 GNAAVIKVSEHASWSGcfyfRIIQAALAAVGAPDNLVHIITGFAET-GQALVSS--VDKIIFVGSPGVGRMIMNRASDTL 292
Cdd:cd07138 158 GCTVVLKPSEVAPLSA----IILAEILDEAGLPAGVFNLVNGDGPVvGEALSAHpdVDMVSFTGSTRAGKRVAEAAADTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 293 IPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMG 372
Cdd:cd07138 234 KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 373 AICMIEHSEKLQNLVNDAVDKGAE-IAGrgsfghlGEDAVDQ-----FFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNS 446
Cdd:cd07138 314 PLASAAQFDRVQGYIQKGIEEGARlVAG-------GPGRPEGlergyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 447 DEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYmcqSLPFGGVKDSGFGRFAGVEGLRACCLVKA 526
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEFLEVKS 463
|
..
gi 1002286994 527 VV 528
Cdd:cd07138 464 IQ 465
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
64-518 |
1.79e-86 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 277.73 E-value: 1.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 64 DKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDA 143
Cdd:PLN02278 40 KTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 144 sLGEIMTTCEKITWLLDEGEKW---LKPEYRSCGRSMLHKKakvefyPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAV 220
Cdd:PLN02278 120 -IGEVAYGASFLEYFAEEAKRVygdIIPSPFPDRRLLVLKQ------PVGVVGAITPWNFPLAMITRKVGPALAAGCTVV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 221 IKVSEHASWSgcfyfriiqaALAA------VGAPDNLVHIITGFA-ETGQALVSS--VDKIIFVGSPGVGRMIMNRASDT 291
Cdd:PLN02278 193 VKPSELTPLT----------ALAAaelalqAGIPPGVLNVVMGDApEIGDALLASpkVRKITFTGSTAVGKKLMAGAAAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 292 LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDM 371
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 372 GAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEdavdQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVV 451
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGG----TFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAI 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286994 452 KLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSymCQSLPFGGVKDSGFGRFAGVEGL 518
Cdd:PLN02278 419 AIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLIS--TEVAPFGGVKQSGLGREGSKYGI 483
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
71-530 |
3.39e-86 |
|
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: 276.54 E-value: 3.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PA-TMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEIM 149
Cdd:cd07131 21 PAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEG-RGDVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 150 TTCEKITWLLDEGEKWLKPEYRScgrSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASW 229
Cdd:cd07131 100 EAIDMAQYAAGEGRRLFGETVPS---ELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 230 SGcfyFRIIQAaLAAVGAPDNLVHIITGFAE-TGQALV--SSVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFI 306
Cdd:cd07131 177 CA---LKLVEL-FAEAGLPPGVVNVVHGRGEeVGEALVehPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 307 VCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNL 386
Cdd:cd07131 253 VMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 387 VNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVF 466
Cdd:cd07131 333 NEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286994 467 SGNQKRAIKIASQLHCGVAAINDFASSYMCQsLPFGGVKDSGFG-RFAGVEGLRACCLVKAVVED 530
Cdd:cd07131 413 TEDVNKAFRARRDLEAGITYVNAPTIGAEVH-LPFGGVKKSGNGhREAGTTALDAFTEWKAVYVD 476
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
51-520 |
3.81e-86 |
|
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: 275.99 E-value: 3.81e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 51 IYIPPRKGKGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKA--QKIWAKSSFKQRRQFLRILLKYILEHQDLI 128
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 129 CEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKWLKPEYRscgRSMLHKKAKVEFYPLGVIGAIVSWNYPFhnvfnp 208
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERR---PGSGGGHVLVRREPVGVVAAIVPWNAPL------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 209 MLA------AIFSGNAAVIKVSEHASWSGCfyfrIIQAALAAVGAPDNLVHIITGFAETGQALVS--SVDKIIFVGSPGV 280
Cdd:cd07139 152 FLAalkiapALAAGCTVVLKPSPETPLDAY----LLAEAAEEAGLPPGVVNVVPADREVGEYLVRhpGVDKVSFTGSTAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 281 GRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSIS 360
Cdd:cd07139 228 GRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 361 VGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSfghlGEDAVDQ--FFPPTVLVNVNHTMKIMQEEAFGPI 438
Cdd:cd07139 308 VGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGG----RPAGLDRgwFVEPTLFADVDNDMRIAQEEIFGPV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 439 LPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFassYMCQSLPFGGVKDSGFGRFAGVEGL 518
Cdd:cd07139 384 LSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF---RLDFGAPFGGFKQSGIGREGGPEGL 460
|
..
gi 1002286994 519 RA 520
Cdd:cd07139 461 DA 462
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
68-519 |
4.70e-86 |
|
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: 276.11 E-value: 4.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 68 CYEPATMKYLGYFPALTPDEVKEHVAQARKA--QKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAS- 144
Cdd:cd07119 17 IINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 145 -LGEIMTTCEKITWLL--DEGEKWLKPEyrscgrsmlHKKAKVEFYPLGVIGAIVSWNYPFHNV---FNPMLAAifsGNA 218
Cdd:cd07119 97 dIDDVANCFRYYAGLAtkETGEVYDVPP---------HVISRTVREPVGVCGLITPWNYPLLQAawkLAPALAA---GNT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 219 AVIKVSEHASWSGCFYFRIIqaalAAVGAPDNLVHIITGFAET-GQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPV 295
Cdd:cd07119 165 VVIKPSEVTPLTTIALFELI----EEAGLPAGVVNLVTGSGATvGAELAESpdVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 296 TLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAIC 375
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 376 MIEHSEKLQNLVNDAVDKGAEIAGRGSfgHLGEDAVDQ--FFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKL 453
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGK--RPTGDELAKgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 454 ANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFaSSYMCQSlPFGGVKDSGFGRFAGVEGLR 519
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDY-HPYFAEA-PWGGYKQSGIGRELGPTGLE 462
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
92-518 |
5.15e-86 |
|
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: 274.45 E-value: 5.15e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 92 VAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTM------VDASLGEIMTTCEKITWLLDEgekw 165
Cdd:cd07105 6 VEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAawagfnVDLAAGMLREAASLITQIIGG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 166 LKPEYRSCGRSMLHKKakvefyPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASwsGCFYFrIIQAALAAv 245
Cdd:cd07105 82 SIPSDKPGTLAMVVKE------PVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSP--RTHWL-IGRVFHEA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 246 GAPDNLVHIITGFAETG----QALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQV 319
Cdd:cd07105 152 GLPKGVLNVVTHSPEDApevvEALIAHpaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 320 AVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPlsgryDMGAICMIEHSEKLQNLVNDAVDKGAEIAg 399
Cdd:cd07105 232 ALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPV-----VLGSLVSAAAADRVKELVDDALSKGAKLV- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 400 rgsFGHLGEDAVD-QFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIAS 478
Cdd:cd07105 306 ---VGGLADESPSgTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAK 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1002286994 479 QLHCGVAAIN-----DFAssymcqSLPFGGVKDSGFGRFAGVEGL 518
Cdd:cd07105 383 RIESGAVHINgmtvhDEP------TLPHGGVKSSGYGRFNGKWGI 421
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
69-532 |
2.57e-85 |
|
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: 273.05 E-value: 2.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEI 148
Cdd:cd07150 4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-WFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTT----------CEKITwlldeGEKwLKPEYRscGR-SMLHKKakvefyPLGVIGAIVSWNYPFHNVFNPMLAAIFSGN 217
Cdd:cd07150 83 TFTpellraaageCRRVR-----GET-LPSDSP--GTvSMSVRR------PLGVVAGITPFNYPLILATKKVAFALAAGN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 218 AAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITG-FAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIP 294
Cdd:cd07150 149 TVVLKPSEETPVIGLKIAEIMEEA----GLPKGVFNVVTGgGAEVGDELVDDprVRMVTFTGSTAVGREIAEKAGRHLKK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 295 VTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAI 374
Cdd:cd07150 225 ITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 375 CMIEHSEKLQNLVNDAVDKGAEIAGRGsfGHLGedavdQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLA 454
Cdd:cd07150 305 ISPRQVERIKRQVEDAVAKGAKLLTGG--KYDG-----NFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELA 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286994 455 NDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDfaSSYMCQS-LPFGGVKDSGFGRFAGVEGLRacclvkAVVEDRW 532
Cdd:cd07150 378 NDTEYGLSAAILTNDLQRAFKLAERLESGMVHIND--PTILDEAhVPFGGVKASGFGREGGEWSME------EFTELKW 448
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
93-520 |
3.16e-85 |
|
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: 272.18 E-value: 3.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 93 AQARKAQKiWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKWLKPEYRS 172
Cdd:cd07134 6 AQQAHALA-LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 173 CGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSE---HASwsgcfyfRIIQAALAAVGAPD 249
Cdd:cd07134 85 TPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSEltpHTS-------AVIAKIIREAFDED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 250 nLVHIITGFAETGQALVS-SVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSS 328
Cdd:cd07134 158 -EVAVFEGDAEVAQALLElPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 329 GQNCAGAERFYVHKDIYSTFVSQVVK-IIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFghlg 407
Cdd:cd07134 237 GQTCIAPDYVFVHESVKDAFVEHLKAeIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQF---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 408 eDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAI 487
Cdd:cd07134 313 -DAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVV 391
|
410 420 430
....*....|....*....|....*....|...
gi 1002286994 488 NDFASSYMCQSLPFGGVKDSGFGRFAGVEGLRA 520
Cdd:cd07134 392 NDVVLHFLNPNLPFGGVNNSGIGSYHGVYGFKA 424
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
71-527 |
7.55e-85 |
|
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: 272.33 E-value: 7.55e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVdASLGEIMT 150
Cdd:cd07107 4 PATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AMLGDVMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TCEKITWLLDEGEKwLKPEYRSCGRSMLHKKAKvefYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWS 230
Cdd:cd07107 83 AAALLDYFAGLVTE-LKGETIPVGGRNLHYTLR---EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 231 GCFYFRIIQAALaavgaPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIV 307
Cdd:cd07107 159 ALRLAELAREVL-----PPGVFNILPGDgATAGAALVRHpdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 308 CEDVDLPSVVQVAVRAA-LQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNL 386
Cdd:cd07107 234 FPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 387 VNDAVDKGAEI--AGRGSFGHLGEDAVdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCA 464
Cdd:cd07107 314 IDSAKREGARLvtGGGRPEGPALEGGF--YVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286994 465 VFSGNQKRAIKIASQLHCGVAAINDFASSYMcqSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
59-528 |
1.21e-84 |
|
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: 272.14 E-value: 1.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 59 KGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAK-SSFKQRRQFLRILLKYILEHQDLICEISSRDTG 137
Cdd:cd07082 11 KESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANLLMWEIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 138 KTMVDAsLGEIMTTCEKITWLLDEGEKwLKPEYrSCGRSMLH---KKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIF 214
Cdd:cd07082 91 KTLKDA-LKEVDRTIDYIRDTIEELKR-LDGDS-LPGDWFPGtkgKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 215 SGNAAVIKVSEHASWSGCFYFRiiqaALAAVGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASdt 291
Cdd:cd07082 168 MGNTVVFKPATQGVLLGIPLAE----AFHDAGFPKGVVNVVTGRgREIGDPLVTHgrIDVISFTGSTEVGNRLKKQHP-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 292 LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDM 371
Cdd:cd07082 242 MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 372 GAicMIEHS--EKLQNLVNDAVDKGAEI--AGRGsfghlgedAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSD 447
Cdd:cd07082 322 TP--LIDPKsaDFVEGLIDDAVAKGATVlnGGGR--------EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 448 EEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDfassyMCQ----SLPFGGVKDSGFGRFAGVEGLRACCL 523
Cdd:cd07082 392 EEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-----KCQrgpdHFPFLGRKDSGIGTQGIGDALRSMTR 466
|
....*
gi 1002286994 524 VKAVV 528
Cdd:cd07082 467 RKGIV 471
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
69-519 |
1.31e-84 |
|
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: 271.39 E-value: 1.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEI 148
Cdd:cd07149 4 ISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA-RKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTTCEKITWLLDEGEkwlkpeyRSCGR-----SMLHKKAKVEFY---PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAV 220
Cdd:cd07149 83 DRAIETLRLSAEEAK-------RLAGEtipfdASPGGEGRIGFTirePIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 221 IKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAET-GQALVSS--VDKIIFVGSPGVGRMIMNRASdtLIPVTL 297
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEA----GLPKGALNVVTGSGETvGDALVTDprVRMISFTGSPAVGEAIARKAG--LKKVTL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 298 ELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMI 377
Cdd:cd07149 230 ELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 378 EHSEKLQNLVNDAVDKGAEIAgrgsfghLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDS 457
Cdd:cd07149 310 AEAERIEEWVEEAVEGGARLL-------TGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDS 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002286994 458 KYGLGCAVFSGNQKRAIKIASQLHCGVAAINDfASSYMCQSLPFGGVKDSGFGRfagvEGLR 519
Cdd:cd07149 383 PYGLQAGVFTNDLQKALKAARELEVGGVMIND-SSTFRVDHMPYGGVKESGTGR----EGPR 439
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
70-518 |
3.50e-84 |
|
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: 270.39 E-value: 3.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 70 EPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIM 149
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 150 TTCEKITW---LLDEgekwLKPEYRSCGRSMLHKKAKVefyPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEH 226
Cdd:cd07108 83 VLADLFRYfggLAGE----LKGETLPFGPDVLTYTVRE---PLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 227 ASWSGCFYFRIIQAALaavgaPDNLVHIITGF-AETGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKD 303
Cdd:cd07108 156 APLAVLLLAEILAQVL-----PAGVLNVITGYgEECGAALVDhpDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 304 AFIVCEDVDLPSVVQVAV---RAALQssGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICmiehS 380
Cdd:cd07108 231 PMIVFPDADLDDAVDGAIagmRFTRQ--GQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAII----S 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 381 EKLQNLVNDAVDKGAEIAG----RGSF----GHLGEDAvdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVK 452
Cdd:cd07108 305 EKQFAKVCGYIDLGLSTSGatvlRGGPlpgeGPLADGF---FVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 453 LANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCQSlpFGGVKDSGFGRFAGVEGL 518
Cdd:cd07108 382 MANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQS--YGGFKQSGLGREASLEGM 445
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
59-511 |
2.97e-82 |
|
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: 265.86 E-value: 2.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 59 KGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGK 138
Cdd:cd07117 11 KGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 139 TMVDASLGEIMTTCEKITW-----LLDEGEKwlkpeyrscgrSMLHKK--AKVEFYPLGVIGAIVSWNYPFHNVFNPMLA 211
Cdd:cd07117 91 PIRETRAVDIPLAADHFRYfagviRAEEGSA-----------NMIDEDtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 212 AIFSGNAAVIKVSEHASWSGCFYFRIIQAALaavgaPDNLVHIITGF-AETGQALVS--SVDKIIFVGSPGVGRMIMNRA 288
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVL-----PKGVVNIVTGKgSKSGEYLLNhpGLDKLAFTGSTEVGRDVAIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 289 SDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGR 368
Cdd:cd07117 235 AKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 369 YDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGsfGHLGEDAVDQ--FFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNS 446
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGG--HRLTENGLDKgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286994 447 DEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFasSYMCQSLPFGGVKDSGFGR 511
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTY--NQIPAGAPFGGYKKSGIGR 455
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
106-529 |
2.03e-81 |
|
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: 262.08 E-value: 2.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 106 SFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKWLKPeyRSCGRSMLHK--KAK 183
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP--RRVSVPLLLQpaKAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 184 VEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALaavgaPDNLVHIITGFAETGQ 263
Cdd:cd07087 96 VIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYF-----DPEAVAVVEGGVEVAT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 264 ALVS-SVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHK 342
Cdd:cd07087 171 ALLAePFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 343 DIYSTFVSQVVKIIKSIsVGPPLSGRYDMGAICMIEHSEKLQNLVNDAvdkgaEIAGRGSFghlgeDAVDQFFPPTVLVN 422
Cdd:cd07087 251 SIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGGQV-----DKEERYIAPTILDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 423 VNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCQSLPFG 502
Cdd:cd07087 320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFG 399
|
410 420
....*....|....*....|....*..
gi 1002286994 503 GVKDSGFGRFAGVEGLRACCLVKAVVE 529
Cdd:cd07087 400 GVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
84-514 |
5.47e-81 |
|
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: 261.46 E-value: 5.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 84 TPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDA--SLGEIMTTCEKITWLLDE 161
Cdd:cd07152 11 DAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAgfEVGAAIGELHEAAGLPTQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 162 GEKWLKPEyrSCGRSMLHKKAkvefyPLGVIGAIVSWNYPFH---NVFNPMLAAifsGNAAVIKVSEHASWSGCFyfrII 238
Cdd:cd07152 91 PQGEILPS--APGRLSLARRV-----PLGVVGVISPFNFPLIlamRSVAPALAL---GNAVVLKPDPRTPVSGGV---VI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 239 QAALAAVGAPDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSV 316
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDpnVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 317 VQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAE 396
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 397 IAGRGSFGHLgedavdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKI 476
Cdd:cd07152 318 LEAGGTYDGL-------FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430
....*....|....*....|....*....|....*....
gi 1002286994 477 ASQLHCGVAAINDFASSYMCQSlPFGGVKDSGFG-RFAG 514
Cdd:cd07152 391 ADRLRTGMLHINDQTVNDEPHN-PFGGMGASGNGsRFGG 428
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
71-533 |
9.51e-81 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 262.75 E-value: 9.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKA-----QKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTmVDASL 145
Cdd:PLN02467 30 PATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKP-LDEAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 146 GEI--MTTCekITWLLDEGEKWLKPEYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNV---FNPMLAAifsGNAAV 220
Cdd:PLN02467 109 WDMddVAGC--FEYYADLAEALDAKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMAtwkVAPALAA---GCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 221 IKVSEHASWSgCFYFriiqAALAA-VGAPDNLVHIITGF-AETGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLIPVT 296
Cdd:PLN02467 184 LKPSELASVT-CLEL----ADICReVGLPPGVLNVVTGLgTEAGAPLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPVS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 297 LELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICM 376
Cdd:PLN02467 259 LELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 377 IEHSEKLQNLVNDAVDKGAEI-AGRGSFGHLGEDAvdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLAN 455
Cdd:PLN02467 339 EGQYEKVLKFISTAKSEGATIlCGGKRPEHLKKGF---FIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELAN 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 456 DSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINdFASSYMCQsLPFGGVKDSGFGRFAGVEGLRACCLVKAVV----EDR 531
Cdd:PLN02467 416 DSHYGLAGAVISNDLERCERVSEAFQAGIVWIN-CSQPCFCQ-APWGGIKRSGFGRELGEWGLENYLSVKQVTkyisDEP 493
|
...
gi 1002286994 532 W-W 533
Cdd:PLN02467 494 WgW 496
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
48-511 |
1.04e-80 |
|
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: 261.89 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 48 DSYI---YIPPRKGkgaqtDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEH 124
Cdd:cd07559 2 DNFIngeWVAPSKG-----EYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 125 QDLICEISSRDTGKTMVDASLGEIMTTCEKITW-----LLDEGekwlkpeyrscGRSMLHKKA-KVEFY-PLGVIGAIVS 197
Cdd:cd07559 77 LELLAVAETLDNGKPIRETLAADIPLAIDHFRYfagviRAQEG-----------SLSEIDEDTlSYHFHePLGVVGQIIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 198 WNYPFHNV---FNPMLAAifsGNAAVIKVSEHASWSGCFYFRIIQAALaavgaPDNLVHIITGF-AETGQALVSS--VDK 271
Cdd:cd07559 146 WNFPLLMAawkLAPALAA---GNTVVLKPASQTPLSILVLMELIGDLL-----PKGVVNVVTGFgSEAGKPLASHprIAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 272 IIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPS------VVQVAVRAALqSSGQNCAGAERFYVHKDIY 345
Cdd:cd07559 218 LAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDADddfddkAEEGQLGFAF-NQGEVCTCPSRALVQESIY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 346 STFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVLVNVNH 425
Cdd:cd07559 297 DEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 426 TMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINdfassymCQSL-----P 500
Cdd:cd07559 377 DMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN-------CYHQypahaP 449
|
490
....*....|.
gi 1002286994 501 FGGVKDSGFGR 511
Cdd:cd07559 450 FGGYKKSGIGR 460
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
71-529 |
1.82e-80 |
|
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: 260.75 E-value: 1.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAS--LGEI 148
Cdd:cd07110 4 PATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdVDDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTTCEkitWLLDEGEKWLKPEYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNV---FNPMLAAifsGNAAVIKVSE 225
Cdd:cd07110 84 AGCFE---YYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAawkVAPALAA---GCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 226 HASWSGCFYFRIIqaalAAVGAPDNLVHIITGFA-ETGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGK 302
Cdd:cd07110 158 LTSLTELELAEIA----AEAGLPPGVLNVVTGTGdEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 303 DAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEK 382
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 383 LQNLVNDAVDKGAE-IAGRGSFGHLGEdavDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGL 461
Cdd:cd07110 314 VLSFIARGKEEGARlLCGGRRPAHLEK---GYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286994 462 GCAVFSGNQKRAIKIASQLHCGVAAINdfASS-YMCQsLPFGGVKDSGFGRFAGVEGLRACCLVKAVVE 529
Cdd:cd07110 391 AAAVISRDAERCDRVAEALEAGIVWIN--CSQpCFPQ-APWGGYKRSGIGRELGEWGLDNYLEVKQITR 456
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
69-527 |
5.18e-80 |
|
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: 259.18 E-value: 5.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEI 148
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTTCEKITWLLD-----EGEkwLKPEYRSCGRSMLHKKakvefyPLGVIGAIVSWNYPFHNV---FNPMLAAifsGNAAV 220
Cdd:cd07092 82 PGAVDNFRFFAGaartlEGP--AAGEYLPGHTSMIRRE------PIGVVAQIAPWNYPLMMAawkIAPALAA---GNTVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 221 IKVSEHASWSGcfyfrIIQAALAAVGAPDNLVHIITGFAE-TGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLIPVTL 297
Cdd:cd07092 151 LKPSETTPLTT-----LLLAELAAEVLPPGVVNVVCGGGAsAGDALVAhpRVRMVSLTGSVRTGKKVARAAADTLKRVHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 298 ELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMI 377
Cdd:cd07092 226 ELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 378 EHSEKLQNLVnDAVDKGAEIAGRGSFGhlgeDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDS 457
Cdd:cd07092 306 AQRERVAGFV-ERAPAHARVLTGGRRA----EGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDV 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286994 458 KYGLGCAVFSGNQKRAIKIASQLHCGVAAIND---FASsymcqSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07092 381 EYGLASSVWTRDVGRAMRLSARLDFGTVWVNThipLAA-----EMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
60-520 |
9.85e-79 |
|
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: 256.72 E-value: 9.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 60 GAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKT 139
Cdd:cd07086 9 GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 140 MVDAsLGEI---MTTCEKITWLldegekwlkpeyrscGRsMLH---------KKAKVEFY-PLGVIGAIVSWNYPFhNVF 206
Cdd:cd07086 89 LPEG-LGEVqemIDICDYAVGL---------------SR-MLYgltipserpGHRLMEQWnPLGVVGVITAFNFPV-AVP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 207 --NPMLAAIfSGNAAVIKVSEHASWSGCFYFRIIQAALAAVGAPDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGR 282
Cdd:cd07086 151 gwNAAIALV-CGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDprVPLVSFTGSTEVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 283 MIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVG 362
Cdd:cd07086 230 RVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 363 PPLSGRYDMGAIcmieHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDAVDQ--FFPPTVLVNVNHTMKIMQEEAFGPILP 440
Cdd:cd07086 310 DPLDEGTLVGPL----INQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPgnYVEPTIVTGVTDDARIVQEETFAPILY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 441 IMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKI--ASQLHCGVAAINDFASSYMCQsLPFGGVKDSGFGRFAGVEGL 518
Cdd:cd07086 386 VIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEIG-GAFGGEKETGGGRESGSDAW 464
|
..
gi 1002286994 519 RA 520
Cdd:cd07086 465 KQ 466
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
56-514 |
1.06e-78 |
|
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: 256.46 E-value: 1.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 56 RKGKGAQTDKVqcYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRD 135
Cdd:cd07151 4 RDGTSERTIDV--LNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 136 TGKTMVDASLgEIMTTCEkitwLLDEGEKW-LKPEYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIF 214
Cdd:cd07151 82 SGSTRIKANI-EWGAAMA----ITREAATFpLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 215 SGNAAVIKVSEHASWSGCFYF-RIIQAAlaavGAPDNLVHIITG-FAETGQALVSS-VDKII-FVGSPGVGRMIMNRASD 290
Cdd:cd07151 157 LGNAVVLKPASDTPITGGLLLaKIFEEA----GLPKGVLNVVVGaGSEIGDAFVEHpVPRLIsFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 291 TLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYD 370
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 371 MGAIcmIEHS--EKLQNLVNDAVDKGAEIagrgsfgHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDE 448
Cdd:cd07151 313 VGPL--INESqvDGLLDKIEQAVEEGATL-------LVGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEE 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002286994 449 EVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDfassymcQS------LPFGGVKDSGFGRFAG 514
Cdd:cd07151 384 EALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIND-------QPvndephVPFGGEKNSGLGRFNG 448
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
71-518 |
1.98e-77 |
|
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: 252.64 E-value: 1.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKA--QKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTmVDASLGEI 148
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKP-ISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTTCEkitwLLD---------EGEKwlkpeYRSCGRSMLhkkAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAA 219
Cdd:cd07118 83 EGAAD----LWRyaaslartlHGDS-----YNNLGDDML---GLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 220 VIKVSEHASWSGcfyFRIIQAALAAvGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVT 296
Cdd:cd07118 151 VVKPSEFTSGTT---LMLAELLIEA-GLPAGVVNIVTGYgATVGQAMTEHpdVDMVSFTGSTRVGKAIAAAAARNLKKVS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 297 LELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICM 376
Cdd:cd07118 227 LELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIIN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 377 IEHSEKLQNLVNDAVDKGAEIAgrgsfghLGEDAVD----QFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVK 452
Cdd:cd07118 307 EAQLAKITDYVDAGRAEGATLL-------LGGERLAsaagLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 453 LANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYmcQSLPFGGVKDSGFGRFAGVEGL 518
Cdd:cd07118 380 LANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGS--PELPFGGFKQSGIGRELGRYGV 443
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
92-528 |
1.17e-76 |
|
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: 251.50 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 92 VAQARKAQKI---WAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKWlkp 168
Cdd:cd07141 50 VKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKI--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 169 eyrsCGRSMlhkKAKVEFY------PLGVIGAIVSWNYPFHnvfnpMLA-----AIFSGNAAVIKVSEHASWSGCFYFRI 237
Cdd:cd07141 127 ----HGKTI---PMDGDFFtytrhePVGVCGQIIPWNFPLL-----MAAwklapALACGNTVVLKPAEQTPLTALYLASL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 238 IQAAlaavGAPDNLVHIITGFAET-GQALVS--SVDKIIFVGSPGVGRMIMNRASDT-LIPVTLELGGKDAFIVCEDVDL 313
Cdd:cd07141 195 IKEA----GFPPGVVNVVPGYGPTaGAAISShpDIDKVAFTGSTEVGKLIQQAAGKSnLKRVTLELGGKSPNIVFADADL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 314 PSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDK 393
Cdd:cd07141 271 DYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 394 GAEI-AGRGSFGHLGedavdQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKR 472
Cdd:cd07141 351 GAKLeCGGKRHGDKG-----YFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDK 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 473 AIKIASQLHCGVAAINDFaSSYMCQSlPFGGVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:cd07141 426 AITFSNALRAGTVWVNCY-NVVSPQA-PFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
51-527 |
8.26e-75 |
|
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: 246.67 E-value: 8.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 51 IYIPPRKGKGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKA-QKIWAKS-SFKQRRQFLRILLKYILEHQDLI 128
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 129 CEISSRDTGKTMVDASLGEIMTTCEKITWLldegEKWLKPEYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNP 208
Cdd:cd07143 89 ASIEALDNGKTFGTAKRVDVQASADTFRYY----GGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 209 MLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAET-GQALVS--SVDKIIFVGSPGVGRMIM 285
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVVSGYGRTcGNAISShmDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 286 NRASDT-LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPP 364
Cdd:cd07143 241 EAAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 365 LSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIA-GRGSFGHLGedavdQFFPPTVLVNVNHTMKIMQEEAFGPILPIMK 443
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGKAEGATVEtGGKRHGNEG-----YFIEPTIFTDVTEDMKIVKEEIFGPVVAVIK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 444 FNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFasSYMCQSLPFGGVKDSGFGRFAGVEGLRACCL 523
Cdd:cd07143 396 FKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCY--NLLHHQVPFGGYKQSGIGRELGEYALENYTQ 473
|
....
gi 1002286994 524 VKAV 527
Cdd:cd07143 474 IKAV 477
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
80-528 |
1.22e-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: 245.87 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 80 FPALTP--DEVKEHVAQ------------ARKA--QKIWAKSSFKQRRqflRILLKY---ILEHQDLICEISSRDTGKTM 140
Cdd:cd07142 21 FPTIDPrnGEVIAHVAEgdaedvdravkaARKAfdEGPWPRMTGYERS---RILLRFadlLEKHADELAALETWDNGKPY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 141 VDASLGEIMTTCEKITWLLDEGEKWLKPEYRSCGRSM---LHKkakvefyPLGVIGAIVSWNYPFHNVFNPMLAAIFSGN 217
Cdd:cd07142 98 EQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHvytLHE-------PIGVVGQIIPWNFPLLMFAWKVGPALACGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 218 AAVIKVSEHASWSGCFYfriiqAALAA-VGAPDNLVHIITGFAETGQALVSS---VDKIIFVGSPGVGRMIMNRASDT-L 292
Cdd:cd07142 171 TIVLKPAEQTPLSALLA-----AKLAAeAGLPDGVLNIVTGFGPTAGAAIAShmdVDKVAFTGSTEVGKIIMQLAAKSnL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 293 IPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMG 372
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 373 AICMIEHSEKLQNLVNDAVDKGAE-IAGRGSFGHLGedavdQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVV 451
Cdd:cd07142 326 PQVDKEQFEKILSYIEHGKEEGATlITGGDRIGSKG-----YYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286994 452 KLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFasSYMCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCY--DVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
71-519 |
2.30e-74 |
|
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: 244.65 E-value: 2.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEIMT 150
Cdd:cd07094 6 PYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TCEKITWLLDEGEKW------LKPEYRSCGRSMLHKKakvefYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVS 224
Cdd:cd07094 85 AIDTLRLAAEEAERIrgeeipLDATQGSDNRLAWTIR-----EPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 225 EHASWSGCFYFRIIQAAlaavGAPDNLVHIITG-FAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIpvTLELGG 301
Cdd:cd07094 160 SKTPLSALELAKILVEA----GVPEGVLQVVTGeREVLGDAFAADerVAMLSFTGSAAVGEALRANAGGKRI--ALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 302 KDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSE 381
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 382 KLQNLVNDAVDKGAEIAGRGSFghlgEDAVdqfFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGL 461
Cdd:cd07094 314 RVERWVEEAVEAGARLLCGGER----DGAL---FKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286994 462 GCAVFSGNQKRAIKIASQLHCGVAAINDfASSYMCQSLPFGGVKDSGFGRfagvEGLR 519
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVND-SSAFRTDWMPFGGVKESGVGR----EGVP 439
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
71-528 |
1.19e-73 |
|
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: 242.65 E-value: 1.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARkaqkiwAKSSFKQRRQFLRILLK---YILEHQDLICEISSRDTGKTMVDAsLGE 147
Cdd:cd07146 6 PYTGEVVGTVPAGTEEALREALALAA------SYRSTLTRYQRSAILNKaaaLLEARREEFARLITLESGLCLKDT-RYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 148 IMTTCEKITW-----LLDEGEKWLKPEYRSCGRsmlhKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIK 222
Cdd:cd07146 79 VGRAADVLRFaaaeaLRDDGESFSCDLTANGKA----RKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 223 VSEHASWSgCFYFRIIqaaLAAVGAPDNLVHIITG-FAETGQALVSS--VDKIIFVGSPGVGRMIMNRASdtLIPVTLEL 299
Cdd:cd07146 155 PSEKTPLS-AIYLADL---LYEAGLPPDMLSVVTGePGEIGDELITHpdVDLVTFTGGVAVGKAIAATAG--YKRQLLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 300 GGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEH 379
Cdd:cd07146 229 GGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 380 SEKLQNLVNDAVDKGAEIAgrgsFGHLGEDAvdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKY 459
Cdd:cd07146 309 AIQIENRVEEAIAQGARVL----LGNQRQGA---LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAY 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 460 GLGCAVFSGNQKRAIKIASQLHCGVAAINDfASSYMCQSLPFGGVKDSGFGRFAGV-EGLRACCLVKAVV 528
Cdd:cd07146 382 GLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFRSELSPFGGVKDSGLGGKEGVrEAMKEMTNVKTYS 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
69-527 |
1.28e-72 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 240.58 E-value: 1.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEI 148
Cdd:PRK13473 22 YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 149 MTTCEKITWL-----LDEGEkwLKPEYRSCGRSMLHKKakvefyPLGVIGAIVSWNYPFhnvfnpMLA------AIFSGN 217
Cdd:PRK13473 102 PAIVDVFRFFagaarCLEGK--AAGEYLEGHTSMIRRD------PVGVVASIAPWNYPL------MMAawklapALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 218 AAVIKVSEHASWSgCFYFriiqAALAAVGAPDNLVHIITGF-AETGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLIP 294
Cdd:PRK13473 168 TVVLKPSEITPLT-ALKL----AELAADILPPGVLNVVTGRgATVGDALVGhpKVRMVSLTGSIATGKHVLSAAADSVKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 295 VTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAI 374
Cdd:PRK13473 243 THLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 375 CMIEHSEKLQNLVNDA-------VDKGAEIAGRGSFghlgedavdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSD 447
Cdd:PRK13473 323 ISAAHRDRVAGFVERAkalghirVVTGGEAPDGKGY----------YYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 448 EEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDfasSYMCQS-LPFGGVKDSGFGRFAGVEGLRACCLVKA 526
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMLVSeMPHGGQKQSGYGKDMSLYGLEDYTVVRH 469
|
.
gi 1002286994 527 V 527
Cdd:PRK13473 470 V 470
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
71-527 |
2.29e-72 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 240.17 E-value: 2.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRqflRILLKY--IL-EHQDLICEISSRDTGKTMVDASLGE 147
Cdd:PRK13252 29 PATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERS---RILRRAvdILrERNDELAALETLDTGKPIQETSVVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 148 IMTTCEKITWLLD-----EGEKW-LKPEyrscgrsmlhkkakvEFY-----PLGVIGAIVSWNYPFHNVF---NPMLAAi 213
Cdd:PRK13252 106 IVTGADVLEYYAGlapalEGEQIpLRGG---------------SFVytrrePLGVCAGIGAWNYPIQIACwksAPALAA- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 214 fsGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDT 291
Cdd:PRK13252 170 --GNAMIFKPSEVTPLTALKLAEIYTEA----GLPDGVFNVVQGDGRVGAWLTEHpdIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 292 LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDM 371
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 372 GAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVV 451
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 452 KLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMcqSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPA--EMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
97-514 |
3.82e-72 |
|
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: 238.56 E-value: 3.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 97 KAQKIWAKS----SFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKWLKPEYRS 172
Cdd:cd07136 5 EKQRAFFKTgatkDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRVK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 173 CGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALaavgaPDNLV 252
Cdd:cd07136 85 TPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETF-----DEEYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 253 HIITGFAETGQALVSS-VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLpsvvQVAVR----AALQS 327
Cdd:cd07136 160 AVVEGGVEENQELLDQkFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANL----KLAAKrivwGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 328 SGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRyDMGAICMIEHSEKLQNLvndaVDKGAEIAGRGSfghlg 407
Cdd:cd07136 236 AGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGL----LDNGKIVFGGNT----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 408 eDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAI 487
Cdd:cd07136 306 -DRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCI 384
|
410 420 430
....*....|....*....|....*....|.
gi 1002286994 488 ND----FASSYMcqslPFGGVKDSGFGRFAG 514
Cdd:cd07136 385 NDtimhLANPYL----PFGGVGNSGMGSYHG 411
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
59-518 |
6.01e-72 |
|
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: 238.83 E-value: 6.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 59 KGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGK 138
Cdd:cd07111 32 KPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 139 TMVDASLGEIMTTCEKItwlldegekwlkpeYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHnvfnpMLA-----AI 213
Cdd:cd07111 112 PIRESRDCDIPLVARHF--------------YHHAGWAQLLDTELAGWKPVGVVGQIVPWNFPLL-----MLAwkicpAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 214 FSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAETGQALVS--SVDKIIFVGSPGVGRMIMNRASDT 291
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEA----GLPPGVLNIVTGNGSFGSALANhpGVDKVAFTGSTEVGRALRRATAGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 292 LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDM 371
Cdd:cd07111 249 GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 372 GAICMIEHSEKLQNLVNDAVDKGAEIAGRG----SFGHlgedavdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSD 447
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGadlpSKGP--------FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286994 448 EEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIN-----DFASsymcqslPFGGVKDSGFGRFAGVEGL 518
Cdd:cd07111 401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlfDAAA-------GFGGYRESGFGREGGKEGL 469
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
69-518 |
9.24e-72 |
|
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: 237.63 E-value: 9.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 69 YEPATMKYLGYFPALTPDEVKEHVAQARKAQK--IWAKSSfKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASlG 146
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEAR-F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 147 EIMTTCEKITWlldegekWLKPEYRSCGR---------SMLHKKakvefyPLGVIGAIVSWNYP---FHNVFNPMLAAif 214
Cdd:cd07120 80 EISGAISELRY-------YAGLARTEAGRmiepepgsfSLVLRE------PMGVAGIIVPWNSPvvlLVRSLAPALAA-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 215 sGNAAVIKVsehASWSGCFYFRIIQAALAAVGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASDT 291
Cdd:cd07120 145 -GCTVVVKP---AGQTAQINAAIIRILAEIPSLPAGVVNLFTESgSEGAAHLVASpdVDVISFTGSTATGRAIMAAAAPT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 292 LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDM 371
Cdd:cd07120 221 LKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDM 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 372 GAICMIEHSEKLQNLVNDAVDKGAEIAGRGsfGHLGED-AVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEV 450
Cdd:cd07120 301 GPLIDRANVDRVDRMVERAIAAGAEVVLRG--GPVTEGlAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEA 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286994 451 VKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYmcQSLPFGGVKDSGFGRFAGVEGL 518
Cdd:cd07120 379 VALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLF--AEAEEGGYRQSGLGRLHGVAAL 444
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
84-520 |
1.58e-70 |
|
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: 234.04 E-value: 1.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 84 TPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGE 163
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 164 KWLKPEYRSCG--RSMLHKkAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAA 241
Cdd:cd07135 83 KWAKDEKVKDGplAFMFGK-PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 242 LaavgaPDNLVHIITG-FAETGQALVSSVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVA 320
Cdd:cd07135 162 L-----DPDAFQVVQGgVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 321 VRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRyDMGAICMIEHSEKLQNLVNDAvdkgaeiAGR 400
Cdd:cd07135 237 LWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDTT-------KGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 401 GSFGHLGEDAvDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQL 480
Cdd:cd07135 309 VVIGGEMDEA-TRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRT 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1002286994 481 HCGVAAINDFASSYMCQSLPFGGVKDSGFGRFAGVEGLRA 520
Cdd:cd07135 388 RSGGVVINDTLIHVGVDNAPFGGVGDSGYGAYHGKYGFDT 427
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
52-527 |
2.74e-69 |
|
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: 231.95 E-value: 2.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 52 YIPPRKGKGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKA-QKIWAKSSFKQRRqflRILLKY---ILEHQDL 127
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERG---RILLRLadlIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 128 ICEISSRDTGKTM-------VDASL--------------GEIMTtcekITWLLDEGEKWLKPEYRScgrsmlhkkakvef 186
Cdd:cd07113 80 LAQLETLCSGKSIhlsrafeVGQSAnflryfagwatkinGETLA----PSIPSMQGERYTAFTRRE-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 187 yPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSgcfYFRIIQAALAAvGAPDNLVHIITGFAETGQALV 266
Cdd:cd07113 142 -PVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLT---LLRVAELAKEA-GIPDGVLNVVNGKGAVGAQLI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 267 SS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDI 344
Cdd:cd07113 217 SHpdVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 345 YSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAgrgsfghLGEDAVDQ---FFPPTVLV 421
Cdd:cd07113 297 FDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIV-------RGGEALAGegyFVQPTLVL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 422 NVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINdfASSYMCQSLPF 501
Cdd:cd07113 370 ARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN--MHTFLDPAVPF 447
|
490 500
....*....|....*....|....*.
gi 1002286994 502 GGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:cd07113 448 GGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
106-538 |
1.04e-68 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 230.69 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 106 SFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKWLKPEYRSCGRSMLHKKAKVE 185
Cdd:PTZ00381 27 PLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVFGPGKSYII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 186 FYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALaavgaPDNLVHIITGFAETGQAL 265
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYL-----DPSYVRVIEGGVEVTTEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 266 VSS-VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDI 344
Cdd:PTZ00381 182 LKEpFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 345 YSTFVSQV-VKIIKSISVGPPLSGryDMGAICMIEHSEKLQNLVNDavDKGAEIAGrgsfghlGE-DAVDQFFPPTVLVN 422
Cdd:PTZ00381 262 KDKFIEALkEAIKEFFGEDPKKSE--DYSRIVNEFHTKRLAELIKD--HGGKVVYG-------GEvDIENKYVAPTIIVN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 423 VNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCQSLPFG 502
Cdd:PTZ00381 331 PDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFG 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1002286994 503 GVKDSGFGRFAGVEGLRACCLVKAVVED----------RWWPYVKT 538
Cdd:PTZ00381 411 GVGNSGMGAYHGKYGFDTFSHPKPVLNKstgnsfdlslRYPPYTSF 456
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
114-518 |
1.65e-68 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 227.70 E-value: 1.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 114 LRILLKYILEHQDLICEISSRDTGKTMVDASLgEIMTTCEKITWLLD-----EGEkwLKPEYRSCGRSMLHKKakvefyP 188
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDYMAEwarryEGE--IIQSDRPGENILLFKR------A 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 189 LGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASwSGCFYFRIIqaaLAAVGAPDNLVHIITGFAET-GQALVS 267
Cdd:PRK10090 72 LGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTP-NNAIAFAKI---VDEIGLPKGVFNLVLGRGETvGQELAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 268 S--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIY 345
Cdd:PRK10090 148 NpkVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 346 STFVSQVVKIIKSISVGPPLSGR-YDMGAICMIEHSEKLQNLVNDAVDKGAEIAgrgsfghLGEDAVDQ---FFPPTVLV 421
Cdd:PRK10090 228 DQFVNRLGEAMQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVA-------LGGKAVEGkgyYYPPTLLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 422 NVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMcQSLpF 501
Cdd:PRK10090 301 DVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM-QGF-H 378
|
410
....*....|....*..
gi 1002286994 502 GGVKDSGFGRFAGVEGL 518
Cdd:PRK10090 379 AGWRKSGIGGADGKHGL 395
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
39-511 |
3.46e-68 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 229.02 E-value: 3.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 39 LEDANQNKEDSYIYIPPRKGKGAQTDKVQcyEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILL 118
Cdd:PRK11241 3 LNDSTLFRQQALINGEWLDANNGEVIDVT--NPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 119 KYILEHQDLICEISSRDTGKTMVDASlGEIMTTCEKITWLLDEGEKWLK---PEYRSCGRSMLHKKakvefyPLGVIGAI 195
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAK-GEISYAASFIEWFAEEGKRIYGdtiPGHQADKRLIVIKQ------PIGVTAAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 196 VSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFA-ETGQALVSS--VDKI 272
Cdd:PRK11241 154 TPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRA----GIPAGVFNVVTGSAgAVGGELTSNplVRKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 273 IFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQV 352
Cdd:PRK11241 230 SFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 353 VKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDavdqFFPPTVLVNVNHTMKIMQE 432
Cdd:PRK11241 310 QQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGN----FFQPTILVDVPANAKVAKE 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286994 433 EAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYmcQSLPFGGVKDSGFGR 511
Cdd:PRK11241 386 ETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISN--EVAPFGGIKASGLGR 462
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
71-527 |
6.50e-68 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 227.70 E-value: 6.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASlGEIMT 150
Cdd:PRK09406 8 PATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK-AEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TCEKITWLLDEGEKWLKPE---YRSCGRSmlhkKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKvseHA 227
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADEpadAAAVGAS----RAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK---HA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 228 SwsgcfyfRIIQAAL------AAVGAPDnlvhiitGFAETgqALVSS--VDKII---------FVGSPGVGRMIMNRASD 290
Cdd:PRK09406 160 S-------NVPQTALyladlfRRAGFPD-------GCFQT--LLVGSgaVEAILrdprvaaatLTGSEPAGRAVAAIAGD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 291 TLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYD 370
Cdd:PRK09406 224 EIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 371 MGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSfghlGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEV 450
Cdd:PRK09406 304 VGPLATEQGRDEVEKQVDDAVAAGATILCGGK----RPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286994 451 VKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYmcQSLPFGGVKDSGFGRFAGVEGLRACCLVKAV 527
Cdd:PRK09406 380 IEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSY--PELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
80-528 |
9.06e-68 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 229.69 E-value: 9.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 80 FPALTP--DEVKEHVAQ------------ARKA--QKIWAKSSFKQRRqflRILLKY---ILEHQDLICEISSRDTGKTM 140
Cdd:PLN02466 75 FPTLDPrtGEVIAHVAEgdaedvnravaaARKAfdEGPWPKMTAYERS---RILLRFadlLEKHNDELAALETWDNGKPY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 141 VDASLGEIMTTCEKITWLLDEGEKWLKPEYRSCGR---SMLHKkakvefyPLGVIGAIVSWNYP---FHNVFNPMLAAif 214
Cdd:PLN02466 152 EQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPhhvQTLHE-------PIGVAGQIIPWNFPllmFAWKVGPALAC-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 215 sGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAETGQALVSS---VDKIIFVGSPGVGRMIMNRASDT 291
Cdd:PLN02466 223 -GNTIVLKTAEQTPLSALYAAKLLHEA----GLPPGVLNVVSGFGPTAGAALAShmdVDKLAFTGSTDTGKIVLELAAKS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 292 -LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYD 370
Cdd:PLN02466 298 nLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 371 MGAICMIEHSEKLQNLVNDAVDKGAEI-AGRGSFGHLGedavdQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEE 449
Cdd:PLN02466 378 QGPQIDSEQFEKILRYIKSGVESGATLeCGGDRFGSKG-----YYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDE 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286994 450 VVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFasSYMCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:PLN02466 453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCF--DVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
77-510 |
2.10e-67 |
|
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: 226.75 E-value: 2.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 77 LGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEIMTTCEKIT 156
Cdd:cd07097 28 VGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEA-RGEVTRAGQIFR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 157 WLLDEGekwlkpeYRSCGRSMLHKKAKVEFY----PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGc 232
Cdd:cd07097 107 YYAGEA-------LRLSGETLPSTRPGVEVEttrePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASA- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 233 fyFRIIQAaLAAVGAPDNLVHIITGF-AETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCE 309
Cdd:cd07097 179 --WALVEI-LEEAGLPAGVFNLVMGSgSEVGQALVEHpdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 310 DVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVND 389
Cdd:cd07097 256 DADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 390 AVDKGAEIA---GRGSFGHLGedavdQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVF 466
Cdd:cd07097 336 ARSEGAKLVyggERLKRPDEG-----YYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIV 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1002286994 467 SGNQKRAIKIASQLHCGVAAINdFASSYMCQSLPFGGVKDSGFG 510
Cdd:cd07097 411 TTSLKHATHFKRRVEAGVVMVN-LPTAGVDYHVPFGGRKGSSYG 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
84-519 |
4.80e-67 |
|
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: 225.20 E-value: 4.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 84 TPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASlGEIMTTCEKITWLLDE-- 161
Cdd:cd07147 19 GPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR-GEVARAIDTFRIAAEEat 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 162 ---GEkWLKPEY--RSCGRSMLHKKakvefYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCfyfr 236
Cdd:cd07147 98 riyGE-VLPLDIsaRGEGRQGLVRR-----FPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSAL---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 237 IIQAALAAVGAPDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTliPVTLELGGKDAFIVCEDVDLP 314
Cdd:cd07147 168 ILGEVLAETGLPKGAFSVLPCSRDDADLLVTDerIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 315 SVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAicMIE--HSEKLQNLVNDAVD 392
Cdd:cd07147 246 FAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGP--MISesEAERVEGWVNEAVD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 393 KGAEI-AGRGSFGHLgedavdqfFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQK 471
Cdd:cd07147 324 AGAKLlTGGKRDGAL--------LEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLE 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1002286994 472 RAIKIASQLHCGVAAINDfASSYMCQSLPFGGVKDSGFGRfagvEGLR 519
Cdd:cd07147 396 KALRAWDELEVGGVVIND-VPTFRVDHMPYGGVKDSGIGR----EGVR 438
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
77-514 |
1.40e-65 |
|
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: 222.87 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 77 LGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRrqfLRILLKY--ILEHQDLicEISSR---DTGKTMVDAsLGEImtt 151
Cdd:cd07124 60 LGTVQKATKEEAEAAVQAARAAFPTWRRTPPEER---ARLLLRAaaLLRRRRF--ELAAWmvlEVGKNWAEA-DADV--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 152 CEKITWLldegekwlkpEYRscGRSMLHKKAKV----------EFY-PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAV 220
Cdd:cd07124 131 AEAIDFL----------EYY--AREMLRLRGFPvemvpgednrYVYrPLGVGAVISPWNFPLAILAGMTTAALVTGNTVV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 221 IKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAET-GQALVSS--VDKIIFVGSPGVGRMIMNRASDT------ 291
Cdd:cd07124 199 LKPAEDTPVIAAKLVEILEEA----GLPPGVVNFLPGPGEEvGDYLVEHpdVRFIAFTGSREVGLRIYERAAKVqpgqkw 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 292 LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDM 371
Cdd:cd07124 275 LKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 372 GAICMIEHSEKLQNLVNDAVDKGAEIAGRGSfghLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVV 451
Cdd:cd07124 355 GPVIDKGARDRIRRYIEIGKSEGRLLLGGEV---LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEAL 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286994 452 KLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCQSLPFGGVKDSGFGRFAG 514
Cdd:cd07124 432 EIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAG 494
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
89-535 |
1.41e-65 |
|
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: 220.94 E-value: 1.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 89 KEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKWLKP 168
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 169 EYRScgRSMLHKKAKVEFY--PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALaavg 246
Cdd:cd07132 81 EPVK--KNLATLLDDVYIYkePLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYL---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 247 apDN-LVHIITGFA-ETGQALVSSVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAA 324
Cdd:cd07132 155 --DKeCYPVVLGGVeETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 325 LQSSGQNCAGAErfYV--HKDIYSTFVSQVVKIIKSISVGPPLSGRyDMGAICMIEHSEKLQNLVndavdKGAEIAGRGS 402
Cdd:cd07132 233 FINAGQTCIAPD--YVlcTPEVQEKFVEALKKTLKEFYGEDPKESP-DYGRIINDRHFQRLKKLL-----SGGKVAIGGQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 403 FghlgeDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHC 482
Cdd:cd07132 305 T-----DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSS 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286994 483 GVAAINDFASSYMCQSLPFGGVKDSGFGRFAGVEGL-----RACCLVK-----AVVEDRWWPY 535
Cdd:cd07132 380 GGVCVNDTIMHYTLDSLPFGGVGNSGMGAYHGKYSFdtfshKRSCLVKslnmeKLNSLRYPPY 442
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
71-531 |
1.39e-64 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 218.96 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASlGEIMT 150
Cdd:PRK13968 14 PATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 TCEKITWLLDEGEKWLKPEyrscgrSML--HKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKvseHA- 227
Cdd:PRK13968 93 SANLCDWYAEHGPAMLKAE------PTLveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK---HAp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 228 SWSGCFyfRIIQAALAAVGAPDNLVHIITGfAETGQALVSSVDKIIFV---GSPGVGRMIMNRASDTLIPVTLELGGKDA 304
Cdd:PRK13968 164 NVMGCA--QLIAQVFKDAGIPQGVYGWLNA-DNDGVSQMINDSRIAAVtvtGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 305 FIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQ 384
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 385 NLVNDAVDKGA-------EIAGRGSfghlgedavdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDS 457
Cdd:PRK13968 321 HQVEATLAEGArlllggeKIAGAGN-----------YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDS 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286994 458 KYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYmcQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVVEDR 531
Cdd:PRK13968 390 EFGLSATIFTTDETQARQMAARLECGGVFINGYCASD--ARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKDR 461
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
188-528 |
1.73e-64 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 219.69 E-value: 1.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 188 PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAETGQALVS 267
Cdd:PLN02766 158 PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLA----GVPDGVINVVTGFGPTAGAAIA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 268 S---VDKIIFVGSPGVGRMIMNRASDT-LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKD 343
Cdd:PLN02766 234 ShmdVDKVSFTGSTEVGRKIMQAAATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 344 IYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAE-IAGRGSFGHLGedavdQFFPPTVLVN 422
Cdd:PLN02766 314 IYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATlLTGGKPCGDKG-----YYIEPTIFTD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 423 VNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASsyMCQSLPFG 502
Cdd:PLN02766 389 VTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFA--FDPDCPFG 466
|
330 340
....*....|....*....|....*.
gi 1002286994 503 GVKDSGFGRFAGVEGLRACCLVKAVV 528
Cdd:PLN02766 467 GYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
106-514 |
9.48e-62 |
|
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: 210.73 E-value: 9.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 106 SFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKWLKPEYRSCGRSMLHKKAKVE 185
Cdd:cd07137 19 SAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLTTFPAKAEIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 186 FYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALaavgaPDNLVHIITGFAETGQAL 265
Cdd:cd07137 99 SEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYL-----DTKAIKVIEGGVPETTAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 266 VSSV-DKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQ-VAVRAALQSSGQNCAGAERFYVHKD 343
Cdd:cd07137 174 LEQKwDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRrIAGGKWGCNNGQACIAPDYVLVEES 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 344 IYSTFVSQVVKIIKSISVGPPLSGRyDMGAICMIEHSEKLQNLVNDAVDKGAEIAGrgsfGHLGEDAVdqFFPPTVLVNV 423
Cdd:cd07137 254 FAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVADKIVHG----GERDEKNL--YIEPTILLDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 424 NHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCQSLPFGG 503
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGG 406
|
410
....*....|.
gi 1002286994 504 VKDSGFGRFAG 514
Cdd:cd07137 407 VGESGFGAYHG 417
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
86-514 |
8.61e-59 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 204.19 E-value: 8.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 86 DEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKW 165
Cdd:PLN02203 6 ETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 166 LKPEYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALAAv 245
Cdd:PLN02203 86 MAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 246 gapdNLVHIITGFAETGQALVSSV-DKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVcEDVDLPSVVQVAVRAA 324
Cdd:PLN02203 165 ----KAVKVIEGGPAVGEQLLQHKwDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV-DSLSSSRDTKVAVNRI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 325 LQS-----SGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYdMGAICMIEHSEKLQNLVNDAVDKGAEIAG 399
Cdd:PLN02203 240 VGGkwgscAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRVAASIVHG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 400 rgsfGHLGEDAVdqFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQ 479
Cdd:PLN02203 319 ----GSIDEKKL--FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSE 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1002286994 480 LHCGVAAINDFASSYMCQSLPFGGVKDSGFGRFAG 514
Cdd:PLN02203 393 TSSGSVTFNDAIIQYACDSLPFGGVGESGFGRYHG 427
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
71-527 |
5.50e-58 |
|
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: 201.95 E-value: 5.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKA--QKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTG-------KTMV 141
Cdd:cd07140 28 PTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGavytlalKTHV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 142 DASlgeIMTT------CEKI---TWLLDEGekwlKPEYRSCgrsmLHKKAkvefyPLGVIGAIVSWNYPFHNVFNPMLAA 212
Cdd:cd07140 108 GMS---IQTFryfagwCDKIqgkTIPINQA----RPNRNLT----LTKRE-----PIGVCGIVIPWNYPLMMLAWKMAAC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 213 IFSGNAAVIKVSEHASWSGCFYfriiqAALAA-VGAPDNLVHIITGFAE-TGQALVSSVD--KIIFVGSPGVGRMIMNRA 288
Cdd:cd07140 172 LAAGNTVVLKPAQVTPLTALKF-----AELTVkAGFPKGVINILPGSGSlVGQRLSDHPDvrKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 289 SDT-LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSG 367
Cdd:cd07140 247 AVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 368 RYDMGAICMIEHSEKLQNLVNDAVDKGAEIAgrgsfghLGEDAVDQ---FFPPTVLVNVNHTMKIMQEEAFGPILPIMKF 444
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLV-------YGGKQVDRpgfFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 445 NSD--EEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIN-----DFASsymcqslPFGGVKDSGFGRFAGVEG 517
Cdd:cd07140 400 DDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynktDVAA-------PFGGFKQSGFGKDLGEEA 472
|
490
....*....|
gi 1002286994 518 LRACCLVKAV 527
Cdd:cd07140 473 LNEYLKTKTV 482
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
50-532 |
6.11e-58 |
|
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: 201.59 E-value: 6.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 50 YIYIPPRKGKGAQTDKVqcYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRrqfLRILLKY---ILEHQD 126
Cdd:cd07085 4 FINGEWVESKTTEWLDV--YNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKR---QQVMFKFrqlLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 127 LICEISSRDTGKTMVDAsLGEIMTTCEKItwlldegekwlkpEYrSCGRSMLHKKAKVE-----------FYPLGVIGAI 195
Cdd:cd07085 79 ELARLITLEHGKTLADA-RGDVLRGLEVV-------------EF-ACSIPHLLKGEYLEnvargidtysyRQPLGVVAGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 196 VSWNYPFH--NVFNPMlaAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAETGQALVS--SVDK 271
Cdd:cd07085 144 TPFNFPAMipLWMFPM--AIACGNTFVLKPSERVPGAAMRLAELLQEA----GLPDGVLNVVHGGKEAVNALLDhpDIKA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 272 IIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQ 351
Cdd:cd07085 218 VSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 352 VVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIA--GRGSFGHLGEDAvdQFFPPTVLVNVNHTMKI 429
Cdd:cd07085 298 LVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVldGRGVKVPGYENG--NFVGPTILDNVTPDMKI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 430 MQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIN--------DFassymcqslPF 501
Cdd:cd07085 376 YKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvpipvplaFF---------SF 446
|
490 500 510
....*....|....*....|....*....|...
gi 1002286994 502 GGVKDSGFG--RFAGVEGLRACCLVKAVVEdRW 532
Cdd:cd07085 447 GGWKGSFFGdlHFYGKDGVRFYTQTKTVTS-RW 478
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
63-508 |
1.55e-57 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 201.32 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 63 TDKVQCYEPA-TMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRqflRILLK---YILEHQDLICEISSRDTGK 138
Cdd:PRK03137 49 EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRA---RILLRaaaIIRRRKHEFSAWLVKEAGK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 139 TMVDASlGEimtTCEKITWLldegekwlkpEYRscGRSMLHKKAKVE-----------FY-PLGViGAIVS-WNYPFHNV 205
Cdd:PRK03137 126 PWAEAD-AD---TAEAIDFL----------EYY--ARQMLKLADGKPvesrpgehnryFYiPLGV-GVVISpWNFPFAIM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 206 FNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGF-AETGQALVSSVDK--IIFVGSPGVGR 282
Cdd:PRK03137 189 AGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEA----GLPAGVVNFVPGSgSEVGDYLVDHPKTrfITFTGSREVGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 283 MIMNRASDT------LIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKII 356
Cdd:PRK03137 265 RIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 357 KSISVGPPLSGRYdMGAICmiehSEKLQNLVNDAVDKGAEiAGRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFG 436
Cdd:PRK03137 345 KELTVGNPEDNAY-MGPVI----NQASFDKIMSYIEIGKE-EGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFG 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002286994 437 PILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCQSLPFGGVKDSG 508
Cdd:PRK03137 419 PVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 490
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
48-511 |
7.71e-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: 198.83 E-value: 7.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 48 DSYI---YIPPRKGKgaQTDKVQcyePATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEH 124
Cdd:cd07116 2 DNFIggeWVAPVKGE--YFDNIT---PVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 125 QDLICEISSRDTGKTMVDASLGEIMTTCEKITWlldegekwlkpeYRSCGRSMLHKKAKV-------EFY-PLGVIGAIV 196
Cdd:cd07116 77 LEMLAVAETWDNGKPVRETLAADIPLAIDHFRY------------FAGCIRAQEGSISEIdentvayHFHePLGVVGQII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 197 SWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALaavgaPDNLVHIITGF-AETGQALVSS--VDKII 273
Cdd:cd07116 145 PWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLL-----PPGVVNVVNGFgLEAGKPLASSkrIAKVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 274 FVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDV----D--LPSVVQVAVRAALqSSGQNCAGAERFYVHKDIYST 347
Cdd:cd07116 220 FTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADVmdadDafFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 348 FVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVlVNVNHTM 427
Cdd:cd07116 299 FMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTT-FKGGNKM 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 428 KIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFaSSYMCQSlPFGGVKDS 507
Cdd:cd07116 378 RIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCY-HLYPAHA-AFGGYKQS 455
|
....
gi 1002286994 508 GFGR 511
Cdd:cd07116 456 GIGR 459
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-511 |
2.76e-55 |
|
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: 193.26 E-value: 2.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 87 EVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEIMTTCEKITWLLDEGEKWL 166
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 167 KPEyrscGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavG 246
Cdd:cd07095 80 GER----ATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA----G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 247 APDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGRMIMNR-ASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRA 323
Cdd:cd07095 152 LPPGVLNLVQGGRETGEALAAHegIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 324 ALQSSGQNCAGAERFYVHKDIYS-TFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGS 402
Cdd:cd07095 232 AFLTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 403 FGhlgeDAVDQFFPPTvLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHC 482
Cdd:cd07095 312 RL----VAGTAFLSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420 430
....*....|....*....|....*....|..
gi 1002286994 483 GVAAIN---DFASSymcqSLPFGGVKDSGFGR 511
Cdd:cd07095 387 GIVNWNrptTGASS----TAPFGGVGLSGNHR 414
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
51-511 |
3.10e-54 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 192.03 E-value: 3.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 51 IYIPPRKGKGAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKA--QKIWAKSSFKQRRQFLRILLKYILEHQDLI 128
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 129 CEISSRDTGKTMVDASLGEIMTTCEKITWLLDEGEKwLKPEYRSCGRSMLhkkAKVEFYPLGVIGAIVSWNYPFHNV--- 205
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDK-VYGEVATTSSHEL---AMIVREPVGVIAAIVPWNFPLLLTcwk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 206 FNPMLAAifsGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFA-ETGQALV--SSVDKIIFVGSPGVGR 282
Cdd:PRK09847 178 LGPALAA---GNSVILKPSEKSPLSAIRLAGLAKEA----GLPDGVLNVVTGFGhEAGQALSrhNDIDAIAFTGSTRTGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 283 MIMNRASDT-LIPVTLELGGKDAFIVCEDV-DLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSIS 360
Cdd:PRK09847 251 QLLKDAGDSnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 361 VGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAE-IAGRGSfGHLGedavdqFFPPTVLVNVNHTMKIMQEEAFGPIL 439
Cdd:PRK09847 331 PGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLlLDGRNA-GLAA------AIGPTIFVDVDPNASLSREEIFGPVL 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002286994 440 PIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMcqSLPFGGVKDSGFGR 511
Cdd:PRK09847 404 VVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNGR 473
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
66-510 |
3.69e-52 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 186.50 E-value: 3.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 66 VQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDA-- 143
Cdd:PLN00412 33 VAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAvt 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 144 ----SLGEIMTTCEKITWLLDEGEKWLKPEYRSCGRSMLHKKAKVefyPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAA 219
Cdd:PLN00412 113 evvrSGDLISYTAEEGVRILGEGKFLVSDSFPGNERNKYCLTSKI---PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 220 VIKVSEHASWSGcfyFRIIQAALAAvGAPDNLVHIITGF-AETGQALVS--SVDKIIFVGSPgVGRMIMNRASdtLIPVT 296
Cdd:PLN00412 190 VLKPPTQGAVAA---LHMVHCFHLA-GFPKGLISCVTGKgSEIGDFLTMhpGVNCISFTGGD-TGIAISKKAG--MVPLQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 297 LELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPlSGRYDMGAICM 376
Cdd:PLN00412 263 MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 377 IEHSEKLQNLVNDAVDKGAEIagrgsfgHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLAND 456
Cdd:PLN00412 342 ESSANFIEGLVMDAKEKGATF-------CQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1002286994 457 SKYGL-GCaVFSGNQKRAIKIASQLHCGVAAINDfASSYMCQSLPFGGVKDSGFG 510
Cdd:PLN00412 415 SNFGLqGC-VFTRDINKAILISDAMETGTVQINS-APARGPDHFPFQGLKDSGIG 467
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
60-514 |
1.79e-51 |
|
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: 183.95 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 60 GAQTDKVQCYEPATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKT 139
Cdd:cd07130 8 GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 140 MVDAsLGEI---MTTCEKITWLLDEGEKWLKPEYRScGRSMLHKkakveFYPLGVIGAIVSWNYPFhNVF--NPMLAAIf 214
Cdd:cd07130 88 LPEG-LGEVqemIDICDFAVGLSRQLYGLTIPSERP-GHRMMEQ-----WNPLGVVGVITAFNFPV-AVWgwNAAIALV- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 215 SGNAAVIKVSEHASWSGCFYFRIIQAALAAVGAPDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGRMIMNRASDTL 292
Cdd:cd07130 159 CGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDprVPLVSFTGSTAVGRQVGQAVAARF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 293 IPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLsgryDMG 372
Cdd:cd07130 239 GRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL----DDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 373 AICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVlVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVK 452
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286994 453 LANDSKYGLGCAVFSGNQKRAIKIASQL--HCGVAAINdfassymcqsLP---------FGGVKDSGFGRFAG 514
Cdd:cd07130 394 WNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVN----------IGtsgaeiggaFGGEKETGGGRESG 456
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
87-514 |
1.12e-43 |
|
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: 163.13 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 87 EVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDaslgEIMTTCEKITWLLDEGEKWL 166
Cdd:cd07083 56 EAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVE----AIDDVAEAIDFIRYYARAAL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 167 KPEYRSCGRSMLHKKAKVEFY-PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaav 245
Cdd:cd07083 132 RLRYPAVEVVPYPGEDNESFYvGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEA---- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 246 GAPDNLVHIITGFAET-GQALVSS--VDKIIFVGSPGVGRMIMNRASD------TLIPVTLELGGKDAFIVCEDVDLPSV 316
Cdd:cd07083 208 GFPPGVVQFLPGVGEEvGAYLTEHerIRGINFTGSLETGKKIYEAAARlapgqtWFKRLYVETGGKNAIIVDETADFELV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 317 VQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAE 396
Cdd:cd07083 288 VEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 397 IAGrGSFghlgEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDE--EVVKLANDSKYGLGCAVFSGNQKRAI 474
Cdd:cd07083 368 VLG-GKR----LEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1002286994 475 KIASQLHCGVAAINDFASSYMCQSLPFGGVKDSGFGRFAG 514
Cdd:cd07083 443 EARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
135-578 |
1.31e-43 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 162.52 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 135 DTGKTMVDASLGEIMTTCEKITWLLDEGEKWLKPEYRSCGRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIF 214
Cdd:PLN02174 59 DLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 215 SGNAAVIKVSEHASWSGCFYFRIIQAALAAvgapdNLVHIITG-FAETGQALVSSVDKIIFVGSPGVGRMIMNRASDTLI 293
Cdd:PLN02174 139 AGNAVVLKPSELAPASSALLAKLLEQYLDS-----SAVRVVEGaVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 294 PVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQ-SSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRyDMG 372
Cdd:PLN02174 214 PVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 373 AICMIEHSEKLQNLVNDAvdkgaEIAGRGSFGhlGE-DAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVV 451
Cdd:PLN02174 293 RIVNSTHFDRLSKLLDEK-----EVSDKIVYG--GEkDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESF 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 452 KLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAINDFASSYMCQSLPFGGVKDSGFGRFAGVEGLRACCLVKAVVedr 531
Cdd:PLN02174 366 DVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVL--- 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1002286994 532 wwpYVKTMIPKPIQYPVSENGfefQELLVETLYGLSVWDRLRSLVNL 578
Cdd:PLN02174 443 ---YRSLFGDSAVRYPPYSRG---KLRLLKALVDSNIFDIFKVLLGL 483
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
32-514 |
3.08e-42 |
|
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: 159.28 E-value: 3.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 32 DVDASDVLEDANQNKEDSYIYIPPRKGKGAQTDKVQ-CYEPATMKY-LGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQ 109
Cdd:cd07125 13 EVPLEALADALKAFDEKEWEAIPIINGEETETGEGApVIDPADHERtIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 110 RRqflRILLKY--ILEHQ--DLICeISSRDTGKTMVDAsLGEIMttcEKITWL---LDEGEKWLKPEYRSCGRSMLhkkA 182
Cdd:cd07125 93 RA---EILEKAadLLEANrgELIA-LAAAEAGKTLADA-DAEVR---EAIDFCryyAAQARELFSDPELPGPTGEL---N 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 183 KVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCfyfRIIQAALAAvGAPDNLVHIITGF-AET 261
Cdd:cd07125 162 GLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAA---RAVELLHEA-GVPRDVLQLVPGDgEEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 262 GQALVS--SVDKIIFVGSPGVGRMImNRA----SDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGA 335
Cdd:cd07125 238 GEALVAhpRIDGVIFTGSTETAKLI-NRAlaerDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 336 ERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNdavdkgaeiAGRGSFGHLGEDAVDQ-- 413
Cdd:cd07125 317 RLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTE---------LMRGEAWLIAPAPLDDgn 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 414 --FFPPTVLVNVN---HtmkimQEEAFGPILPIMKFNSD--EEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAA 486
Cdd:cd07125 388 gyFVAPGIIEIVGifdL-----TTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLY 462
|
490 500
....*....|....*....|....*...
gi 1002286994 487 INDFASSYMCQSLPFGGVKDSGFGRFAG 514
Cdd:cd07125 463 INRNITGAIVGRQPFGGWGLSGTGPKAG 490
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
84-508 |
2.46e-36 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 142.02 E-value: 2.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 84 TPDEVKEHVAQARKAQKIWAKSSFKQRrqfLRILLKY---ILEHQDLICEISSRDTGK------TMVDASLGEIMT---- 150
Cdd:PRK09457 35 TAAQVDAAVRAARAAFPAWARLSFEER---QAIVERFaalLEENKEELAEVIARETGKplweaaTEVTAMINKIAIsiqa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 151 ----TCEKITWLLDegekwlkpeyrscGRSML-HKkakvefyPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSE 225
Cdd:PRK09457 112 yherTGEKRSEMAD-------------GAAVLrHR-------PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 226 HASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAETGQALVSS--VDKIIFVGSPGVGrMIMNR--ASDTLIPVTLELGG 301
Cdd:PRK09457 172 LTPWVAELTVKLWQQA----GLPAGVLNLVQGGRETGKALAAHpdIDGLLFTGSANTG-YLLHRqfAGQPEKILALEMGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 302 KDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYS-TFVSQVVKIIKSISVGPPLSgryD----MGAICM 376
Cdd:PRK09457 247 NNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVGRWDA---EpqpfMGAVIS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 377 IEHSEKLQNLVNDAVDKGAEI--------AGRGsfghlgedavdqFFPPTvLVNVNHTMKIMQEEAFGPILPIMKFNSDE 448
Cdd:PRK09457 324 EQAAQGLVAAQAQLLALGGKSllemtqlqAGTG------------LLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFD 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286994 449 EVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIN---DFASSymcqSLPFGGVKDSG 508
Cdd:PRK09457 391 EAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkplTGASS----AAPFGGVGASG 449
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
71-488 |
5.78e-31 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 127.94 E-value: 5.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 71 PATMKYLGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRqflRILLKY---ILEHQDLICEISSRDTGKTMVDaSLGE 147
Cdd:PLN02419 136 PATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQ---RVMLKFqelIRKNMDKLAMNITTEQGKTLKD-SHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 148 IMTTCEKITwlldegekwlkpeyRSCGRSMLHK-------KAKVEFY----PLGVIGAIVSWNYPFHNVFNPMLAAIFSG 216
Cdd:PLN02419 212 IFRGLEVVE--------------HACGMATLQMgeylpnvSNGVDTYsirePLGVCAGICPFNFPAMIPLWMFPVAVTCG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 217 NAAVIKVSEHASWSGcfyfrIIQAALA-AVGAPDNLVHIITGFAETGQALVSSVD--KIIFVGSPGVGRMIMNRASDTLI 293
Cdd:PLN02419 278 NTFILKPSEKDPGAS-----VILAELAmEAGLPDGVLNIVHGTNDTVNAICDDEDirAVSFVGSNTAGMHIYARAAAKGK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 294 PVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYStFVSQVVKIIKSISVGPPLSGRYDMGA 373
Cdd:PLN02419 353 RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKS-WEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 374 ICMIEHSEKLQNLVNDAVDKGAEIAGRGSFGHLGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEEVVKL 453
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430
....*....|....*....|....*....|....*
gi 1002286994 454 ANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIN 488
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
188-510 |
6.28e-31 |
|
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: 125.99 E-value: 6.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 188 PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAETGQALVS 267
Cdd:cd07148 124 PIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEA----GLPEGWCQAVPCENAVAEKLVT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 268 S--VDKIIFVGSPGVGRMIMNRASdtliPVT---LELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHK 342
Cdd:cd07148 200 DprVAFFSFIGSARVGWMLRSKLA----PGTrcaLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 343 DIYSTFVSQVVKIIKSISVGPPLSGRYDMGAICMIEHSEKLQNLVNDAVDKGAEIAGRGSfgHLGedavDQFFPPTVLVN 422
Cdd:cd07148 276 EIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGK--RLS----DTTYAPTVLLD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 423 VNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCGVAAIND---FASSYMcqsl 499
Cdd:cd07148 350 PPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDhtaFRVDWM---- 425
|
330
....*....|.
gi 1002286994 500 PFGGVKDSGFG 510
Cdd:cd07148 426 PFAGRRQSGYG 436
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
188-514 |
2.37e-30 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 124.95 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 188 PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALAAVGAPDNLVHIITGFAETGQALV- 266
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAk 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 267 -SSVDKIIFVGSPGVGRMIMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIY 345
Cdd:PLN02315 234 dTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIY 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 346 STFVSQVVKIIKSISVGPPLsgryDMGAICMIEHSEKLQnlvnDAVDKGAEI----AGRGSFGHLGEDAVDQFFPPTVlV 421
Cdd:PLN02315 314 DDVLEQLLTVYKQVKIGDPL----EKGTLLGPLHTPESK----KNFEKGIEIiksqGGKILTGGSAIESEGNFVQPTI-V 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 422 NVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLANDSKYGLGCAVFSGNQKRAIKIASQL--HCGVAAINdfassymcqsL 499
Cdd:PLN02315 385 EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVN----------I 454
|
330 340
....*....|....*....|....
gi 1002286994 500 P---------FGGVKDSGFGRFAG 514
Cdd:PLN02315 455 PtngaeiggaFGGEKATGGGREAG 478
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
77-508 |
4.02e-30 |
|
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: 124.24 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 77 LGYFPALTPDEVKEHVAQARKAQKIWAKSSFKQRRQ-FLRI--LL--KYilehqdliceissRDT---------GKTMVD 142
Cdd:cd07123 60 LATYHYADAALVEKAIEAALEARKEWARMPFEDRAAiFLKAadLLsgKY-------------RYElnaatmlgqGKNVWQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 143 AslgEIMTTCEKITWL------LDEGEKWlKPEyrscgRSMLHKKAKVEFYPL-GVIGAIVswnyPFHnvF-----NPML 210
Cdd:cd07123 127 A---EIDAACELIDFLrfnvkyAEELYAQ-QPL-----SSPAGVWNRLEYRPLeGFVYAVS----PFN--FtaiggNLAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 211 AAIFSGNAAVIKVSEHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAET-GQALVSSVD--KIIFVGSPGVGRMIMNR 287
Cdd:cd07123 192 APALMGNVVLWKPSDTAVLSNYLVYKILEEA----GLPPGVINFVPGDGPVvGDTVLASPHlaGLHFTGSTPTFKSLWKQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 288 ASDTL-----IP-VTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISV 361
Cdd:cd07123 268 IGENLdryrtYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKM 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 362 GPPLSGRYDMGAICMIEHSEKLQNLVNDA-VDKGAEIAGRGSfghlGEDAVDQFFPPTVLVNVNHTMKIMQEEAFGPILP 440
Cdd:cd07123 348 GDPDDFSNFMGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGK----CDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLT 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286994 441 IMKF-NSD-EEVVKLAND-SKYGLGCAVFSGNQKrAIKIASQLH---CGVAAINDFASSYMCQSLPFGGVKDSG 508
Cdd:cd07123 424 VYVYpDSDfEETLELVDTtSPYALTGAIFAQDRK-AIREATDALrnaAGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
84-514 |
3.76e-22 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 101.48 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 84 TPDEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDAsLGEIMttcEKITWL---LD 160
Cdd:PRK11905 588 SAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANA-IAEVR---EAVDFLryyAA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 161 EGEKWLKPEYRScgrsmlhkkakvefyPLGVIGAIVSWNYPFhnvfnpmlaAIF---------SGNAAVIKVSEHASwsg 231
Cdd:PRK11905 664 QARRLLNGPGHK---------------PLGPVVCISPWNFPL---------AIFtgqiaaalvAGNTVLAKPAEQTP--- 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 232 cfyfrIIqAALA-----AVGAPDNLVHIITGFAET-GQALVSS--VDKIIFVGSPGVGRMImNRA----SDTLIPVTLEL 299
Cdd:PRK11905 717 -----LI-AARAvrllhEAGVPKDALQLLPGDGRTvGAALVADprIAGVMFTGSTEVARLI-QRTlakrSGPPVPLIAET 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 300 GGKDAFIvcedVD---LP-SVVQVAVRAALQSSGQNCAgAER-FYVHKDIystfVSQVVKIIK--------------SIS 360
Cdd:PRK11905 790 GGQNAMI----VDssaLPeQVVADVIASAFDSAGQRCS-ALRvLCLQEDV----ADRVLTMLKgamdelrigdpwrlSTD 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 361 VGPPLsgryDMGAICMIE-HSEKLQNL--------VNDAVDKGAeiagrgsfghlgedavdqFFPPTvLVNVNHtMKIMQ 431
Cdd:PRK11905 861 VGPVI----DAEAQANIEaHIEAMRAAgrlvhqlpLPAETEKGT------------------FVAPT-LIEIDS-ISDLE 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 432 EEAFGPILPIMKFNSDE--EVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCG--------VAAIndfassymCQSLPF 501
Cdd:PRK11905 917 REVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGniyvnrniIGAV--------VGVQPF 988
|
490
....*....|...
gi 1002286994 502 GGVKDSGFGRFAG 514
Cdd:PRK11905 989 GGEGLSGTGPKAG 1001
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
84-483 |
9.33e-22 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 100.40 E-value: 9.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 84 TPDEVKEHVAQARKAQKIWAKSSFKQRRQflrILLKY--ILE-HQDLICEISSRDTGKTMVDAsLGEImttCEKItwllD 160
Cdd:COG4230 591 TAADVEAALAAAQAAFPAWSATPVEERAA---ILERAadLLEaHRAELMALLVREAGKTLPDA-IAEV---REAV----D 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 161 -------EGEkwlkpeyRSCGRSMLHKkakvefyPLGVIGAIVSWNYPFhnvfnpmlaAIF---------SGNAAVIKVS 224
Cdd:COG4230 660 fcryyaaQAR-------RLFAAPTVLR-------GRGVFVCISPWNFPL---------AIFtgqvaaalaAGNTVLAKPA 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 225 EHASWSGCFYFRIIQAAlaavGAPDNLVHIITGFAET-GQALVSS--VDKIIFVGSPGVGRMImNRA----SDTLIPVTL 297
Cdd:COG4230 717 EQTPLIAARAVRLLHEA----GVPADVLQLLPGDGETvGAALVADprIAGVAFTGSTETARLI-NRTlaarDGPIVPLIA 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 298 ELGGKDAFIvcedVD---LP-SVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTfvsqVVKIIKS----ISVGPPLSGRY 369
Cdd:COG4230 792 ETGGQNAMI----VDssaLPeQVVDDVLASAFDSAGQRCSALRVLCVQEDIADR----VLEMLKGamaeLRVGDPADLST 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 370 DMG------AICMIE-HSEKLQ---NLVnDAVDKGAEIAGrgsfGHlgedavdqFFPPTvLVNVNHtMKIMQEEAFGPIL 439
Cdd:COG4230 864 DVGpvidaeARANLEaHIERMRaegRLV-HQLPLPEECAN----GT--------FVAPT-LIEIDS-ISDLEREVFGPVL 928
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1002286994 440 PIMKFNSDE--EVVKLANDSKYGLGCAVFSGNQKRAIKIASQLHCG 483
Cdd:COG4230 929 HVVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVG 974
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
95-454 |
5.36e-19 |
|
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: 89.99 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 95 ARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTmvDASLGEIMTTCEKITWLLDEGEKWLKP----EY 170
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG--WMFAENICGDQVQLRARAFVIYSYRIPhepgNH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 171 RSCGRSMlhkKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALAavgAPDN 250
Cdd:cd07084 86 LGQGLKQ---QSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 251 LVHIITGFAETGQALVS--SVDKIIFVGSPGVGRMIMNRASDtlIPVTLELGGKDAFIVCEDVD-LPSVVQVAVRAALQS 327
Cdd:cd07084 160 DVTLINGDGKTMQALLLhpNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 328 SGQNCAGAERFYVHKDIYST-FVSQVVKIIKSISVGPPLSGR--YDmGAICMIEHSEKlqnlvndavDKGAEIAGRGSFG 404
Cdd:cd07084 238 SGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLLLGPvqTF-TTLAMIAHMEN---------LLGSVLLFSGKEL 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286994 405 HLGEdaVDQFF----PPTVLV---NVNHTMKIMQEEAFGPILPIMKFNSDEEVVKLA 454
Cdd:cd07084 308 KNHS--IPSIYgacvASALFVpidEILKTYELVTEEIFGPFAIVVEYKKDQLALVLE 362
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
86-286 |
2.53e-12 |
|
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: 69.19 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 86 DEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITwlldeGEKW 165
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAEKTP-----GTED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 166 LKPEYRSCGRSMlhkkAKVEFYPLGVIGAIVSWNYPFHNVFN---PMLAAifsGNAAVIKVSEHASWSGCFYFRIIQAAL 242
Cdd:cd07121 79 LTTTAWSGDNGL----TLVEYAPFGVIGAITPSTNPTETIINnsiSMLAA---GNAVVFNPHPGAKKVSAYAVELINKAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002286994 243 AAVGAPDNLVHII-TGFAETGQALVS--SVDKIIFVGSPGVGRMIMN 286
Cdd:cd07121 152 AEAGGPDNLVVTVeEPTIETTNELMAhpDINLLVVTGGPAVVKAALS 198
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
188-514 |
4.91e-11 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 66.15 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 188 PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASwsgcfyfrIIQAA----LAAVGAPDNLVHIITGFAET-G 262
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTP--------LIAAQavriLLEAGVPAGVVQLLPGRGETvG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 263 QALVSS--VDKIIFVGSPGVGRMIMNRASDTL------IPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAG 334
Cdd:PRK11809 840 AALVADarVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSA 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 335 AERFYVHKDIystfVSQVVKIIKsisvgpplsgrydmGAI--CMIEHSEKLQNLVNDAVDKGAEI-----------AGRG 401
Cdd:PRK11809 920 LRVLCLQDDV----ADRTLKMLR--------------GAMaeCRMGNPDRLSTDIGPVIDAEAKAnierhiqamraKGRP 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 402 SFGHLGEDAVDQ----FFPPTvLVNVNHTMKiMQEEAFGPILPIMKFNSDE--EVVKLANDSKYGLGCAVFSGNQKRAIK 475
Cdd:PRK11809 982 VFQAARENSEDWqsgtFVPPT-LIELDSFDE-LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQ 1059
|
330 340 350
....*....|....*....|....*....|....*....
gi 1002286994 476 IASQLHCGVAAINDFASSYMCQSLPFGGVKDSGFGRFAG 514
Cdd:PRK11809 1060 VTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAG 1098
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
88-520 |
7.33e-11 |
|
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: 64.60 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 88 VKEHVAQAR-KAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRdTGKTMVDASL---GEIMT----------TCE 153
Cdd:cd07128 38 FAAAVAYAReKGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAA-TGATRRDSWIdidGGIGTlfayaslgrrELP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 154 KITWLLDEGEKWLKPEYRSCGRSMLHKKAkvefyplGVIGAIVSWNYPFHNV---FNPMLAAifsGNAAVIKVSEHASWs 230
Cdd:cd07128 117 NAHFLVEGDVEPLSKDGTFVGQHILTPRR-------GVAVHINAFNFPVWGMlekFAPALLA---GVPVIVKPATATAY- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 231 gcfyfrIIQAALAAVGA----PDNLVHIITGfaETGQAL--VSSVDKIIFVGSPGVGRMImnRASDTL----IPVTLELG 300
Cdd:cd07128 186 ------LTEAVVKDIVEsgllPEGALQLICG--SVGDLLdhLGEQDVVAFTGSAATAAKL--RAHPNIvarsIRFNAEAD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 301 GKDAFIVCEDV-------DLpsVVQVAVRAALQSSGQNCAGAERFYVHKDIYSTFVSQVVKIIKSISVGPPLSGRYDMGA 373
Cdd:cd07128 256 SLNAAILGPDAtpgtpefDL--FVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 374 ICMIEHSEKlqnlVNDAVDK---GAEIA--GRGSFGHLGEDAVD-QFFPPTVLV--NVNHTMKIMQEEAFGPILPIMKFN 445
Cdd:cd07128 334 LVSREQRED----VRAAVATllaEAEVVfgGPDRFEVVGADAEKgAFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 446 SDEEVVKLANDSKYGLGCAVFSGNQKRA----IKIASqLHCGVAAIN-DFASSYMCQSLPFGGVKDSGFGRFAGVE---G 517
Cdd:cd07128 410 SLAEAIELAARGRGSLVASVVTNDPAFArelvLGAAP-YHGRLLVLNrDSAKESTGHGSPLPQLVHGGPGRAGGGEelgG 488
|
...
gi 1002286994 518 LRA 520
Cdd:cd07128 489 LRG 491
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
86-286 |
5.97e-10 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 61.84 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 86 DEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRDTGKTMVDASLGEIMTTCEKITwlldeGEKW 165
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKNVAAAEKTP-----GVED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 166 LKPEYRSCGRSMlhkkAKVEFYPLGVIGAIVSWNYPFHNVFN---PMLAA----IFSGNAAVIKVSEHAswsgcfyFRII 238
Cdd:PRK15398 111 LTTEALTGDNGL----TLIEYAPFGVIGAVTPSTNPTETIINnaiSMLAAgnsvVFSPHPGAKKVSLRA-------IELL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002286994 239 QAALAAVGAPDNLVHII-TGFAETGQALVS--SVDKIIFVGSPGVGRMIMN 286
Cdd:PRK15398 180 NEAIVAAGGPENLVVTVaEPTIETAQRLMKhpGIALLVVTGGPAVVKAAMK 230
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
187-449 |
1.50e-06 |
|
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: 50.96 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 187 YPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIiqaaLAAVGAPDNLVHIITGFAETGQALV 266
Cdd:cd07126 141 WPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRL----LHLCGMPATDVDLIHSDGPTMNKIL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 267 SSVD--KIIFVGSPGVGRMImnrASDTLIPVTLELGGKDAFIVCEDV-DLPSVVQVAVRAALQSSGQNCAGAERFYVHKD 343
Cdd:cd07126 217 LEANprMTLFTGSSKVAERL---ALELHGKVKLEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAHEN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 344 -IYSTFVSQVVKI-----IKSISVGPPLSgrYDMGAicMIEHSEKLQNLVNDAVDKGAEIAGRGS----FGHLGEDAVdq 413
Cdd:cd07126 294 wVQAGILDKLKALaeqrkLEDLTIGPVLT--WTTER--ILDHVDKLLAIPGAKVLFGGKPLTNHSipsiYGAYEPTAV-- 367
|
250 260 270
....*....|....*....|....*....|....*.
gi 1002286994 414 fFPPTVLVNVNHTMKIMQEEAFGPILPIMKFNSDEE 449
Cdd:cd07126 368 -FVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQL 402
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
86-354 |
2.06e-06 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 50.45 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 86 DEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRD--------TGKTMVD--------------- 142
Cdd:PRK00197 4 EYLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAANAKDlaaarangLSAAMLDrlllteariegiaeg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 143 ----ASL----GEIMttcekITWLLDEGekwLKPEYRSCgrsmlhkkakvefyPLGVIGAIvswnY---PfhNVfnpmLA 211
Cdd:PRK00197 84 lrqvAALpdpvGEVL-----DGWTLPNG---LRIGRVRV--------------PLGVIGVI----YesrP--NV----TV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 212 AIF-----SGNAAVIKVSEHASWSGCFYFRIIQAALAAVGAPDNLVHII--TGFAETGQ--ALVSSVDKIIFVGSPGVGR 282
Cdd:PRK00197 132 DAAalclkSGNAVILRGGSEAIHSNRALVAVIQEALEEAGLPADAVQLVetTDRAAVGEllKLDGYVDVIIPRGGAGLIR 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286994 283 MIMNRASdtlIPVTLELGGkdafiVC-----EDVDLPSVVQVAVRAALQSSGQnCAGAERFYVHKDIYSTFVSQVVK 354
Cdd:PRK00197 212 RVVENAT---VPVIEHGDG-----IChiyvdESADLDKALKIVLNAKTQRPSV-CNALETLLVHEAIAEEFLPKLAE 279
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
94-354 |
9.99e-06 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 48.20 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 94 QARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRD--------TGKTMVD-------------------ASL- 145
Cdd:cd07079 6 RAKAASRALATLSTEQKNAALLAIADALEANRDEILEANAKDlaaareagLSEALLDrllltperieamaeglrqvAALp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 146 ---GEIMTTcekitWLLDEGekwLKPEYRSCgrsmlhkkakvefyPLGVIGAIvswnY---PfhNVfnpmLA-----AIF 214
Cdd:cd07079 86 dpvGEVLRG-----WTLPNG---LQIEKVRV--------------PLGVIGII----YesrP--NV----TVdaaalCLK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 215 SGNAAVIKVSEHASWSGCFYFRIIQAALAAVGAPDNLVHII--TGFAETGQ--ALVSSVDKIIFVGSPGVGRMIMNRASd 290
Cdd:cd07079 134 SGNAVILRGGSEALHSNRALVEIIQEALEEAGLPEDAVQLIpdTDREAVQEllKLDDYIDLIIPRGGAGLIRFVVENAT- 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286994 291 tlIPVTLELGGkdafiVC-----EDVDLPSVVQVAVRAALQSSGQnCAGAERFYVHKDIYSTFVSQVVK 354
Cdd:cd07079 213 --IPVIKHGDG-----NChvyvdESADLEMAVRIVVNAKTQRPSV-CNALETLLVHRDIAEEFLPKLAE 273
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
188-280 |
2.81e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 46.72 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 188 PLGVIGAIVswnyPfhnVFNPMLAAIF-------SGNAAVI-------KVSEHASwsgcfyfRIIQAALAAVGAPDNLVH 253
Cdd:cd07122 95 PVGVIAALI----P---STNPTSTAIFkalialkTRNAIIFsphprakKCSIEAA-------KIMREAAVAAGAPEGLIQ 160
|
90 100 110
....*....|....*....|....*....|
gi 1002286994 254 IITGFA-ETGQALVSS--VDKIIFVGSPGV 280
Cdd:cd07122 161 WIEEPSiELTQELMKHpdVDLILATGGPGM 190
|
|
| ProA |
COG0014 |
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl ... |
86-354 |
3.33e-04 |
|
Gamma-glutamyl phosphate reductase [Amino acid transport and metabolism]; Gamma-glutamyl phosphate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 439785 Cd Length: 414 Bit Score: 43.45 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 86 DEVKEHVAQARKAQKIWAKSSFKQRRQFLRILLKYILEHQDLICEISSRD--------TGKTMVD--------------- 142
Cdd:COG0014 1 AYLEELGKRARAASRALATLSTAQKNAALLAMADALEANADEILAANAKDleaarengLSEALLDrlklteerieamaeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 143 ----ASL----GEIMttcekITWLLDEGekwLKPEYRSCgrsmlhkkakvefyPLGVIGAIvswnY---PfhNVfnpmLA 211
Cdd:COG0014 81 lrqvAALpdpvGEVL-----DGWTRPNG---LQIGRVRV--------------PLGVIGII----YesrP--NV----TV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 212 AIF-----SGNAAVIKVSEHASWSGCFYFRIIQAALAAVGAPDNLVHIITGF--AETGQ--ALVSSVDKIIFVGSPGVGR 282
Cdd:COG0014 129 DAAalclkSGNAVILRGGSEAIHSNRALVAVIQEALEEAGLPEDAVQLVPTTdrEAVGEllTLDGYIDVIIPRGGAGLIR 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286994 283 MIMNRASdtlIPVtLE-LGGkdafiVC-----EDVDLPSVVQVAVRAALQSSGQnCAGAERFYVHKDIYSTFVSQVVK 354
Cdd:COG0014 209 RVVENAT---VPV-IEhGDG-----NChvyvdASADLEMAVDIVVNAKTQRPGV-CNALETLLVHRDIAAEFLPRLAA 276
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
188-345 |
1.05e-03 |
|
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: 41.87 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 188 PLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALAAVGAPDNLVHIITGFA-ETGQALV 266
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSiELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 267 --SSVDKIIFVGSPGVgrmiMNRASDTLIPVTLELGGKDAFIVCEDVDLPSVVQVAVRAALQSSGQNCAGAERFYVHKDI 344
Cdd:cd07081 175 kfPGIGLLLATGGPAV----VKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSV 250
|
.
gi 1002286994 345 Y 345
Cdd:cd07081 251 Y 251
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
165-343 |
2.18e-03 |
|
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: 40.92 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 165 WLKPEYRscgRSMLHKKAKVEFYPLGVIGAIVSWNYPFHNVFNPMLAAIFSGNAAVIKVSEHASWSGCFYFRIIQAALAA 244
Cdd:cd07127 173 WEKPQGK---HDPLAMEKTFTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQVAREVLAE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286994 245 VGAPDNLVHII--TGFAETGQALVS--SVDKIIFVGSPGVGRMIMNRASDTLipVTLELGGKDAFIVCEDVDLPSVVQVA 320
Cdd:cd07127 250 AGFDPNLVTLAadTPEEPIAQTLATrpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNL 327
|
170 180
....*....|....*....|...
gi 1002286994 321 VRAALQSSGQNCAGAERFYVHKD 343
Cdd:cd07127 328 AFSLSLYSGQMCTTPQNIYVPRD 350
|
|
| |
