|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-496 |
0e+00 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 1077.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 1 MAGTGLFAEILDGEVYKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAEL 80
Cdd:PLN00412 1 MAGTGFFAEILDGDVYKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 81 LHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEGKFLLSDSFPGNDRTKYCLTSKIPLG 160
Cdd:PLN00412 81 LHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGKFLVSDSFPGNERNKYCLTSKIPLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 161 VVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNC 240
Cdd:PLN00412 161 VVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 241 ISFTGGDTGISISKKAGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKA 320
Cdd:PLN00412 241 ISFTGGDTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 321 KVAKLTVGPPEENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVL 400
Cdd:PLN00412 321 KVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 401 RINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTK 480
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTK 480
|
490
....*....|....*.
gi 15224111 481 VKTTVINLPTPSYSMG 496
Cdd:PLN00412 481 VKSTVINLPKPSYTMG 496
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
15-487 |
0e+00 |
|
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: 740.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 15 VYKYYADGEWKTSSsGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKT-PLWKRAELLHKAAAILKDNKA 93
Cdd:cd07082 1 QFKYLINGEWKESS-GKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 94 PMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRIlgEGKFLLSDSFPGNdRTKYCLTSKIPLGVVLAIPPFNYPVN 173
Cdd:cd07082 80 EVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRL--DGDSLPGDWFPGT-KGKIAQVRREPLGVVLAIGPFNYPLN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 174 LAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGD-TGISI 252
Cdd:cd07082 157 LTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTeVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 253 SKKAGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEE 332
Cdd:cd07082 237 KKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 333 NS-DITAVVSESSANFIEGLVMDAKEKGATFCQEYKRE-GNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGIN 410
Cdd:cd07082 317 NGvDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREgGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224111 411 HCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVIN 487
Cdd:cd07082 397 LANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
26-483 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 516.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 26 TSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAK 105
Cdd:pfam00171 2 VDSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 106 PAKDSVTEVVRSGDLISYCAEEGVRILGEgkfllsdSFPgNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIA 185
Cdd:pfam00171 82 PLAEARGEVDRAIDVLRYYAGLARRLDGE-------TLP-SDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 186 GNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQ 262
Cdd:pfam00171 154 GNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGStAVGRHIAEAAAqnLKRVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 263 MELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVS 341
Cdd:pfam00171 234 LELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPlDPDTDMGPLIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 342 ESSANFIEGLVMDAKEKGATFC---QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFG 418
Cdd:pfam00171 314 KAQLERVLKYVEDAKEEGAKLLtggEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15224111 419 LQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKT 483
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
16-488 |
8.80e-177 |
|
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: 505.05 E-value: 8.80e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPM 95
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 96 AESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEgkfllsdSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLA 175
Cdd:COG1012 86 AALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGE-------TIPSDAPGTRAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 176 VSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISK 254
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGStAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 255 KAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-E 331
Cdd:COG1012 239 AAAenLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPlD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 332 ENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR----EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEE 407
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRpdgeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 408 GINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVIN 487
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 15224111 488 L 488
Cdd:COG1012 479 L 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
56-486 |
1.07e-141 |
|
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: 413.91 E-value: 1.07e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 56 NAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEg 135
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 136 kfllSDSFPGNDRTKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPK 215
Cdd:cd07078 80 ----VIPSPDPGELAI--VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 216 GLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFS 292
Cdd:cd07078 154 GVLNVVTGDGDEVGAALASHPRVDKISFTGStAVGKAIMRAAAenLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 293 YSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKRE-- 369
Cdd:cd07078 234 NAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPlDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeg 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 370 --GNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINS 447
Cdd:cd07078 314 gkGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 15224111 448 APARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07078 394 YSVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-486 |
4.44e-138 |
|
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: 405.44 E-value: 4.44e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 37 NPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVR 116
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 117 SGDLISYCAEEGVRILGEGkfLLSDSFPGN-DRTKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPT 195
Cdd:cd07149 85 AIETLRLSAEEAKRLAGET--IPFDASPGGeGRIGF--TIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 196 QGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAGMIPLQMELGGKDACIVL 274
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSpAVGEAIARKAGLKKVTLELGSNAAVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 275 DDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLVM 353
Cdd:cd07149 241 ADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPlDEDTDVGPMISEAEAERIEEWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 354 DAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAIL 433
Cdd:cd07149 321 EAVEGGARLLTGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15224111 434 ISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07149 401 AARELEVGGVMINDSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
33-486 |
2.01e-135 |
|
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: 399.03 E-value: 2.01e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 33 VAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVT 112
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 113 EVVRSGDLISYCAEEgVRILgEGKFLLSDSFPGNDRtKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLK 192
Cdd:cd07145 81 EVERTIRLFKLAAEE-AKVL-RGETIPVDAYEYNER-RIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 193 PPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKD 269
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGStAVGLLIASKAGgtGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 270 ACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFI 348
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 349 EGLVMDAKEKGATFCQEYKR-EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKD 427
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRdEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15224111 428 INKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07145 398 INRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
35-486 |
7.87e-124 |
|
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: 369.00 E-value: 7.87e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKswaKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 VRSGDLISYCAEEGVRILGEgKFLLSDSFPGNDRTKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPP 194
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGE-SFSCDLTANGKARKIF--TLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 195 TQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAGMIPLQMELGGKDACIV 273
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGvAVGKAIAATAGYKRQLLELGGNDPLIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 274 LDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLV 352
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPmDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 353 MDAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAI 432
Cdd:cd07146 317 EEAIAQGARVLLGNQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIK 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15224111 433 LISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGS-QGVTNSINLMTKVKTTVI 486
Cdd:cd07146 397 RLVERLDVGTVNVNEVPGFRSELSPFGGVKDSGLGGkEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
33-486 |
3.93e-122 |
|
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: 364.83 E-value: 3.93e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 33 VAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVT 112
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 113 EVVRSGDLISYCAEEGVRILGEgkFLLSDSFPGNDrTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLK 192
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGE--EIPLDATQGSD-NRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 193 PPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAGMIPLQMELGGKDAC 271
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSaAVGEALRANAGGKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 272 IVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEG 350
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 351 LVMDAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINK 430
Cdd:cd07094 318 WVEEAVEAGARLLCGGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15224111 431 AILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07094 398 AFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
54-482 |
1.15e-120 |
|
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: 360.31 E-value: 1.15e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 54 EVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILG 133
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 134 EgkfLLSDSFPGndrtKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSC-LHMVHCFHLAG 212
Cdd:cd07104 81 E---ILPSDVPG----KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 213 FPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKG 289
Cdd:cd07104 154 LPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGStAVGRHIGELAGrhLKKVALELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 290 GFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR 368
Cdd:cd07104 234 AFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPrDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 369 EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSA 448
Cdd:cd07104 314 EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ 393
|
410 420 430
....*....|....*....|....*....|....
gi 15224111 449 PARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVK 482
Cdd:cd07104 394 TVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
19-467 |
2.88e-120 |
|
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: 360.43 E-value: 2.88e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAES 98
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 99 LVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRIlgEGKFLLSDSfPGndrtKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRI--EGEIIPSDR-PN----ENIFIFKVPIGVVAGILPWNFPFFLIARK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 179 IAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG 257
Cdd:cd07088 154 LAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGStEAGQKIMEAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 258 --MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENS 334
Cdd:cd07088 234 enITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPfDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 335 DITAVVSESSANFIEGLVMDAKEKGATFCQEYKR----EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGIN 410
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRpegeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15224111 411 HCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFpFQGLKDSGIG 467
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGF-HAGWKKSGLG 449
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
16-483 |
1.19e-119 |
|
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: 359.26 E-value: 1.19e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWKTSSSGKSVaiMNPA-TRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAP 94
Cdd:cd07097 1 YRNYIDGEWVAGGDGEEN--RNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 95 MAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEgkfllsdSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNL 174
Cdd:cd07097 79 LARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGE-------TLPSTRPGVEVETTREPLGVVGLITPWNFPIAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 175 AVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTG-GDTGISIS 253
Cdd:cd07097 152 PAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGsTAVGRRIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 254 KKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP- 330
Cdd:cd07097 232 AAAAarGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 331 EENSDITAVVSESSANFIEGLVMDAKEKGATFC---QEYKR--EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSV 405
Cdd:cd07097 312 DEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVyggERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 406 EEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINsAPARGPD-HFPFQGLKDSGIGS--QGvTNSINLMTKVK 482
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVN-LPTAGVDyHVPFGGRKGSSYGPreQG-EAALEFYTTIK 469
|
.
gi 15224111 483 T 483
Cdd:cd07097 470 T 470
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
35-470 |
2.63e-119 |
|
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: 357.51 E-value: 2.63e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 VRSGDLISYCAEEGVRILGegkfllsDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPP 194
Cdd:cd07103 81 DYAASFLEWFAEEARRIYG-------RTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 195 TQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKA--GMIPLQMELGGKDAC 271
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGStAVGKLLMAQAadTVKRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 272 IVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEG 350
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGlDEGTDMGPLINERAVEKVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 351 LVMDAKEKGATFCQEYKR---EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKD 427
Cdd:cd07103 314 LVEDAVAKGAKVLTGGKRlglGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15224111 428 INKAILISDAMETGTVQIN----SAPArgpdhFPFQGLKDSGIGSQG 470
Cdd:cd07103 394 LARAWRVAEALEAGMVGINtgliSDAE-----APFGGVKESGLGREG 435
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
62-486 |
7.18e-117 |
|
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: 348.45 E-value: 7.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 62 AKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGegkfllsD 141
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGG-------P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 142 SFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCI 221
Cdd:cd06534 76 ELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 222 TGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRC 298
Cdd:cd06534 156 PGGGDEVGAALLSHPRVDKISFTGStAVGKAIMKAAAenLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 299 TAVKVVLVMESVADELVEKVKAkvakltvgppeensditavvsessanfieglvmdakekgatfcqeykregnliwplLL 378
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLVT--------------------------------------------------------VL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 379 DNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFPF 458
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPF 339
|
410 420
....*....|....*....|....*...
gi 15224111 459 QGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd06534 340 GGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
35-486 |
9.48e-117 |
|
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: 351.16 E-value: 9.48e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 VRSGDLISYCAEEGVRILGEgkFLLSDSFPGNDrTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPP 194
Cdd:cd07147 83 ARAIDTFRIAAEEATRIYGE--VLPLDISARGE-GRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 195 TQGAVSCLHMVHCFHLAGFPKGLISCITGKgSEIGDFLTMHPAVNCISFTGGDT-GISISKKAGMIPLQMELGGKDACIV 273
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAvGWDLKARAGKKKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 274 LDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLV 352
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPkDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 353 MDAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAI 432
Cdd:cd07147 319 NEAVDAGAKLLTGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKAL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15224111 433 LISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07147 399 RAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
37-485 |
3.43e-113 |
|
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: 342.00 E-value: 3.43e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 37 NPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVR 116
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 117 SGDLISYCAEEGVRILGEgkFLLSDsFPGndrtKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQ 196
Cdd:cd07150 85 TPELLRAAAGECRRVRGE--TLPSD-SPG----TVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 197 GAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIV 273
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGStAVGREIAEKAGrhLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 274 LDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLV 352
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPrDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 353 MDAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAI 432
Cdd:cd07150 318 EDAVAKGAKLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15224111 433 LISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVK-TTV 485
Cdd:cd07150 398 KLAERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELKwITV 451
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
35-467 |
2.71e-111 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 336.81 E-value: 2.71e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 VRSGDLISYCAEegVRILGEgkfLLSDSFPGNDRTKYcltskIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPP 194
Cdd:cd07106 81 GGAVAWLRYTAS--LDLPDE---VIEDDDTRRVELRR-----KPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 195 TQGAVSCLHMVHcfhLAG--FPKGLISCITGkGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKD 269
Cdd:cd07106 151 PFTPLCTLKLGE---LAQevLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGStATGKKVMASAAktLKRVTLELGGND 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 270 ACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFI 348
Cdd:cd07106 227 AAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGlDPGTTLGPVQNKMQYDKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 349 EGLVMDAKEKGATFC---QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFT 425
Cdd:cd07106 307 KELVEDAKAKGAKVLaggEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15224111 426 KDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIG 467
Cdd:cd07106 387 SDLERAEAVARRLEAGTVWINTHGALDP-DAPFGGHKQSGIG 427
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
19-487 |
7.29e-108 |
|
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: 329.31 E-value: 7.29e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPA-TRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAE 97
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 98 SLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEgkfllsdSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVS 177
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGE-------TVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 178 KIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKA 256
Cdd:cd07131 155 KIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGStEVGERIGETC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 257 G--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EEN 333
Cdd:cd07131 235 ArpNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGlDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 334 SDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVE 406
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltgggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 407 EGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINsAPARGPD-HFPFQGLKDSGIGS-QGVTNSINLMTKVKTT 484
Cdd:cd07131 395 EAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN-APTIGAEvHLPFGGVKKSGNGHrEAGTTALDAFTEWKAV 473
|
...
gi 15224111 485 VIN 487
Cdd:cd07131 474 YVD 476
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
22-467 |
1.53e-104 |
|
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: 320.02 E-value: 1.53e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 22 GEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVK 101
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 102 EIAKPAKDSVTEVVRSGDLISYCAEEGVRIlgEGKFLLSDSfPGNDRTKYcltsKIPLGVVLAIPPFNYPVNLAVSKIAP 181
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRM--EGRILPSDV-PGKENRVY----REPLGVVGVISPWNFPLHLSMRSVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 182 ALIAGNSLVLKPPTQGAVSC-LHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG-- 257
Cdd:cd07151 154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGStPVGRHIGELAGrh 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 258 MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVG-PPEENSDI 336
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGdPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 337 TAVVSESSANFIEGLVMDAKEKGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASN 416
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15224111 417 FGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIG 467
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLG 444
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
37-486 |
4.63e-102 |
|
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: 313.33 E-value: 4.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 37 NPATRKTQYKVQACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 VRSGDLISYCAeeGVRILGEGKFLlsdsfPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPP 194
Cdd:cd07114 83 RYLAEWYRYYA--GLADKIEGAVI-----PVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 195 TQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGD-TGISISKKAG--MIPLQMELGGKDAC 271
Cdd:cd07114 156 EHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTeTGRHIARAAAenLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 272 IVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEG 350
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPlDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 351 LVMDAKEKGATFCQEYKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCV 423
Cdd:cd07114 316 YVARAREEGARVLTGGERpsgadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224111 424 FTKDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07114 396 WTRDLARAHRVARAIEAGTVWVNTYRALSP-SSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
37-470 |
9.48e-102 |
|
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: 314.55 E-value: 9.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 37 NPA-TRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVV 115
Cdd:cd07124 52 NPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 116 RSGDLISYCAEEGVRILGEGKfllsDSFPGNDrTKYCLtskIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPT 195
Cdd:cd07124 132 EAIDFLEYYAREMLRLRGFPV----EMVPGED-NRYVY---RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 196 QGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAGMI-PLQ-------MELG 266
Cdd:cd07124 204 DTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSrEVGLRIYERAAKVqPGQkwlkrviAEMG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 267 GKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENS-DITAVVSESSA 345
Cdd:cd07124 284 GKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEvYMGPVIDKGAR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 346 NFIEGLVMDAKEKGATFCQ----EYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQG 421
Cdd:cd07124 364 DRIRRYIEIGKSEGRLLLGgevlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTG 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15224111 422 CVFTKDINKAILISDAMETGTVQINsapaRG-----PDHFPFQGLKDSGIGSQG 470
Cdd:cd07124 444 GVFSRSPEHLERARREFEVGNLYAN----RKitgalVGRQPFGGFKMSGTGSKA 493
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
16-486 |
2.30e-97 |
|
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: 301.82 E-value: 2.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKA 93
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAfeTGWWRKMDPRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 94 PMA--ESLV--KEIAKPAKDSVTEVVRSgdlISYCAEEGVRILGEgkfllsdSFPGNDRtKYCLTSKIPLGVVLAIPPFN 169
Cdd:cd07091 84 ELAalESLDngKPLEESAKGDVALSIKC---LRYYAGWADKIQGK-------TIPIDGN-FLAYTRREPIGVCGQIIPWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 170 YPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DT 248
Cdd:cd07091 153 FPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGStAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 249 GISISKKAGMIPLQ---MELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKL 325
Cdd:cd07091 233 GRTIMEAAAKSNLKkvtLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 326 TVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGAT-FC--QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLR 401
Cdd:cd07091 313 VVGDPfDPDTFQGPQVSKAQFDKILSYIESGKKEGATlLTggERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 402 INSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGVTNSINLMTKV 481
Cdd:cd07091 393 FKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDA-AVPFGGFKQSGFGRELGEEGLEEYTQV 471
|
....*
gi 15224111 482 KTTVI 486
Cdd:cd07091 472 KAVTI 476
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
37-486 |
5.59e-97 |
|
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: 300.25 E-value: 5.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 37 NPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVR 116
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 117 SG--------DLISYCAEEgvrilgegkfllsdSFPgNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNS 188
Cdd:cd07093 83 RAaanfrffaDYILQLDGE--------------SYP-QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 189 LVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKA--GMIPLQMEL 265
Cdd:cd07093 148 VVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGEtATGRTIMRAAapNLKPVSLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 266 GGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESS 344
Cdd:cd07093 228 GGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPlDPDTEVGPLISKEH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 345 ANFIEGLVMDAKEKGATFC-------QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNF 417
Cdd:cd07093 308 LEKVLGYVELARAEGATILtgggrpeLPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPY 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 418 GLQGCVFTKDINKAILISDAMETGTVQINSAPARgpD-HFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07093 388 GLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVR--DlRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
36-486 |
5.76e-97 |
|
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: 300.29 E-value: 5.76e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 36 MNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVV 115
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 116 RSGDLISYCAEEGVRILGEGKFLLSDSFPGndrtKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPT 195
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVPTGLLMPN----KKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 196 QGAVSCLHMVHCFHLAGFPKGLISCITGKGsEIGDFLTMHPaVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACI 272
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDAG-VDKVAFTGSvATGRKVMAAAAerLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 273 VLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPE-ENSDITAVVSESSANFIEGL 351
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDiGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 352 VMDAKEKGATFCQEYKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDI 428
Cdd:cd07099 315 VDDAVAKGAKALTGGARSnggGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15224111 429 NKAILISDAMETGTVQINSAPARGPDH-FPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDVLLTAGIPaLPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
55-467 |
5.93e-97 |
|
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: 299.38 E-value: 5.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 55 VNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVrilge 134
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 135 gKFLLSDSFPGNDRTKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFP 214
Cdd:cd07100 76 -AFLADEPIETDAGKAY--VRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 215 KGLISCITGKGSEIGDFLTmHPAVNCISFTGGDT-GISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGF 291
Cdd:cd07100 153 EGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERaGRAVAAEAGknLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 292 SYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATF---CQEYK 367
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPmDEDTDLGPLARKDLRDELHEQVEEAVAAGATLllgGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 368 REGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINS 447
Cdd:cd07100 312 GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING 391
|
410 420
....*....|....*....|
gi 15224111 448 APARGPDhFPFQGLKDSGIG 467
Cdd:cd07100 392 MVKSDPR-LPFGGVKRSGYG 410
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
17-483 |
3.21e-96 |
|
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: 299.05 E-value: 3.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 17 KYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMA 96
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 97 ESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEGkflLSDSFPGNDrtkyCLTSKIPLGVVLAIPPFNYPVNLAV 176
Cdd:cd07085 82 RLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEY---LENVARGID----TYSYRQPLGVVAGITPFNFPAMIPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 177 SKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGkGSEIGDFLTMHPAVNCISFTGGD--------T 248
Cdd:cd07085 155 WMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTpvgeyiyeR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 249 GISISKKAgmiplQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVG 328
Cdd:cd07085 234 AAANGKRV-----QALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 329 PP-EENSDITAVVSESSANFIEGLVMDAKEKGAT--------FCQEYKrEGNLIWPLLLDNVRPDMRIAWEEPFGPVVPV 399
Cdd:cd07085 309 AGdDPGADMGPVISPAAKERIEGLIESGVEEGAKlvldgrgvKVPGYE-NGNFVGPTILDNVTPDMKIYKEEIFGPVLSI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 400 LRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQIN-SAPARGPdHFPFQGLKDSGIGSQGVT--NSIN 476
Cdd:cd07085 388 VRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINvPIPVPLA-FFSFGGWKGSFFGDLHFYgkDGVR 466
|
....*..
gi 15224111 477 LMTKVKT 483
Cdd:cd07085 467 FYTQTKT 473
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
54-483 |
7.92e-96 |
|
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: 296.41 E-value: 7.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 54 EVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILG 133
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 134 EgkfllsdSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLK-----PPTQGAVsclhmVHCF 208
Cdd:cd07105 81 G-------SIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKaselsPRTHWLI-----GRVF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 209 HLAGFPKGLISCITGK---GSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLV 282
Cdd:cd07105 149 HEAGLPKGVLNVVTHSpedAPEVVEALIAHPAVRKVNFTGStRVGRIIAETAAkhLKPVLLELGGKAPAIVLEDADLDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 283 ASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPpeenSDITAVVSESSANFIEGLVMDAKEKGATF 362
Cdd:cd07105 229 ANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP----VVLGSLVSAAAADRVKELVDDALSKGAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 363 C----QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAM 438
Cdd:cd07105 305 VvgglADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRI 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 15224111 439 ETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKT 483
Cdd:cd07105 385 ESGAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKW 429
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
35-486 |
1.83e-95 |
|
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: 296.45 E-value: 1.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWA-KTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTE 113
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 114 VVRSGDLISYCAEEGVRILGEgkfllsdSFP-GNDRTKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLK 192
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGE-------TIPlGPGYFVY--TVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 193 PPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKD 269
Cdd:cd07109 152 PAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSvETGIAVMRAAAenVVPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 270 ACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIE 349
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 350 GLVMDAKEKGA------TFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCV 423
Cdd:cd07109 312 GFVARARARGArivaggRIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224111 424 FTKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
18-467 |
2.76e-93 |
|
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: 290.94 E-value: 2.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 18 YYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAE 97
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 98 SLVKEIAKPAKDSVTEVVRSGDLIsycAEEGVRILGEGKFllsDSFPGNDrtkycLTSKIPLGVVLAIPPFNYPVNLAVS 177
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGH---LRAAADALKDFEF---EERRGNS-----LVVREPIGVCGLITPWNWPLNQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 178 KIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTG-GDTGISISKKA 256
Cdd:cd07138 150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGsTRAGKRVAEAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 257 G--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EEN 333
Cdd:cd07138 230 AdtVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPrDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 334 SDITAVVSESSANFIEGLVMDAKEKGATFCQ------EYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEE 407
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAggpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 408 GINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGpdHFPFQGLKDSGIG 467
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP--GAPFGGYKQSGNG 447
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
16-488 |
8.91e-93 |
|
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: 290.12 E-value: 8.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPM 95
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 96 AESLVKEIAKPAKDSVT-EVVRSGDLISYCAeeGVrILGEgkfllSDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNL 174
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRYFA--GV-IRAE-----EGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 175 AVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAgFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-----DTG 249
Cdd:cd07117 153 AAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGStevgrDVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 250 ISISKKagMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGP 329
Cdd:cd07117 232 IAAAKK--LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 330 P-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLR 401
Cdd:cd07117 310 PlDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltengldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 402 INSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGVTNSINLMTKV 481
Cdd:cd07117 390 FKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTY-NQIPAGAPFGGYKKSGIGRETHKSMLDAYTQM 468
|
....*..
gi 15224111 482 KTTVINL 488
Cdd:cd07117 469 KNIYIDL 475
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
51-479 |
1.05e-92 |
|
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: 288.81 E-value: 1.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 51 TQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEI-AKPAKDSVtEVVRSGDLISYCAEEGV 129
Cdd:cd07152 11 DAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESgSIRPKAGF-EVGAAIGELHEAAGLPT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 130 RILGEgkfLLSdSFPGndRTKYCltSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMV-HCF 208
Cdd:cd07152 90 QPQGE---ILP-SAPG--RLSLA--RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 209 HLAGFPKGLISCITGkGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASN 285
Cdd:cd07152 162 EEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGStAVGRKVGEAAGrhLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 286 IIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQ 364
Cdd:cd07152 241 GAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPaTGQVALGPLINARQLDRVHAIVDDSVAAGARLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 365 EYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQ 444
Cdd:cd07152 321 GGTYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLH 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 15224111 445 INSAPARGPDHFPFQGLKDSGIGSQ-GVTNSINLMT 479
Cdd:cd07152 401 INDQTVNDEPHNPFGGMGASGNGSRfGGPANWEEFT 436
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
37-468 |
1.25e-92 |
|
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: 289.15 E-value: 1.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 37 NPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVR 116
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 117 SGDLISYCAEEGVRILGEGKFLLSDSFpgndrTKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQ 196
Cdd:cd07102 82 MLERARYMISIAEEALADIRVPEKDGF-----ERY--IRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 197 GAVSCLHMVHCFHLAGFPKGLISCITGKGsEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIV 273
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSH-ETSAALIADPRIDHVSFTGSvAGGRAIQRAAAgrFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 274 LDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVG-PPEENSDITAVVSESSANFIEGLV 352
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGdPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 353 MDAKEKGATFC------QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTK 426
Cdd:cd07102 314 ADAIAKGARALidgalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15224111 427 DINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGS 468
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPA-LAWTGVKDSGRGV 434
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
35-488 |
1.29e-92 |
|
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: 289.20 E-value: 1.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 VRSGDLISYCAEEGVRILGEgkfllsdSFP-GNDRTKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKP 193
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGE-------HVPlPGGSFAY--TRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 194 PTQGAVSCLHMVHCFHLAGFPKGLISCITGkGSEIGDFLTMHPAVNCISFTGG-DTGISISKKA--GMIPLQMELGGKDA 270
Cdd:cd07090 152 SPFTPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSvPTGKKVMSAAakGIKHVTLELGGKSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 271 CIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIE 349
Cdd:cd07090 231 LIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPlDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 350 GLVMDAKEKGATF-C-------QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQG 421
Cdd:cd07090 311 GYIESAKQEGAKVlCggervvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 422 CVFTKDINKAILISDAMETGTVQINS---APArgpdHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVINL 488
Cdd:cd07090 391 GVFTRDLQRAHRVIAQLQAGTCWINTyniSPV----EVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEM 456
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
21-470 |
7.94e-92 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 288.51 E-value: 7.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 21 DGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLV 100
Cdd:PLN02278 30 GGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 101 KEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGegkfllsDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIA 180
Cdd:PLN02278 110 LEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYG-------DIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 181 PALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGD-TGISISKKAG-- 257
Cdd:PLN02278 183 PALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTaVGKKLMAGAAat 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 258 MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDI 336
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGfEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 337 TAVVSESSANFIEGLVMDAKEKGATFCQEYKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCN 413
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHslgGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224111 414 ASNFGLQGCVFTKDINKAILISDAMETGTVQIN-----SAPArgpdhfPFQGLKDSGIGSQG 470
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNeglisTEVA------PFGGVKQSGLGREG 478
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
19-470 |
1.22e-91 |
|
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: 287.16 E-value: 1.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKAPMA 96
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 97 ESLVKEIAKPAKDSVT-EVVRSGDLISYCAEegvrilgegkflLSDSFPGNDR-----TKYCLTSKIPLGVVLAIPPFNY 170
Cdd:cd07139 82 RLWTAENGMPISWSRRaQGPGPAALLRYYAA------------LARDFPFEERrpgsgGGHVLVRREPVGVVAAIVPWNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 171 PVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGkGSEIGDFLTMHPAVNCISFTGGD-TG 249
Cdd:cd07139 150 PLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTaAG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 250 ISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTV 327
Cdd:cd07139 229 RRIAAVCGerLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 328 GPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR-----EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLR 401
Cdd:cd07139 309 GDPlDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpagldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIP 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 402 INSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAparGPD-HFPFQGLKDSGIGSQG 470
Cdd:cd07139 389 YDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF---RLDfGAPFGGFKQSGIGREG 455
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
13-431 |
6.99e-91 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 286.45 E-value: 6.99e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 13 GEVYKYYADGEWKTSSsGKSVAImNPA-TRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDN 91
Cdd:PRK03137 34 GQDYPLIIGGERITTE-DKIVSI-NPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 92 KAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRiLGEGKFLLSdsFPGND-RTKYcltskIPLGVVLAIPPFNY 170
Cdd:PRK03137 112 KHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKPVES--RPGEHnRYFY-----IPLGVGVVISPWNF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 171 PVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTG 249
Cdd:PRK03137 184 PFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSrEVG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 250 ISISKKAGMI-PLQ-------MELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAK 321
Cdd:PRK03137 264 LRIYERAAKVqPGQiwlkrviAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 322 VAKLTVGPPEENSDITAVVSESSANFIEGLVMDAKEKGATFC--QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPV 399
Cdd:PRK03137 344 TKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLggEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAF 423
|
410 420 430
....*....|....*....|....*....|....*
gi 15224111 400 LRINSVEEGINHCNASNFGLQGCVFTKD---INKA 431
Cdd:PRK03137 424 IKAKDFDHALEIANNTEYGLTGAVISNNrehLEKA 458
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
19-488 |
1.62e-89 |
|
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: 281.99 E-value: 1.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKS-WAKTPLWKRAELLHKAAAILKDNKAPMAE 97
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 98 SLVKEIAKP----AKDSVTEVVrsgDLISYCAEEGVRILGEgkfllsdSFPgNDRTKYCLTSKIPLGVVLAIPPFNYPVN 173
Cdd:cd07144 91 IEALDSGKPyhsnALGDLDEII---AVIRYYAGWADKIQGK-------TIP-TSPNKLAYTLHEPYGVCGQIIPWNYPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 174 LAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISI 252
Cdd:cd07144 160 MAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGStATGRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 253 SKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAK-LTVGP 329
Cdd:cd07144 240 MKAAAqnLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 330 P-EENSDITAVVSESSANFIEGLVMDAKEKGA------TFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRI 402
Cdd:cd07144 320 PfDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAklvyggEKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 403 NSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGVTNSINLMTKVK 482
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV-GVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
....*.
gi 15224111 483 TTVINL 488
Cdd:cd07144 479 AVHINL 484
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
35-486 |
2.02e-89 |
|
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: 280.79 E-value: 2.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAK-DSVTE 113
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 114 VVRSGDLISYCAEEGVRILGEgkfllsdSFPGNDRTkYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKP 193
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGE-------TLPFGPDV-LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 194 PTQGAVSCLHMVHCFHlAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDA 270
Cdd:cd07108 153 AEDAPLAVLLLAEILA-QVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGStEVGKIIYRAAAdrLIPVSLELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 271 CIVLDDADLDLVASNIIKG-GFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFI 348
Cdd:cd07108 232 MIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 349 EGLVMDAKE-KGAT--FCQEYKREGNL-----IWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQ 420
Cdd:cd07108 312 CGYIDLGLStSGATvlRGGPLPGEGPLadgffVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224111 421 GCVFTKDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGVTNS-INLMTKVKTTVI 486
Cdd:cd07108 392 AYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPG-QSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
19-491 |
5.18e-88 |
|
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: 278.04 E-value: 5.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKAPMA 96
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 97 ESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEgkfllsdSFPGNDRTKyCLTSKIPLGVVLAIPPFNYPVNLAV 176
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGE-------VYDVPPHVI-SRTVREPVGVCGLITPWNYPLLQAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 177 SKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKK 255
Cdd:cd07119 153 WKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGtATGRSIMRA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 256 AG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPE-E 332
Cdd:cd07119 233 AAgnVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLdA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 333 NSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSV 405
Cdd:cd07119 313 DTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRptgdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 406 EEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIGSQGVTNSINLMTKVKTTV 485
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEA-PWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
....*..
gi 15224111 486 INL-PTP 491
Cdd:cd07119 472 INLsPQP 478
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
35-470 |
1.77e-85 |
|
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: 270.65 E-value: 1.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWA-KTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAkdSVTE 113
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPV--MTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 114 ---VVRSGDLISYCAEEgvrilgEGKFLLSDSFPGNDRTKYCLTSKI---PLGVVLAIPPFNYPVNLAVSKIAPALIAGN 187
Cdd:cd07089 79 amqVDGPIGHLRYFADL------ADSFPWEFDLPVPALRGGPGRRVVrrePVGVVAAITPWNFPFFLNLAKLAPALAAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 188 SLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGD-TGISISKKAG--MIPLQME 264
Cdd:cd07089 153 TVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTaVGRRIMAQAAatLKRVLLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 265 LGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENSDITA-VVSES 343
Cdd:cd07089 233 LGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGpLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 344 SANFIEGLVMDAKEKGATFCQEYKREGNL-----IWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFG 418
Cdd:cd07089 313 QRDRVEGYIARGRDEGARLVTGGGRPAGLdkgfyVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYG 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15224111 419 LQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIGSQG 470
Cdd:cd07089 393 LSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDA-PFGGYKQSGLGREN 443
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
19-487 |
2.81e-85 |
|
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: 270.97 E-value: 2.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWkTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAES 98
Cdd:cd07086 2 VIGGEW-VGSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 99 LVKEIAKPAKDSVTEVVRSGDLISYCAeegvrilGEGKFLLSDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVnlAVS- 177
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAV-------GLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPV--AVPg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 178 -KIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLA----GFPKGLISCITGkGSEIGDFLTMHPAVNCISFTGG-----D 247
Cdd:cd07086 152 wNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGStevgrR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 248 TGISISKKAGMIPLqmELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTV 327
Cdd:cd07086 231 VGETVARRFGRVLL--ELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 328 GPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR-----EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLR 401
Cdd:cd07086 309 GDPlDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRidggePGNYVEPTIVTGVTDDARIVQEETFAPILYVIK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 402 INSVEEGINHCNASNFGLQGCVFTKDINKAILISDAM--ETGTVQINsAPARGPD-HFPFQGLKDSGIGSQGVTNSINLM 478
Cdd:cd07086 389 FDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVN-IPTSGAEiGGAFGGEKETGGGRESGSDAWKQY 467
|
....*....
gi 15224111 479 TKVKTTVIN 487
Cdd:cd07086 468 MRRSTCTIN 476
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
30-486 |
7.52e-85 |
|
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: 269.09 E-value: 7.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 30 GKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKS--WAKTPLWKRAELLHKAAAILKDNKAPMA--ESLvkEIAK 105
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELAllETL--DMGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 106 PAKDSVTEVVRSG-DLISYCAEEGVRILGEgkfllsdSFP-GNDRTKycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPAL 183
Cdd:cd07112 79 PISDALAVDVPSAaNTFRWYAEAIDKVYGE-------VAPtGPDALA--LITREPLGVVGAVVPWNFPLLMAAWKIAPAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 184 IAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTG-GDTGISISKKAG---MI 259
Cdd:cd07112 150 AAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGsTEVGRRFLEYSGqsnLK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 260 PLQMELGGKDACIVLDDA-DLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDIT 337
Cdd:cd07112 230 RVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPlDPATRMG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 338 AVVSESSANFIEGLVMDAKEKGATFCQEYKRE-----GNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHC 412
Cdd:cd07112 310 ALVSEAHFDKVLGYIESGKAEGARLVAGGKRVltetgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224111 413 NASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPArGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07112 390 NDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDE-GDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
19-488 |
1.15e-84 |
|
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: 269.40 E-value: 1.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA-QKSWA-KTPLWKRAELLHKAAAILKDNKAPMA 96
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 97 --ESLVKEIAKPAKDSVtEVVRSGDLISYCAEEGVRILGEgkfllsdsFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNL 174
Cdd:cd07143 90 siEALDNGKTFGTAKRV-DVQASADTFRYYGGWADKIHGQ--------VIETDIKKLTYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 175 AVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTG----GDTGI 250
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGstlvGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 251 SISKKAGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP 330
Cdd:cd07143 241 EAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 331 -EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKREGNL---IWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVE 406
Cdd:cd07143 321 fAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEgyfIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 407 EGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHH-QVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
..
gi 15224111 487 NL 488
Cdd:cd07143 480 NL 481
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
14-483 |
1.49e-84 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 269.06 E-value: 1.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 14 EVYKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKA 93
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 94 PMAESLVKEIAKP-AKDSVTEVVRSGDLISYCAEEGVRILGEGKFLLSDSFpgndrtKYclTSKIPLGVVLAIPPFNYPV 172
Cdd:PRK13252 85 ELAALETLDTGKPiQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSF------VY--TRREPLGVCAGIGAWNYPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 173 NLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGsEIGDFLTMHPAVNCISFTGG-DTGis 251
Cdd:PRK13252 157 QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGvPTG-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 252 isKK------AGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKL 325
Cdd:PRK13252 234 --KKvmaaaaASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 326 TVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVV 397
Cdd:PRK13252 312 RIGDPmDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERlteggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 398 PVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINS---APARgpdhFPFQGLKDSGIGSQGVTNS 474
Cdd:PRK13252 392 SVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgeSPAE----MPVGGYKQSGIGRENGIAT 467
|
....*....
gi 15224111 475 INLMTKVKT 483
Cdd:PRK13252 468 LEHYTQIKS 476
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
16-488 |
1.73e-84 |
|
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: 268.83 E-value: 1.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKA-- 93
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 94 PMAESLvkEIAKPAKDSVT-EVVRSGDLISYCAeeGVrILGEgkfllSDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPV 172
Cdd:cd07559 81 AVAETL--DNGKPIRETLAaDIPLAIDHFRYFA--GV-IRAQ-----EGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 173 NLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCF-HLagFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGI 250
Cdd:cd07559 151 LMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIgDL--LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGStTVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 251 SISKKAG--MIPLQMELGGKDACIVLDDA-----DLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVA 323
Cdd:cd07559 229 LIMQYAAenLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 324 KLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGP 395
Cdd:cd07559 309 AIKVGNPlDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERltlggldKGYFYEPTLIKGGNNDMRIFQEEIFGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 396 VVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARgPDHFPFQGLKDSGIGSQGVTNSI 475
Cdd:cd07559 389 VLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQY-PAHAPFGGYKKSGIGRETHKMML 467
|
490
....*....|...
gi 15224111 476 NLMTKVKTTVINL 488
Cdd:cd07559 468 DHYQQTKNILVSY 480
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
17-486 |
1.71e-83 |
|
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: 266.14 E-value: 1.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 17 KYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQK---SWAKTPLWKRAELLHKAAAILKDNKA 93
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 94 PMA--ESLvkEIAKP-AKDSVTEVVRSGDLISYCAEEGVRILGE-----GKFllsdsfpgndrtkYCLTSKIPLGVVLAI 165
Cdd:cd07141 88 YLAslETL--DNGKPfSKSYLVDLPGAIKVLRYYAGWADKIHGKtipmdGDF-------------FTYTRHEPVGVCGQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 166 PPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTG 245
Cdd:cd07141 153 IPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 246 G-DTGISISKKAGMIPLQ---MELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAK 321
Cdd:cd07141 233 StEVGKLIQQAAGKSNLKrvtLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 322 VAKLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKREGN---LIWPLLLDNVRPDMRIAWEEPFGPVV 397
Cdd:cd07141 313 AKKRVVGNPfDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDkgyFIQPTVFSDVTDDMRIAKEEIFGPVQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 398 PVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGVTNSINL 477
Cdd:cd07141 393 QIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSP-QAPFGGYKMSGNGRELGEYGLQE 471
|
....*....
gi 15224111 478 MTKVKTTVI 486
Cdd:cd07141 472 YTEVKTVTI 480
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
35-488 |
2.00e-83 |
|
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: 265.39 E-value: 2.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 VRSGDLISYCAEEGVRILGEgkfllsdSFPGNDRTKYcLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPP 194
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGE-------TIPVGGRNLH-YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 195 TQGAVSCLHMVHcfhLAG--FPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKA--GMIPLQMELGGKD 269
Cdd:cd07107 153 EQAPLSALRLAE---LARevLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSvPTGRAIMRAAaeGIKHVTLELGGKN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 270 ACIVLDDADLDLVASNIIKG-GFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANF 347
Cdd:cd07107 230 ALIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPtDPATTMGPLVSRQQYDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 348 IEGLVMDAKEKGATFCQEYKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQ 420
Cdd:cd07107 310 VMHYIDSAKREGARLVTGGGRpegpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLT 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224111 421 GCVFTKDINKAILISDAMETGTVQINSaparGPDHF---PFQGLKDSGIGSQGVTNSINLMTKVKTTVINL 488
Cdd:cd07107 390 AAIWTNDISQAHRTARRVEAGYVWING----SSRHFlgaPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
35-488 |
2.61e-83 |
|
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: 265.07 E-value: 2.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSV-TE 113
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 114 VVRSGDLISYCAEEGVRILGE-----GKFLlsdsfpgndrtKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNS 188
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEvipvrGPFL-----------NY--TVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 189 LVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG--MIPLQMEL 265
Cdd:cd07115 148 VVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGStAVGRKIMQGAAgnLKRVSLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 266 GGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESS 344
Cdd:cd07115 228 GGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPlDPKTQMGPLVSQAQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 345 ANFIEGLVMDAKEKGATFCQEYKRE---GNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQG 421
Cdd:cd07115 308 FDRVLDYVDVGREEGARLLTGGKRPgarGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224111 422 CVFTKDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGVTNSINLMTKVKTTVINL 488
Cdd:cd07115 388 GVWTRDLGRAHRVAAALKAGTVWINTYNRFDPG-SPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
26-467 |
3.00e-82 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 264.43 E-value: 3.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 26 TSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAK 105
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 106 PAKDSVTEVVRSGDLISYCAEEGVRILGEGKflLSDSFPGNDRTKyclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIA 185
Cdd:PRK09407 107 ARRHAFEEVLDVALTARYYARRAPKLLAPRR--RAGALPVLTKTT---ELRQPKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 186 GNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHpaVNCISFTGGD-TGISISKKAG--MIPLQ 262
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTaTGRVLAEQAGrrLIGFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 263 MELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVS 341
Cdd:PRK09407 260 LELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGyDYSADMGSLIS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 342 ESSANFIEGLVMDAKEKGAT-------------FCQEykregnliwPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEG 408
Cdd:PRK09407 340 EAQLETVSAHVDDAVAKGATvlaggkarpdlgpLFYE---------PTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224111 409 INHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINS--APARGPDHFPFQGLKDSGIG 467
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgyAAAWGSVDAPMGGMKDSGLG 471
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
19-486 |
9.07e-82 |
|
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: 261.61 E-value: 9.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKS-WAKTPLWKRAELLHKAAAILKDNKAPMA- 96
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 97 -ESLV--KEIAKpakDSVTEVVRSGDLISYCAEEGVRILGEgkfLLSDSFPGNDRTKY-CLTSKIPLGVVLAIPPFNYPV 172
Cdd:cd07113 83 lETLCsgKSIHL---SRAFEVGQSANFLRYFAGWATKINGE---TLAPSIPSMQGERYtAFTRREPVGVVAGIVPWNFSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 173 NLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGsEIGDFLTMHPAVNCISFTGG-DTGIS 251
Cdd:cd07113 157 MIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSvATGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 252 ISKKA--GMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGP 329
Cdd:cd07113 236 IGRQAasDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 330 P-EENSDITAVVSESSANFIEGLVMDAKEKGATFC---QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSV 405
Cdd:cd07113 316 PmDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVrggEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 406 EEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGVTNSINLMTKVKTTV 485
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPA-VPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
.
gi 15224111 486 I 486
Cdd:cd07113 475 I 475
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
38-467 |
1.37e-81 |
|
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: 260.32 E-value: 1.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 38 PATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRS 117
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 118 GDLISYCAEEGVRILGEGKflLSDSFPGNDRTKYCltsKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQG 197
Cdd:cd07101 83 AIVARYYARRAERLLKPRR--RRGAIPVLTRTTVN---RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 198 AVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHpaVNCISFTGGD-TGISISKKAG--MIPLQMELGGKDACIVL 274
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTaTGRVVAERAGrrLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 275 DDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENS-DITAVVSESSANFIEGLVM 353
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGpDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 354 DAKEKGAT-FCQEYKRE--GNLIW-PLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDIN 429
Cdd:cd07101 316 DAVAKGATvLAGGRARPdlGPYFYePTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15224111 430 KAILISDAMETGTVQINS--APARGPDHFPFQGLKDSGIG 467
Cdd:cd07101 396 RGRRIAARLRAGTVNVNEgyAAAWASIDAPMGGMKDSGLG 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
35-467 |
9.40e-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: 255.74 E-value: 9.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 vrsGDLIS---YCAE--EGVRILGEGKFLL-SDSFPGNDRtkycltsKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNS 188
Cdd:cd07110 81 ---DDVAGcfeYYADlaEQLDAKAERAVPLpSEDFKARVR-------REPVGVVGLITPWNFPLLMAAWKVAPALAAGCT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 189 LVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGD-TGISISKKA--GMIPLQMEL 265
Cdd:cd07110 151 VVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTaTGSQVMQAAaqDIKPVSLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 266 GGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESS 344
Cdd:cd07110 231 GGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPlEEGVRLGPLVSQAQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 345 ANFIEGLVMDAKEKGATFCQEYKR-----EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGL 419
Cdd:cd07110 311 YEKVLSFIARGKEEGARLLCGGRRpahleKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15224111 420 QGCVFTKDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIG 467
Cdd:cd07110 391 AAAVISRDAERCDRVAEALEAGIVWINCSQPCFP-QAPWGGYKRSGIG 437
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-467 |
2.59e-79 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 256.20 E-value: 2.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA-----QKSWAKTPLWKRAELLHKAAAILKDNKA 93
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 94 PMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEGKFLLS---DSFPGNDRtkycltsKIPLGVVLAIPPFNY 170
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSlpmETFKGYVL-------KEPLGVVGLITPWNY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 171 PVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTG 249
Cdd:PLN02467 164 PLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGStATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 250 ISI-SKKAGMI-PLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTV 327
Cdd:PLN02467 244 RKImTAAAQMVkPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 328 GPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKR-----EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLR 401
Cdd:PLN02467 324 SDPlEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRpehlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224111 402 INSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQIN-SAPARgpDHFPFQGLKDSGIG 467
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINcSQPCF--CQAPWGGIKRSGFG 468
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
37-467 |
7.84e-79 |
|
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: 253.76 E-value: 7.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 37 NPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKD-SVTEVV 115
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDaSLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 116 RSGDLISYCAEEGVRILGEgkfllsDSFPGNDRTKYcLTSKI---PLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLK 192
Cdd:cd07098 82 VTCEKIRWTLKHGEKALRP------ESRPGGLLMFY-KRARVeyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 193 PPTQGAVSC---LHMVH-CFHLAGFPKGLISCITGKGsEIGDFLTMHPAVNCISFTGGDT-GISISKKAG--MIPLQMEL 265
Cdd:cd07098 155 VSEQVAWSSgffLSIIReCLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPvGKKVMAAAAesLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 266 GGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESS 344
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPlDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 345 ANFIEGLVMDAKEKGATFCQEYKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNF 417
Cdd:cd07098 314 FDRLEELVADAVEKGARLLAGGKRyphpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEY 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15224111 418 GLQGCVFTKDINKAILISDAMETGTVQINS-APARGPDHFPFQGLKDSGIG 467
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAINDfGVNYYVQQLPFGGVKGSGFG 444
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
35-467 |
3.49e-78 |
|
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: 251.48 E-value: 3.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVT-E 113
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 114 VVRSGDLISYCAeegvrilGEGKFLlsdsfPGNDRTKYC--LTSKI---PLGVVLAIPPFNYPVNLAVSKIAPALIAGNS 188
Cdd:cd07092 81 LPGAVDNFRFFA-------GAARTL-----EGPAAGEYLpgHTSMIrrePIGVVAQIAPWNYPLMMAAWKIAPALAAGNT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 189 LVLKPPTQGAVSCLHMVHcfhLA--GFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKA--GMIPLQM 263
Cdd:cd07092 149 VVLKPSETTPLTTLLLAE---LAaeVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSvRTGKKVARAAadTLKRVHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 264 ELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVS- 341
Cdd:cd07092 226 ELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPdDEDTEMGPLNSa 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 342 ---ESSANFIEGLVMDAK-EKGATFCqeyKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNF 417
Cdd:cd07092 306 aqrERVAGFVERAPAHARvLTGGRRA---EGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15224111 418 GLQGCVFTKDINKAILISDAMETGTVQINsapargpDHF------PFQGLKDSGIG 467
Cdd:cd07092 383 GLASSVWTRDVGRAMRLSARLDFGTVWVN-------THIplaaemPHGGFKQSGYG 431
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
49-486 |
1.41e-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: 249.95 E-value: 1.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 49 ACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAE 126
Cdd:cd07118 15 EGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAAS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 127 EGVRILGEGKFLLSDSFPGndrtkycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVH 206
Cdd:cd07118 95 LARTLHGDSYNNLGDDMLG-------LVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 207 CFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGD-TGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVA 283
Cdd:cd07118 168 LLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTrVGKAIAAAAArnLKKVSLELGGKNPQIVFADADLDAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 284 SNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATF 362
Cdd:cd07118 248 DAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPlDPETKVGAIINEAQLAKITDYVDAGRAEGATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 363 C----QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAM 438
Cdd:cd07118 328 LlggeRLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRI 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15224111 439 ETGTVQINSAPARGPDhFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07118 408 RAGTVWVNTFLDGSPE-LPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
19-488 |
5.38e-76 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 246.74 E-value: 5.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAES 98
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 99 LVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGegkfllsDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG-------DTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 179 IAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG 257
Cdd:PRK11241 167 AGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGStEIGRQLMEQCA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 258 --MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENS 334
Cdd:PRK11241 247 kdIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGlEKGV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 335 DITAVVSESSANFIEGLVMDAKEKGATFC---QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINH 411
Cdd:PRK11241 327 TIGPLIDEKAVAKVEEHIADALEKGARVVcggKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQ 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224111 412 CNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGpDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVINL 488
Cdd:PRK11241 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISN-EVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
34-467 |
9.83e-74 |
|
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: 241.72 E-value: 9.83e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 34 AIMNPATRKTQ-YKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVT 112
Cdd:cd07125 49 PVIDPADHERTiGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 113 EVVRSGDLISYCAEEGVRILGEGkfLLSDSFPGNDRTKYcltskIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLK 192
Cdd:cd07125 129 EVREAIDFCRYYAAQARELFSDP--ELPGPTGELNGLEL-----HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 193 PPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISK-----KAGMIPLQMELG 266
Cdd:cd07125 202 PAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGStETAKLINRalaerDGPILPLIAETG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 267 GKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEE-NSDITAVVSESSA 345
Cdd:cd07125 282 GKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDlSTDVGPLIDKPAG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 346 NFIEGLvmdakekgatfCQEYKREGNLIWPLLLDNVRPDM---RIAW--------EEPFGPVVPVLRINS--VEEGINHC 412
Cdd:cd07125 362 KLLRAH-----------TELMRGEAWLIAPAPLDDGNGYFvapGIIEivgifdltTEVFGPILHVIRFKAedLDEAIEDI 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 413 NASNFGLQGCVFTKDINKAILISDAMETGTVQINsapaRGpd-----hfPFQGLKDSGIG 467
Cdd:cd07125 431 NATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN----RNitgaivgrqPFGGWGLSGTG 486
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
16-470 |
1.12e-73 |
|
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: 240.76 E-value: 1.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPM 95
Cdd:cd07111 22 FGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 96 A--ESLVKeiAKPAKDS----VTEVVRsgdLISYCAeegvrilGEGKFLLSDsFPGNDrtkycltskiPLGVVLAIPPFN 169
Cdd:cd07111 102 AvlESLDN--GKPIRESrdcdIPLVAR---HFYHHA-------GWAQLLDTE-LAGWK----------PVGVVGQIVPWN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 170 YPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSeIGDFLTMHPAVNCISFTGG-DT 248
Cdd:cd07111 159 FPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGStEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 249 GISISKK-AGMIP-LQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLT 326
Cdd:cd07111 238 GRALRRAtAGTGKkLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 327 VGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQ---EYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRI 402
Cdd:cd07111 318 VGDPlDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQpgaDLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTF 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224111 403 NSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIGSQG 470
Cdd:cd07111 398 RTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAA-GFGGYRESGFGREG 464
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
16-468 |
7.75e-73 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 238.27 E-value: 7.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWkTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPM 95
Cdd:PRK13473 3 TKLLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 96 AESLVKEIAKPAKDSVT-EVVRSGDLISYCAeeG-VRILgEGKfLLSDSFPGNdrtkyclTSKI---PLGVVLAIPPFNY 170
Cdd:PRK13473 82 ARLESLNCGKPLHLALNdEIPAIVDVFRFFA--GaARCL-EGK-AAGEYLEGH-------TSMIrrdPVGVVASIAPWNY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 171 PVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHcfhLAG--FPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-D 247
Cdd:PRK13473 151 PLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAE---LAAdiLPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSiA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 248 TGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKL 325
Cdd:PRK13473 228 TGKHVLSAAAdsVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 326 TVGPP-EENSDITAVVSESSANFIEGLVMDAKEKG----ATFCQEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVL 400
Cdd:PRK13473 308 KVGDPdDEDTELGPLISAAHRDRVAGFVERAKALGhirvVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVT 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224111 401 RINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINsapargpDHF------PFQGLKDSGIGS 468
Cdd:PRK13473 388 PFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVN-------THFmlvsemPHGGQKQSGYGK 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
17-485 |
8.41e-72 |
|
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: 235.85 E-value: 8.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 17 KYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKAP 94
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 95 MAESLVKEIAKPAKDSVT-EVVRSGDLISYCAEEGVRILGEgkfllsdSFPGnDRTKYCLTSKIPLGVVLAIPPFNYPVN 173
Cdd:cd07142 85 LAALETWDNGKPYEQARYaEVPLAARLFRYYAGWADKIHGM-------TLPA-DGPHHVYTLHEPIGVVGQIIPWNFPLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 174 LAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISI 252
Cdd:cd07142 157 MFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGStEVGKII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 253 ---SKKAGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGP 329
Cdd:cd07142 237 mqlAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 330 P-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKREGN---LIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSV 405
Cdd:cd07142 317 PfRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSkgyYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 406 EEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGVTNSINLMTKVKTTV 485
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDAS-IPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
37-467 |
7.61e-71 |
|
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: 232.62 E-value: 7.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 37 NPATRKTQYKVQACTQEEVNAVMELAKSAQK--SWAKTPLwKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEV 114
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 115 VRSGDLISYCAEEGVRILGEGKfllsDSFPGNdrtkYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPP 194
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMI----EPEPGS----FSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 195 TQGAVSCLHMVHCFH-LAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGD-TGISISKKAG--MIPLQMELGGKDA 270
Cdd:cd07120 154 GQTAQINAAIIRILAeIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTaTGRAIMAAAAptLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 271 CIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANFIE 349
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGlDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 350 GLVMDAKEKGATFC------QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCV 423
Cdd:cd07120 314 RMVERAIAAGAEVVlrggpvTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15224111 424 FTKDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIG 467
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDW-NKLFAEAEEGGYRQSGLG 436
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
81-467 |
1.17e-68 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 225.39 E-value: 1.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 81 LHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRIlgEGKFLLSDSfPGNDrtkyCLTSKIPLG 160
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRY--EGEIIQSDR-PGEN----ILLFKRALG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 161 VVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNC 240
Cdd:PRK10090 74 VTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 241 ISFTGG-DTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEK 317
Cdd:PRK10090 154 VSMTGSvSAGEKIMAAAAknITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 318 VKAKVAKLTVGPPEENSDIT--AVVSESSANFIEGLVMDAKEKGATFCQEYKRE---GNLIWPLLLDNVRPDMRIAWEEP 392
Cdd:PRK10090 234 LGEAMQAVQFGNPAERNDIAmgPLINAAALERVEQKVARAVEEGARVALGGKAVegkGYYYPPTLLLDVRQEMSIMHEET 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15224111 393 FGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFpFQGLKDSGIG 467
Cdd:PRK10090 314 FGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGF-HAGWRKSGIG 387
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
13-483 |
2.56e-66 |
|
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: 222.07 E-value: 2.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 13 GEVYKYYADGEWKTSSSGKSvaIMNP-ATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDN 91
Cdd:cd07083 16 GRAYPLVIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 92 KAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRIlgEGKFLLSDSFPGNDRTkyclTSKIPLGVVLAIPPFNYP 171
Cdd:cd07083 94 RRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRL--RYPAVEVVPYPGEDNE----SFYVGLGAGVVISPWNFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 172 VNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGI 250
Cdd:cd07083 168 VAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSlETGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 251 SISKKAG--------MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKV 322
Cdd:cd07083 248 KIYEAAArlapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 323 AKLTVGPPEEN-SDITAVVSESSANFIEGLVMDAKEKGATFCQEYKREGN--LIWPLLLDNVRPDMRIAWEEPFGPVVPV 399
Cdd:cd07083 328 ERLSVGPPEENgTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEgyFVAPTVVEEVPPKARIAQEEIFGPVLSV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 400 LRINSVE--EGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQIN---SAPARGPDhfPFQGLKDSGIGSQ-GVTN 473
Cdd:cd07083 408 IRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkiTGALVGVQ--PFGGFKLSGTNAKtGGPH 485
|
490
....*....|
gi 15224111 474 SINLMTKVKT 483
Cdd:cd07083 486 YLRRFLEMKA 495
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
32-467 |
1.08e-64 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 216.53 E-value: 1.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 32 SVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSV 111
Cdd:PRK09406 2 PIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 112 TEVVRSGDLISYCAEEGVRILGEgkfllSDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVL 191
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLAD-----EPADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 192 KPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTmHPAVNCISFTGGD-TGISISKKAG--MIPLQMELGGK 268
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILR-DPRVAAATLTGSEpAGRAVAAIAGdeIKKTVLELGGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 269 DACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSANF 347
Cdd:PRK09406 236 DPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPtDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 348 IEGLVMDAKEKGAT-FCQEYKREGNLIW--PLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVF 424
Cdd:PRK09406 316 VEKQVDDAVAAGATiLCGGKRPDGPGWFypPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15224111 425 TKDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIG 467
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMTVSYPE-LPFGGVKRSGYG 437
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
35-486 |
2.33e-64 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 215.36 E-value: 2.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 35 IMNPATRKTQYKVQACTQEEVNAVMELAKSAQK---SWakTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSV 111
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 112 TEVVRSGDLISYCAEEgVRILGEGKFLLSDSFPGNDRTKYclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVL 191
Cdd:cd07148 81 VEVTRAIDGVELAADE-LGQLGGREIPMGLTPASAGRIAF--TTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 192 KPPTQGAVSCLHMVHCFHLAGFPKG---LISCitgkGSEIGDFLTMHPAVNCISFTG-GDTGISI-SKKAGMIPLQMELG 266
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGwcqAVPC----ENAVAEKLVTDPRVAFFSFIGsARVGWMLrSKLAPGTRCALEHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 267 GKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDITAVVSESSA 345
Cdd:cd07148 234 GAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPtDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 346 NFIEGLVMDAKEKGATFCQEYKREGN-LIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVF 424
Cdd:cd07148 314 DRVEEWVNEAVAAGARLLCGGKRLSDtTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224111 425 TKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNSINLMTKVKTTVI 486
Cdd:cd07148 394 TKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
17-483 |
1.13e-62 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 211.66 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 17 KYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMA 96
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 97 ESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEgkflLSDSFPGN-DRTKYcltsKIPLGVVLAIPPFNYPVNLA 175
Cdd:TIGR01722 82 ELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGE----TSTQVATRvDVYSI----RQPLGVCAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 176 VSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGkGSEIGDFLTMHPAVNCISFTGG--------D 247
Cdd:TIGR01722 154 LWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGStpigryihT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 248 TGISISKKagmipLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVlVMESVADELVEKVKAKVAKLTV 327
Cdd:TIGR01722 233 TGSAHGKR-----VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAA-VLVGAADEWVPEIRERAEKIRI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 328 GPPEE-NSDITAVVSESSANFIEGLVMDAKEKGATFCQE---YK----REGNLIWPLLLDNVRPDMRIAWEEPFGPVVPV 399
Cdd:TIGR01722 307 GPGDDpGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDgrgYKvdgyEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 400 LRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINsAPARGP-DHFPFQGLKDSGIGSQGV--TNSIN 476
Cdd:TIGR01722 387 LEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN-VPIPVPlPYFSFTGWKDSFFGDHHIygKQGTH 465
|
....*..
gi 15224111 477 LMTKVKT 483
Cdd:TIGR01722 466 FYTRGKT 472
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
16-486 |
3.19e-62 |
|
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: 210.81 E-value: 3.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKA 93
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 94 PMA--ESL----VKEIAKPakdsvTEVVRSGDLISYCAEEGVRILGEgKFLLSDSFPGNDrtkYCLTSKIPLGVVLAIPP 167
Cdd:cd07140 86 ELAtiESLdsgaVYTLALK-----THVGMSIQTFRYFAGWCDKIQGK-TIPINQARPNRN---LTLTKREPIGVCGIVIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 168 FNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG- 246
Cdd:cd07140 157 WNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 247 DTGISISKKAGMIPLQ---MELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVA 323
Cdd:cd07140 237 PIGKHIMKSCAVSNLKkvsLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 324 KLTVGPPEENSdiTAVVSESSANFIEGLV---MDAKEKGATFC---QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVV 397
Cdd:cd07140 317 KMKIGDPLDRS--TDHGPQNHKAHLDKLVeycERGVKEGATLVyggKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 398 PVLRINS--VEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGVTNSI 475
Cdd:cd07140 395 IISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTY-NKTDVAAPFGGFKQSGFGKDLGEEAL 473
|
490
....*....|.
gi 15224111 476 NLMTKVKTTVI 486
Cdd:cd07140 474 NEYLKTKTVTI 484
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
17-488 |
7.86e-62 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 209.75 E-value: 7.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 17 KYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKS--WAKTPLWKRAELLHKAAAILKDNKAP 94
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 95 MA--ESL--VKEIAKPAKDSVTEVVRSgdlISYCAEEGVRILGEGKFLLSDSFpgndrtkyCLTSKIPLGVVLAIPPFNY 170
Cdd:PRK09847 101 LAllETLdtGKPIRHSLRDDIPGAARA---IRWYAEAIDKVYGEVATTSSHEL--------AMIVREPVGVIAAIVPWNF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 171 PVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGD-TG 249
Cdd:PRK09847 170 PLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTrTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 250 ISISKKAG---MIPLQMELGGKDACIVLDDA-DLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKL 325
Cdd:PRK09847 250 KQLLKDAGdsnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 326 TVGPPEENSD-----ITAVVSESSANFIEG------LVMDAKEKGATFCqeykregnlIWPLLLDNVRPDMRIAWEEPFG 394
Cdd:PRK09847 330 QPGHPLDPATtmgtlIDCAHADSVHSFIREgeskgqLLLDGRNAGLAAA---------IGPTIFVDVDPNASLSREEIFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 395 PVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGVTNS 474
Cdd:PRK09847 401 PVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNY-NDGDMTVPFGGYKQSGNGRDKSLHA 479
|
490
....*....|....
gi 15224111 475 INLMTKVKTTVINL 488
Cdd:PRK09847 480 LEKFTELKTIWISL 493
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
21-493 |
3.87e-61 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 209.28 E-value: 3.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 21 DGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKAPMAES 98
Cdd:PLN02466 63 NGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 99 LVKEIAKPAKDSV-TEVVRSGDLISYCAEEGVRILGEgkfllsdSFPGnDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVS 177
Cdd:PLN02466 143 ETWDNGKPYEQSAkAELPMFARLFRYYAGWADKIHGL-------TVPA-DGPHHVQTLHEPIGVAGQIIPWNFPLLMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 178 KIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTG---ISIS 253
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGStDTGkivLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 254 KKAGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP--- 330
Cdd:PLN02466 295 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPfkk 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 331 --EENSDITAVVSESSANFIEGLVmdakEKGATFC---QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSV 405
Cdd:PLN02466 375 gvEQGPQIDSEQFEKILRYIKSGV----ESGATLEcggDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 406 EEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSApargpDHF----PFQGLKDSGIGSQGVTNSINLMTKV 481
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCF-----DVFdaaiPFGGYKMSGIGREKGIYSLNNYLQV 525
|
490
....*....|..
gi 15224111 482 KTTVINLPTPSY 493
Cdd:PLN02466 526 KAVVTPLKNPAW 537
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
17-489 |
1.21e-60 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 206.98 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 17 KYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSA--QKSWAKTPLWKRAELLHKAAAILKDNKAP 94
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 95 MAESLVKEIAK-PAKDSVTEVVRSGDLISYCAEEGVRILGEgKFLLSDSFPGndrtkycLTSKIPLGVVLAIPPFNYPVN 173
Cdd:PLN02766 102 LAALDTIDAGKlFALGKAVDIPAAAGLLRYYAGAADKIHGE-TLKMSRQLQG-------YTLKEPIGVVGHIIPWNFPST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 174 LAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISI 252
Cdd:PLN02766 174 MFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGStEVGRKI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 253 SKKAG---MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGP 329
Cdd:PLN02766 254 MQAAAtsnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 330 P-EENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSV 405
Cdd:PLN02766 334 PfDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKpcgDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 406 EEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGVTNSINLMTKVKTTV 485
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPD-CPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
....
gi 15224111 486 INLP 489
Cdd:PLN02766 493 TPLY 496
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
54-465 |
2.23e-59 |
|
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: 201.73 E-value: 2.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 54 EVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILG 133
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 134 EGKFLLSDsfpGNDRTKYCltskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGF 213
Cdd:cd07095 81 ERATPMAQ---GRAVLRHR-----PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 214 PKGLISCITGkGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAGMIP---LQMELGGKDACIVLDDADLDLVASNIIKG 289
Cdd:cd07095 153 PPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSaATGLLLHRQFAGRPgkiLALEMGGNNPLVVWDVADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 290 GFSYSGQRCTAVKVVLVMES-VADELVEKVKAKVAKLTVGPPEENsditavvsesSANFIEGLVMDAKEKGATFCQEYKR 368
Cdd:cd07095 232 AFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAE----------PPFMGPLIIAAAAARYLLAQQDLLA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 369 EG--------------NLIWPLLLD----NVRPDmriawEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINK 430
Cdd:cd07095 302 LGgepllamerlvagtAFLSPGIIDvtdaADVPD-----EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEAL 376
|
410 420 430
....*....|....*....|....*....|....*
gi 15224111 431 AILISDAMETGTVQINSAPARGPDHFPFQGLKDSG 465
Cdd:cd07095 377 FERFLARIRAGIVNWNRPTTGASSTAPFGGVGLSG 411
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
19-419 |
5.40e-57 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 196.72 E-value: 5.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKTSSsGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAES 98
Cdd:PRK09457 4 WINGDWIAGQ-GEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 99 LVKEIAKPAKDSVTEVvrsGDLI--------SYCAEEGVRilgegkfllSDSFPGNdrtKYCLTSKiPLGVVLAIPPFNY 170
Cdd:PRK09457 83 IARETGKPLWEAATEV---TAMInkiaisiqAYHERTGEK---------RSEMADG---AAVLRHR-PHGVVAVFGPYNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 171 PVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGkGSEIGDFLTMHPAVNCISFTG-GDTG 249
Cdd:PRK09457 147 PGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGsANTG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 250 ISISKKAGMIP---LQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESV-ADELVEKVKAKVAKL 325
Cdd:PRK09457 226 YLLHRQFAGQPekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 326 TVGPPeeNSD----ITAVVSESSANFIEGLVMDAKEKGATFCQEYKR---EGNLIWPLLLD--NV--RPDmriawEEPFG 394
Cdd:PRK09457 306 TVGRW--DAEpqpfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQlqaGTGLLTPGIIDvtGVaeLPD-----EEYFG 378
|
410 420
....*....|....*....|....*
gi 15224111 395 PVVPVLRINSVEEGINHCNASNFGL 419
Cdd:PRK09457 379 PLLQVVRYDDFDEAIRLANNTRFGL 403
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
26-469 |
2.04e-53 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 186.61 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 26 TSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAK 105
Cdd:PRK13968 2 TITPATHAISVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 106 PAKDSVTEVVRSGDLISYCAEEGVRILGEGKFLLSDsfpgndrtKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIA 185
Cdd:PRK13968 82 PINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVEN--------QQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 186 GNSLVLKPpTQGAVSCLHMV-HCFHLAGFPKGLISCIT----GKGSEIGDfltmhPAVNCISFTGG-DTGISISKKAG-- 257
Cdd:PRK13968 154 GNGYLLKH-APNVMGCAQLIaQVFKDAGIPQGVYGWLNadndGVSQMIND-----SRIAAVTVTGSvRAGAAIGAQAGaa 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 258 MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP-EENSDI 336
Cdd:PRK13968 228 LKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPrDEENAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 337 TAVVSESSANFIEGLVMDAKEKGATFC---QEYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCN 413
Cdd:PRK13968 308 GPMARFDLRDELHHQVEATLAEGARLLlggEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELAN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15224111 414 ASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQ 469
Cdd:PRK13968 388 DSEFGLSATIFTTDETQARQMAARLECGGVFINGYCASDA-RVAFGGVKKSGFGRE 442
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
19-431 |
1.81e-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: 181.64 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWktSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAES 98
Cdd:cd07130 2 VYDGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 99 LVKEIAKPAKDSVTEVvrsGDLISYC--AEEGVRILGeGKFLLSDSfPG-------NdrtkycltskiPLGVVLAIPPFN 169
Cdd:cd07130 80 VSLEMGKILPEGLGEV---QEMIDICdfAVGLSRQLY-GLTIPSER-PGhrmmeqwN-----------PLGVVGVITAFN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 170 YPV-----NLAVskiapALIAGNSLVLKP-PTQG--AVSCLHMV-HCFHLAGFPKGLISCITGkGSEIGDFLTMHPAVNC 240
Cdd:cd07130 144 FPVavwgwNAAI-----ALVCGNVVVWKPsPTTPltAIAVTKIVaRVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 241 ISFTGG-----DTGISISKKAGMIPLqmELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELV 315
Cdd:cd07130 218 VSFTGStavgrQVGQAVAARFGRSLL--ELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 316 EKVKAKVAKLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFC---QEYKREGNLIWPLLLDnVRPDMRIAWEE 391
Cdd:cd07130 296 ERLKKAYKQVRIGDPlDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLfggKVIDGPGNYVEPTIVE-GLSDAPIVKEE 374
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15224111 392 PFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKA 431
Cdd:cd07130 375 TFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNA 414
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
16-470 |
2.04e-50 |
|
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: 179.19 E-value: 2.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 16 YKYYADGEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPM 95
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 96 AESLVKEIAKPAKDSV-TEVVRSGDLISYCAeeGVRILGEGKFLLSDSfpgnDRTKYCLTSkiPLGVVLAIPPFNYPVNL 174
Cdd:cd07116 81 AVAETWDNGKPVRETLaADIPLAIDHFRYFA--GCIRAQEGSISEIDE----NTVAYHFHE--PLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 175 AVSKIAPALIAGNSLVLKPPTQGAVSCLHMVhcfHLAG--FPKGLISCITGKGSEIGDFLTMHPAVNCISFTG-GDTGIS 251
Cdd:cd07116 153 ATWKLAPALAAGNCVVLKPAEQTPASILVLM---ELIGdlLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGeTTTGRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 252 ISKKA--GMIPLQMELGGKDACIVLDD---ADLDLVASNIikGGFSY----SGQRCTAVKVVLVMESVADELVEKVKAKV 322
Cdd:cd07116 230 IMQYAseNIIPVTLELGGKSPNIFFADvmdADDAFFDKAL--EGFVMfalnQGEVCTCPSRALIQESIYDRFMERALERV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 323 AKLTVGPP-EENSDITAVVSESSANFIEGLVMDAKEKGATFC---QEYKREGNL-----IWPLLLDNVRpdMRIAWEEPF 393
Cdd:cd07116 308 KAIKQGNPlDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLtggERNELGGLLgggyyVPTTFKGGNK--MRIFQEEIF 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224111 394 GPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARgPDHFPFQGLKDSGIGSQG 470
Cdd:cd07116 386 GPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLY-PAHAAFGGYKQSGIGREN 461
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
22-483 |
1.61e-49 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 179.17 E-value: 1.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 22 GEWKTSSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVK 101
Cdd:PLN02419 120 GSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 102 EIAKPAKDSVTEVVRSGDLISYCAeeGVRILGEGKFLLSDSfpgNDRTKYCLtsKIPLGVVLAIPPFNYPVNLAVSKIAP 181
Cdd:PLN02419 200 EQGKTLKDSHGDIFRGLEVVEHAC--GMATLQMGEYLPNVS---NGVDTYSI--REPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 182 ALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIgDFLTMHPAVNCISFTGGDT-GISISKKAGM-- 258
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTaGMHIYARAAAkg 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 259 IPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVM---ESVADELVEkvKAKVAKLTVGpPEENSD 335
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVgdaKSWEDKLVE--RAKALKVTCG-SEPDAD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 336 ITAVVSESSANFIEGLVMDAKEKGATFCQEYK-------REGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEG 408
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224111 409 INHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGVTNS--INLMTKVKT 483
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKagVDFFTQIKL 585
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
156-468 |
2.23e-49 |
|
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: 175.02 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKP----PtqgAVSCLhmvhcfhLA-----GFPKGLISCITGKGS 226
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPselaP---ATSAL-------LAklipkYFDPEAVAVVEGGVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 227 EIGDFLTmHPaVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKV 303
Cdd:cd07087 168 VATALLA-EP-FDHIFFTGSpAVGKIVMEAAAkhLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 304 VLVMESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLVMDAK-EKGAtfcqEYKREGNLIWPLLLDNVR 382
Cdd:cd07087 246 VLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKvVIGG----QVDKEERYIAPTILDDVS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 383 PDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSA--PArGPDHFPFQG 460
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVllHA-AIPNLPFGG 400
|
....*...
gi 15224111 461 LKDSGIGS 468
Cdd:cd07087 401 VGNSGMGA 408
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
39-468 |
7.86e-47 |
|
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: 168.17 E-value: 7.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 39 ATRKTQYKVQACTQEEVNAVMELAKSAqkswaktpLWKRAELLHkaAAILKDNKAPMAESLVKEIaKPAKDSVTEVVRsg 118
Cdd:cd07134 6 AQQAHALALRASTAAERIAKLKRLKKA--------ILARREEII--AALAADFRKPAAEVDLTEI-LPVLSEINHAIK-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 119 DLISYCAEEGVR--ILGEGkfllsdsfpgndrTKycltSKI---PLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKP 193
Cdd:cd07134 73 HLKKWMKPKRVRtpLLLFG-------------TK----SKIryePKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 194 PTQgavsclhmvhCFHLAGFPKGLISCI---------TGkGSEIGDFLTMHPaVNCISFTGGDT-GISISKKAG--MIPL 261
Cdd:cd07134 136 SEL----------TPHTSAVIAKIIREAfdedevavfEG-DAEVAQALLELP-FDHIFFTGSPAvGKIVMAAAAkhLASV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 262 QMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKL--TVGPPEENSDITAV 339
Cdd:cd07134 204 TLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASPDLARI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 340 VSESSANFIEGLVMDAKEKGATFCQ--EYKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNF 417
Cdd:cd07134 284 VNDRHFDRLKGLLDDAVAKGAKVEFggQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPK 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15224111 418 GLQGCVFTKD---INKAIlisDAMETGTVQINSAPArgpdHF-----PFQGLKDSGIGS 468
Cdd:cd07134 364 PLALYVFSKDkanVNKVL---ARTSSGGVVVNDVVL----HFlnpnlPFGGVNNSGIGS 415
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
73-468 |
3.98e-46 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 167.51 E-value: 3.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 73 PLWKRAELLHKAAAILKDNKAPMAESLVKEIAKPAKDS-VTEVVRS--------GDLISYCAEEGVRIlgEGKFLLSDSF 143
Cdd:PTZ00381 27 PLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETkMTEVLLTvaeiehllKHLDEYLKPEKVDT--VGVFGPGKSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 144 pgndrtkyclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPpTQGAVSCLHMVHCFHLAGFPKGLISCITG 223
Cdd:PTZ00381 105 ----------IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKP-SELSPHTSKLMAKLLTKYLDPSYVRVIEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 224 kGSEIGDFLTMHPaVNCISFTGG-DTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTA 300
Cdd:PTZ00381 174 -GVEVTTELLKEP-FDHIFFTGSpRVGKLVMQAAAenLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 301 VKVVLVMESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLVMDAKEKGAtFCQEYKREGNLIWPLLLDN 380
Cdd:PTZ00381 252 PDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGKVV-YGGEVDIENKYVAPTIIVN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 381 VRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPAR-GPDHFPFQ 459
Cdd:PTZ00381 331 PDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHlLNPNLPFG 410
|
....*....
gi 15224111 460 GLKDSGIGS 468
Cdd:PTZ00381 411 GVGNSGMGA 419
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
17-446 |
2.29e-45 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 165.85 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 17 KYYADGEWKtsssgksvAIMNPATRKTQY-KVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPM 95
Cdd:TIGR01238 45 SYKADGEAQ--------PVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 96 AESLVKEIAKPAKDSVTEVVRSGDLISYCAEEgvrilgegkflLSDSFPgNDRTKycltskiPLGVVLAIPPFNYPVNLA 175
Cdd:TIGR01238 117 MALCVREAGKTIHNAIAEVREAVDFCRYYAKQ-----------VRDVLG-EFSVE-------SRGVFVCISPWNFPLAIF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 176 VSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGDTGISI--- 252
Cdd:TIGR01238 178 TGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLinq 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 253 ---SKKAGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGP 329
Cdd:TIGR01238 258 tlaQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 330 PEE-NSDITAVVSESSANFIEGLVMDAKEKGATFCQEYK------REGNLIWPLL--LDNVRPdmriAWEEPFGPVVPVL 400
Cdd:TIGR01238 338 PHLlTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLddsracQHGTFVAPTLfeLDDIAE----LSEEVFGPVLHVV 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15224111 401 RINSVE--EGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQIN 446
Cdd:TIGR01238 414 RYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
26-419 |
6.59e-44 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 166.19 E-value: 6.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 26 TSSSGKSVAIMNPATRKTQY-KVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIA 104
Cdd:PRK11905 562 GDVDGGTRPVLNPADHDDVVgTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 105 KPAKDSVTEVVRSGDLISYCAEEGVRilgegkfllsdsFPGNDRTKycltskiPLGVVLAIPPFNYPVNLAVSKIAPALI 184
Cdd:PRK11905 642 KTLANAIAEVREAVDFLRYYAAQARR------------LLNGPGHK-------PLGPVVCISPWNFPLAIFTGQIAAALV 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 185 AGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKK-----AGM 258
Cdd:PRK11905 703 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGStEVARLIQRTlakrsGPP 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 259 IPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEE-NSDIT 337
Cdd:PRK11905 783 VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRlSTDVG 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 338 AVVSEssanfieglvmDAKEKGATFCQEYKREGNLIWPLLLDN-------VRP------DMRIAWEEPFGPVVPVLRINS 404
Cdd:PRK11905 863 PVIDA-----------EAQANIEAHIEAMRAAGRLVHQLPLPAetekgtfVAPtlieidSISDLEREVFGPVLHVVRFKA 931
|
410
....*....|....*..
gi 15224111 405 --VEEGINHCNASNFGL 419
Cdd:PRK11905 932 deLDRVIDDINATGYGL 948
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
81-485 |
1.37e-43 |
|
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: 159.31 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 81 LHKAAAILKDNKAPMAESLVKEIAKPAKDSV-TEVVRS-GDLISYCA-------EEGVrilgegKFLLSDSFPGNDRTKy 151
Cdd:cd07135 33 LKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVkNDILHMLKnlkkwakDEKV------KDGPLAFMFGKPRIR- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 152 cltsKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKP----PTQGAVsCLHMVHcfhlAGFPKGLISCITGKGSE 227
Cdd:cd07135 106 ----KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPseltPHTAAL-LAELVP----KYLDPDAFQVVQGGVPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 228 IGDFLTMHpaVNCISFTGGDT-GISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVV 304
Cdd:cd07135 177 TTALLEQK--FDKIFYTGSGRvGRIIAEAAAkhLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 305 LVMESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLVMDAKEK---GATFcqeyKREGNLIWPLLLDNV 381
Cdd:cd07135 255 LVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGKvviGGEM----DEATRFIPPTIVSDV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 382 RPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKD---INKailISDAMETGTVQIN-SAPARGPDHFP 457
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDkseIDH---ILTRTRSGGVVINdTLIHVGVDNAP 407
|
410 420
....*....|....*....|....*...
gi 15224111 458 FQGLKDSGIGSQGVTNSINLMTKVKTTV 485
Cdd:cd07135 408 FGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
6-419 |
2.09e-43 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 164.60 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 6 LFAEIldgevyKYYADGEWKTSS----SGKSVAIMNPA-TRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAEL 80
Cdd:PRK11904 539 LAAAI------AAFLEKQWQAGPiingEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAI 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 81 LHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGVRILGEGKFLlsdsfPGND--RTKYCLTSKip 158
Cdd:PRK11904 613 LERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKL-----PGPTgeSNELRLHGR-- 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 159 lGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAV 238
Cdd:PRK11904 686 -GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRI 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 239 NCISFTGG-DTGISI-----SKKAGMIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVAD 312
Cdd:PRK11904 765 AGVAFTGStETARIInrtlaARDGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIAD 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 313 ELVEKVKAKVAKLTVGPPEENS-DItavvsessanfieGLVMD--AKEKGATFCQEYKREGNLIWPLLLDN-------VR 382
Cdd:PRK11904 845 RVIEMLKGAMAELKVGDPRLLStDV-------------GPVIDaeAKANLDAHIERMKREARLLAQLPLPAgtenghfVA 911
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15224111 383 P---------DMRiawEEPFGPVVPVLR-----INSVEEGInhcNASNFGL 419
Cdd:PRK11904 912 PtafeidsisQLE---REVFGPILHVIRykasdLDKVIDAI---NATGYGL 956
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
143-468 |
2.43e-41 |
|
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: 153.43 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 143 FPGNDRTKYcltskIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKP----PtqgAVSCL--HMVHcfhlAGFPKG 216
Cdd:cd07136 90 FPSKSYIYY-----EPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPseltP---NTSKViaKIIE----ETFDEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 217 LISCITGkGSEIGDFLtMHPAVNCISFTGGDT-GISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSY 293
Cdd:cd07136 158 YVAVVEG-GVEENQEL-LDQKFDYIFFTGSVRvGKIVMEAAAkhLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 294 SGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLVmdakEKGATFCQ-EYKREGNL 372
Cdd:cd07136 236 AGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLL----DNGKIVFGgNTDRETLY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 373 IWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQIN------ 446
Cdd:cd07136 312 IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimhl 391
|
330 340
....*....|....*....|..
gi 15224111 447 SAPargpdHFPFQGLKDSGIGS 468
Cdd:cd07136 392 ANP-----YLPFGGVGNSGMGS 408
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
27-419 |
2.97e-40 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 155.52 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 27 SSSGKSVAIMNPATRKTQY-KVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAK 105
Cdd:PRK11809 655 VAAGEMSPVINPADPRDIVgYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 106 PAKDSVTEVVRSGDLISYCAEEgVRilgegkfllsDSFpGNDrtkycltSKIPLGVVLAIPPFNYPVNLAVSKIAPALIA 185
Cdd:PRK11809 735 TFSNAIAEVREAVDFLRYYAGQ-VR----------DDF-DND-------THRPLGPVVCISPWNFPLAIFTGQVAAALAA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 186 GNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTgGDTGI------SISKK---A 256
Cdd:PRK11809 796 GNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFT-GSTEVarllqrNLAGRldpQ 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 257 GM-IPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENS- 334
Cdd:PRK11809 875 GRpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSt 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 335 DITAVVSESSANFIEGLVMDAKEKGATFCQ------EYKREGNLIWPLL--LDNVRPDMRiaweEPFGPVVPVLR----- 401
Cdd:PRK11809 955 DIGPVIDAEAKANIERHIQAMRAKGRPVFQaarensEDWQSGTFVPPTLieLDSFDELKR----EVFGPVLHVVRynrnq 1030
|
410
....*....|....*...
gi 15224111 402 INSVEEGInhcNASNFGL 419
Cdd:PRK11809 1031 LDELIEQI---NASGYGL 1045
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
158-468 |
1.67e-39 |
|
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: 148.40 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKP----PTQGAVsclhMVHCFHlAGFPKGLISCITGkGSEIG-DFL 232
Cdd:cd07133 101 PLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPseftPRTSAL----LAELLA-EYFDEDEVAVVTG-GADVAaAFS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 233 TM---HpavncISFTG-GDTGISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLV 306
Cdd:cd07133 175 SLpfdH-----LLFTGsTAVGRHVMRAAAenLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 307 MESVADELVEKVKAKVAKLtVGPPEENSDITAVVSESSANFIEGLVMDAKEKGATFCQ-----EYKREGNLIWPLLLDNV 381
Cdd:cd07133 250 PEDKLEEFVAAAKAAVAKM-YPTLADNPDYTSIINERHYARLQGLLEDARAKGARVIElnpagEDFAATRKLPPTLVLNV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 382 RPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKD--INKAIL---ISdametGTVQINSAPAR-GPDH 455
Cdd:cd07133 329 TDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDkaEQDRVLrrtHS-----GGVTINDTLLHvAQDD 403
|
330
....*....|...
gi 15224111 456 FPFQGLKDSGIGS 468
Cdd:cd07133 404 LPFGGVGASGMGA 416
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
27-419 |
1.07e-38 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 150.86 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 27 SSSGKSVAIMNPATRKTQY-KVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAK 105
Cdd:COG4230 566 AASGEARPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 106 PAKDSVTEV---VrsgDLISYCAEEGVRILGEGKFLLsdsfpgndrtkycltskiPLGVVLAIPPFNYPvnLA--VSKIA 180
Cdd:COG4230 646 TLPDAIAEVreaV---DFCRYYAAQARRLFAAPTVLR------------------GRGVFVCISPWNFP--LAifTGQVA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 181 PALIAGNSLVLKPPTQG------AVSCLHMvhcfhlAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISIS 253
Cdd:COG4230 703 AALAAGNTVLAKPAEQTpliaarAVRLLHE------AGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGStETARLIN 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 254 KK-----AGMIPLQMELGGKDACIVldD--ADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLT 326
Cdd:COG4230 777 RTlaardGPIVPLIAETGGQNAMIV--DssALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELR 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 327 VGPPEE-NSDITAVVSEssanfieglvmDAKEKGATFCQEYKREGNLIWPLLLDN-------VRPdmrIAWE-------- 390
Cdd:COG4230 855 VGDPADlSTDVGPVIDA-----------EARANLEAHIERMRAEGRLVHQLPLPEecangtfVAP---TLIEidsisdle 920
|
410 420 430
....*....|....*....|....*....|....*
gi 15224111 391 -EPFGPVVPVLR-----INSVEEGInhcNASNFGL 419
Cdd:COG4230 921 rEVFGPVLHVVRykadeLDKVIDAI---NATGYGL 952
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
51-431 |
8.01e-38 |
|
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: 145.04 E-value: 8.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 51 TQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAIL------KDNKAPM-AESlvKEIAKPAKDSVTEVVrsgDLISY 123
Cdd:cd07123 67 DAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgkyryELNAATMlGQG--KNVWQAEIDAACELI---DFLRF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 124 CAEEGVRILGEGKflLSDSFPGNDRTKYcltskIPL-GVVLAIPPFNYPV---NLAvskIAPALIaGNSLVLKP-PTqgA 198
Cdd:cd07123 142 NVKYAEELYAQQP--LSSPAGVWNRLEY-----RPLeGFVYAVSPFNFTAiggNLA---GAPALM-GNVVLWKPsDT--A 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 199 VSCLHMVH-CFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG-DTGISISKKAG-------MIP-LQMELGGK 268
Cdd:cd07123 209 VLSNYLVYkILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGStPTFKSLWKQIGenldryrTYPrIVGETGGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 269 DACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENSD-ITAVVSESSANF 347
Cdd:cd07123 289 NFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNfMGAVIDEKAFDR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 348 IEGLVMDAKE-KGATF-----CQeyKREGNLIWPLLLDNVRPDMRIAWEEPFGPVVPVL-----RINSVEEGINhcNASN 416
Cdd:cd07123 369 IKGYIDHAKSdPEAEIiaggkCD--DSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYvypdsDFEETLELVD--TTSP 444
|
410
....*....|....*...
gi 15224111 417 FGLQGCVFTKD---INKA 431
Cdd:cd07123 445 YALTGAIFAQDrkaIREA 462
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
19-426 |
5.20e-35 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 136.89 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 19 YADGEWKtsSSGKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAES 98
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 99 LVKEIAKPAKDSVTEVVRSGDLISYCaeegvriLGEGKFLLSDSFPGNDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
Cdd:PLN02315 102 VSLEMGKILAEGIGEVQEIIDMCDFA-------VGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 179 IAPALIAGNSLVLK-PPTQGAVSCLH---MVHCFHLAGFPKGLISCITGkGSEIGDFLTMHPAVNCISFTGgdtgisiSK 254
Cdd:PLN02315 175 ACIALVCGNCVVWKgAPTTPLITIAMtklVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTG-------SS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 255 KAGMIPLQ----------MELGGKDACIVLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAK 324
Cdd:PLN02315 247 KVGLMVQQtvnarfgkclLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 325 LTVGPPEENSDITAVV--SESSANFIEGLVMDAKEKGA--TFCQEYKREGNLIWPLLLDnVRPDMRIAWEEPFGPVVPVL 400
Cdd:PLN02315 327 VKIGDPLEKGTLLGPLhtPESKKNFEKGIEIIKSQGGKilTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVM 405
|
410 420
....*....|....*....|....*.
gi 15224111 401 RINSVEEGINHCNASNFGLQGCVFTK 426
Cdd:PLN02315 406 KFKTLEEAIEINNSVPQGLSSSIFTR 431
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
75-468 |
6.25e-30 |
|
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: 121.36 E-value: 6.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 75 WKRAELlHKAAAILKDNKAPMAESLVKEIAKPAKDS-VTEVvrsGDLISYCAeegVRILGEGKFLLSDSFPGNdRTKYCL 153
Cdd:cd07137 22 WRKSQL-KGLLRLVDENEDDIFAALRQDLGKPSAESfRDEV---SVLVSSCK---LAIKELKKWMAPEKVKTP-LTTFPA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 154 TSKI---PLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQG-AVSCLhmvhcfhLAG-FPKGL----ISCITGk 224
Cdd:cd07137 94 KAEIvsePLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELApATSAL-------LAKlIPEYLdtkaIKVIEG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 225 GSEIGDFLTMHpAVNCISFTGgdtgisiSKKAGMI----------PLQMELGGKDACIVLDDADLDLVASNIIKGGF-SY 293
Cdd:cd07137 166 GVPETTALLEQ-KWDKIFFTG-------SPRVGRIimaaaakhltPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 294 SGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKREGNL- 372
Cdd:cd07137 238 NGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLy 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 373 IWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPAR- 451
Cdd:cd07137 318 IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQy 397
|
410
....*....|....*..
gi 15224111 452 GPDHFPFQGLKDSGIGS 468
Cdd:cd07137 398 AIDTLPFGGVGESGFGA 414
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
152-468 |
3.67e-28 |
|
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: 116.55 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 152 CLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPpTQGAVSCLHMVH----------CFHLagfpkgliscI 221
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKP-SEVSPATAKLLAelipkyldkeCYPV----------V 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 222 TGKGSEIGDFLTM---HpavncISFTGGDT-GISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFSYSG 295
Cdd:cd07132 163 LGGVEETTELLKQrfdY-----IFYTGSTSvGKIVMQAAAkhLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 296 QRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLV----------MDAKEKgatfcqe 365
Cdd:cd07132 238 QTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLsggkvaiggqTDEKER------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 366 YkregnlIWPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQI 445
Cdd:cd07132 311 Y------IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCV 384
|
330 340
....*....|....*....|....
gi 15224111 446 NSAPAR-GPDHFPFQGLKDSGIGS 468
Cdd:cd07132 385 NDTIMHyTLDSLPFGGVGNSGMGA 408
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
157-399 |
5.47e-28 |
|
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: 115.80 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 157 IPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAG-FPKGLISCITGKGsEIGDFLTMH 235
Cdd:cd07084 99 WPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDG-KTMQALLLH 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 236 PAVNCISFTGG-DTGISISKKAGMIPLQMELGGKDACIVLDDAD-LDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADE 313
Cdd:cd07084 178 PNPKMVLFTGSsRVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 314 -LVEKVKAKVAKLTVGP----PEENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKreGNLIWPLLLDNVRPDMRI- 387
Cdd:cd07084 258 pLVEKLKALLARRKLEDlllgPVQTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIY--GACVASALFVPIDEILKTy 335
|
250
....*....|....
gi 15224111 388 -AW-EEPFGPVVPV 399
Cdd:cd07084 336 eLVtEEIFGPFAIV 349
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
158-467 |
1.20e-27 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 115.59 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQgAVSClhmvHCFHLAGFPKGL----ISCITGkGSEIGDFLT 233
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSEL-APAT----SAFLAANIPKYLdskaVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 234 MHPAvNCISFTGGD-TGISISKKAG--MIPLQMELGGKDACIV--LDDA-DLDLVASNIIKGGFSY-SGQRCTAVKVVLV 306
Cdd:PLN02203 182 QHKW-DKIFFTGSPrVGRIIMTAAAkhLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 307 MESVADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLVMDAKEKGATFCQEYKREGNL-IWPLLLDNVRPDM 385
Cdd:PLN02203 261 EERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLfIEPTILLNPPLDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 386 RIAWEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPAR-GPDHFPFQGLKDS 464
Cdd:PLN02203 341 DIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQyACDSLPFGGVGES 420
|
...
gi 15224111 465 GIG 467
Cdd:PLN02203 421 GFG 423
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
158-468 |
3.93e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 96.27 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKgLISCITGKGSEIGDFLTMhpA 237
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQ--K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 238 VNCISFTGGDT-GISISKKAG--MIPLQMELGGKDACIVLDDADLDLVASNIIKGGFS-YSGQRCTAVKVVLVMESVADE 313
Cdd:PLN02174 189 WDKIFYTGSSKiGRVIMAAAAkhLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 314 LVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLvMDAKE--KGATFCQEYKREGNLIWPLLLDNVRPDMRIAWEE 391
Cdd:PLN02174 269 VIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKL-LDEKEvsDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEE 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15224111 392 PFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMETGTVQINSAPARGPDH-FPFQGLKDSGIGS 468
Cdd:PLN02174 348 IFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtLPFGGVGESGMGA 425
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
118-427 |
1.44e-20 |
|
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: 94.64 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 118 GDLISYcAEEGVRILGEGKFLLSDSFP--GNDRT---KYCLTSKipLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLK 192
Cdd:cd07128 102 GTLFAY-ASLGRRELPNAHFLVEGDVEplSKDGTfvgQHILTPR--RGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 193 PPTQGAVSCLHMVHCFHLAG-FPKGLISCITGKGSEIGDFLTMHpavNCISFTG-GDTGISISKKAGM----IPLQMELG 266
Cdd:cd07128 179 PATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQ---DVVAFTGsAATAAKLRAHPNIvarsIRFNAEAD 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 267 GKDACI-----VLDDADLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVG-PPEENSDITAVV 340
Cdd:cd07128 256 SLNAAIlgpdaTPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGdPRLEGVRMGPLV 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 341 S----ESSANFIEGLVMDAK----------------EKGATFCqeykregnliwPLLLDNVRPDMRIAWE--EPFGPVVP 398
Cdd:cd07128 336 SreqrEDVRAAVATLLAEAEvvfggpdrfevvgadaEKGAFFP-----------PTLLLCDDPDAATAVHdvEAFGPVAT 404
|
330 340
....*....|....*....|....*....
gi 15224111 399 VLRINSVEEGINHCNASNFGLQGCVFTKD 427
Cdd:cd07128 405 LMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
77-330 |
3.84e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 87.07 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 77 RAELLHKAAAILKDNKAPMAESLVKEIAKPAKDSVTEVVRSGDLISYCAEEGvRILGEGKFLL---------SDSFPGnd 147
Cdd:PRK11903 65 RAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLG-AALGDARLLRdgeavqlgkDPAFQG-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 148 rtKYCLTSKipLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAG-FPKGLISCITGKGs 226
Cdd:PRK11903 142 --QHVLVPT--RGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 227 eiGDFLTMHPAVNCISFTG-GDTGISISKKAGMIP----LQMELGGKDACIVLDDAD-----LDLVASNIIKGGFSYSGQ 296
Cdd:PRK11903 217 --AGLLDHLQPFDVVSFTGsAETAAVLRSHPAVVQrsvrVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQ 294
|
250 260 270
....*....|....*....|....*....|....
gi 15224111 297 RCTAVKVVLVMESVADELVEKVKAKVAKLTVGPP 330
Cdd:PRK11903 295 KCTAIRRIFVPEALYDAVAEALAARLAKTTVGNP 328
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
60-456 |
6.34e-18 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 85.74 E-value: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 60 ELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKE----IAKPAKDSVTEVVRSGD-LIS-YCAEEGV---- 129
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSErgayIRSLIANWIAMMGCSESkLYKnIDTERGItasv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 130 -RILGEgkfLLSDSFPgndrtkyCLTSKIPLGVVLAIPPFNYPVnLAVSKIAPALIAGNSLVLKPPTQGAVS--CLHMVH 206
Cdd:cd07077 81 gHIQDV---LLPDNGE-------TYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTnrALALLF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 207 CFHLA-GFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGDTGISISKKAG-MIPLqMELGGKDACIVLDDADLDLVAS 284
Cdd:cd07077 150 QAADAaHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSpHIPV-IGFGAGNSPVVVDETADEERAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 285 NIIKGGFSYSGQRCTAVKVVLVMESVADELVEKVKAKVAKLTVGPPEEnsditavvsessANFIEGLVMDAKEKGATfcq 364
Cdd:cd07077 229 GSVHDSKFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQE------------TKPLSKETTPSFDDEAL--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 365 eykregnliwpllldnvrpdmriaweEPFGPVVPVLR----INSVEEGINHCNASNFGLQGCVFTKDINKAILISDAMET 440
Cdd:cd07077 294 --------------------------ESMTPLECQFRvldvISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDT 347
|
410
....*....|....*.
gi 15224111 441 GTVQINSAPARGPDHF 456
Cdd:cd07077 348 ASFYPNESSKKGRGAF 363
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
53-409 |
3.59e-15 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 77.64 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 53 EEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKE---------IAK--------PAKDSVTEVV 115
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEEtgmgrvedkIAKnvaaaektPGVEDLTTEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 116 RSGD----LISYCaeegvrilgegkfllsdsfpgndrtkycltskiPLGVVLAIPPFNYP----VNLAVSKIApaliAGN 187
Cdd:PRK15398 116 LTGDngltLIEYA---------------------------------PFGVIGAVTPSTNPtetiINNAISMLA----AGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 188 SLVLKPPTQGAVSCLHMVHCFHLA----GFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG----DTGISISKK---A 256
Cdd:PRK15398 159 SVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGpavvKAAMKSGKKaigA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 257 GmiplqmelGGKDACIVLDDADLDLVASNIIKGG-FSYSgQRCTAVKVVLVMESVADELVEK-VKAKVAKLTvgpPEENS 334
Cdd:PRK15398 239 G--------AGNPPVVVDETADIEKAARDIVKGAsFDNN-LPCIAEKEVIVVDSVADELMRLmEKNGAVLLT---AEQAE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 335 DITAVVSE-----------SSANFIeglvmdAKEKGATFCQEYKregnliwpLLLDNVRPDMRIAWEEPFGPVVPVLRIN 403
Cdd:PRK15398 307 KLQKVVLKnggtvnkkwvgKDAAKI------LEAAGINVPKDTR--------LLIVETDANHPFVVTELMMPVLPVVRVK 372
|
....*.
gi 15224111 404 SVEEGI 409
Cdd:PRK15398 373 DVDEAI 378
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
22-329 |
2.94e-14 |
|
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: 74.84 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 22 GEWKTSSsgKSVAIMNPATRKTQYKVQACTQEEVNAVMELAKSAQKSWAKTPLwKRAE-------LLHKAAAILKdnKAP 94
Cdd:cd07126 5 GKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPL-KNPEryllygdVSHRVAHELR--KPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 95 MAESLVKEIAKPAKDS----VTEVVRSGDLISYCAEEGVRILGEGkFLLSDSFPGNDRTKYcltsKIPLGVVLAIPPFNY 170
Cdd:cd07126 80 VEDFFARLIQRVAPKSdaqaLGEVVVTRKFLENFAGDQVRFLARS-FNVPGDHQGQQSSGY----RWPYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 171 PVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVHCFHLAGFPKGLISCITGKGSEIGDFLT-MHPAVncISFTGGDTg 249
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANPRM--TLFTGSSK- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 250 isISKKagmipLQMELGGKdacIVLDDA------------DLDLVASNIIKGGFSYSGQRCTAVKVVLVMESVADE-LVE 316
Cdd:cd07126 232 --VAER-----LALELHGK---VKLEDAgfdwkilgpdvsDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILD 301
|
330
....*....|....*...
gi 15224111 317 KVKA-----KVAKLTVGP 329
Cdd:cd07126 302 KLKAlaeqrKLEDLTIGP 319
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
53-410 |
3.20e-14 |
|
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: 74.58 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 53 EEVNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKE---------IAK--------PAKDSVTEVV 115
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEEtgmgrvedkIAKnhlaaektPGTEDLTTTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 116 RSGD----LISYCaeegvrilgegkfllsdsfpgndrtkycltskiPLGVVLAIPPFNYP----VNLAVSKIApaliAGN 187
Cdd:cd07121 84 WSGDngltLVEYA---------------------------------PFGVIGAITPSTNPtetiINNSISMLA----AGN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 188 SLVLKPPTQGAVSCLHMVHCFHLA----GFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGG----DTGISISKKA-GM 258
Cdd:cd07121 127 AVVFNPHPGAKKVSAYAVELINKAiaeaGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGpavvKAALSSGKKAiGA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 259 IPlqmelgGKDACIVLDDADLDLVASNIIKGGfSYSGQ-RCTAVKVVLVMESVADELVEKVKA------------KVAKL 325
Cdd:cd07121 207 GA------GNPPVVVDETADIEKAARDIVQGA-SFDNNlPCIAEKEVIAVDSVADYLIAAMQRngayvlndeqaeQLLEV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 326 TVGPPEENSDITAVVSESSANFIE--GLVMDAKEKgatfcqeykregnliwpLLLDNVRPDMRIAWEEPFGPVVPVLRIN 403
Cdd:cd07121 280 VLLTNKGATPNKKWVGKDASKILKaaGIEVPADIR-----------------LIIVETDKDHPFVVEEQMMPILPVVRVK 342
|
....*..
gi 15224111 404 SVEEGIN 410
Cdd:cd07121 343 NFDEAIE 349
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
55-452 |
4.60e-14 |
|
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: 74.22 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 55 VNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDNKAPMAESLVKEIAKP-AKDSVTEVVRSGDLI--SYCAEEGVRI 131
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGrVEDKVIKNHFAAEYIynVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 132 LGEgkfllsdsfpgnDRTKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKP------PTQGAVSCLhmV 205
Cdd:cd07081 81 LTG------------DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprakkVTQRAATLL--L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 206 HCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGGDTGISISKKAGMiPLQMELGGKDACIVLDDADLDLVASN 285
Cdd:cd07081 147 QAAVAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGK-PAIGVGAGNTPVVIDETADIKRAVQS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 286 IIKGGFSYSGQRCTAVKVVLVMESVADELVE--------KVKAKVAKLTVGPPEENSDITAVVSESSANFIEGLVmdake 357
Cdd:cd07081 226 IVKSKTFDNGVICASEQSVIVVDSVYDEVMRlfegqgayKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIAAAA----- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 358 kGATFCQEYKregnliwpLLLDNVrpdMRIAWEEPFG-----PVVPVLRINSVEEGINHC----NASNFGLQGCVFTKDI 428
Cdd:cd07081 301 -GLKVPQETR--------ILIGEV---TSLAEHEPFAheklsPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNI 368
|
410 420
....*....|....*....|....*..
gi 15224111 429 N---KAILISDAMETGTVQINSAPARG 452
Cdd:cd07081 369 KaieNMNQFANAMKTSRFVKNGPCSQG 395
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
55-324 |
1.89e-12 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 69.11 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 55 VNAVMELAKSAQKSWAKTPLWKRAELLHK-AAAI--LKDNKAPMAES--------LVKEIAKpakdsvT--------EVV 115
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAiADEIeaLGDELVARAHAetglpearLQGELGR------TtgqlrlfaDLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 116 RSGDlisycaEEGVRI---LGEGKFLlsdsfPGNDRTKYcltsKIPLGVVLAIPPFNYPvnLAVSKI----APALIAGNS 188
Cdd:cd07129 75 REGS------WLDARIdpaDPDRQPL-----PRPDLRRM----LVPLGPVAVFGASNFP--LAFSVAggdtASALAAGCP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 189 LVLK-----PPTQGAVSCLhMVHCFHLAGFPKGLISCITGKGSEIGDFLTMHPAVNCISFTGgdtgisiSKKAGM----- 258
Cdd:cd07129 138 VVVKahpahPGTSELVARA-IRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTG-------SRRGGRalfda 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 259 -------IPLQMELGGKDACIVLDDA------DL--DLVASniIKGGfsySGQRCTAVKVVLVMESVA-DELVEKVKAKV 322
Cdd:cd07129 210 aaarpepIPFYAELGSVNPVFILPGAlaergeAIaqGFVGS--LTLG---AGQFCTNPGLVLVPAGPAgDAFIAALAEAL 284
|
..
gi 15224111 323 AK 324
Cdd:cd07129 285 AA 286
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
157-409 |
5.84e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 61.34 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 157 IPLGVVLAI-----PPFN-YPVNLAvskiapALIAGNSLVLKPpTQGAVSCLHMV-----HCFHLAGFPKGLISCIT-GK 224
Cdd:cd07127 192 VPRGVALVIgcstfPTWNgYPGLFA------SLATGNPVIVKP-HPAAILPLAITvqvarEVLAEAGFDPNLVTLAAdTP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 225 GSEIGDFLTMHPAVNCISFTGGDT-GISISKKAGMIPLQMELGGKDACIVLDDADLDLVASNIikgGFS---YSGQRCTA 300
Cdd:cd07127 265 EEPIAQTLATRPEVRIIDFTGSNAfGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNL---AFSlslYSGQMCTT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 301 VKVVLVMES---------VADELVEKVKAKVAKLTVGPPEENSDITAVVSESSANFIE-----GLVMDAKEKGA--TFCQ 364
Cdd:cd07127 342 PQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAearqlGEVLLASEAVAhpEFPD 421
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15224111 365 EYKREgnliwPLLLDNVRPDMRIAWEEPFGPVVPVLRINSVEEGI 409
Cdd:cd07127 422 ARVRT-----PLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSI 461
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
158-320 |
7.61e-10 |
|
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: 60.97 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNSLVLKPPTQGAVSCLHMVH----CFHLAGFPKGLISCITGKGSEIGDFLT 233
Cdd:cd07122 95 PVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKimreAAVAAGAPEGLIQWIEEPSIELTQELM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 234 MHPAVNCISFTGGdtgisiskkAGMI--------PlqmELG---GKDACIVLDDADLDLVASNIIKG-GFSYsGQRCTAV 301
Cdd:cd07122 175 KHPDVDLILATGG---------PGMVkaayssgkP---AIGvgpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASE 241
|
170
....*....|....*....
gi 15224111 302 KVVLVMESVADELVEKVKA 320
Cdd:cd07122 242 QSVIVDDEIYDEVRAELKR 260
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
55-445 |
3.38e-07 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 52.44 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 55 VNAVMELAKSAQKSWAKTPLWKRAELLHKAAAILKDnkaPMAESLVKEIAKPAKDSVTEVVRSGdlisycaeegvriLGE 134
Cdd:pfam05893 6 LEEILDLLERAAKLWADPNYSKRHIETLAQITGYSE---AMLNYLKSLMAFCRRRNLQNVLESE-------------LGQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 135 GKFLlsDSFpgnDRTKYCLTSKIPLGVVLAIPPFNYPVnLAVSKIAPALIAGNSLVLKPPT--QGAVSCLHMVHCFHLAG 212
Cdd:pfam05893 70 PFIL--DEW---LPTKPSYEKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSsdPFTAAALLASFADLDPT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 213 FP-KGLISCITGKGS--EIGDFLTMHpAVNCISFTGGDTGISISKKAG----MI----PLQMELGGKDACIvldDADLDL 281
Cdd:pfam05893 144 HPlADSLSVVYWDGGstQLEDLIVAN-ADVVIAWGGEDAINAIRECLKpgkqWIdfgaKISFAVVDREAAL---DKAAER 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 282 VASNIIKggfsYSGQRCTAVKVVLVM---ESVADELVEKVKAKVAKLTVGPPeensdiTAVVSESSANFIEGLVMDAKEK 358
Cdd:pfam05893 220 AADDICV----FDQQACLSPQTVFVEsddKITPDEFAERLAAALAKRARILP------KAVLDIDEAAKISSDRAECKLD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 359 gATFCQEYKREG--NLIWPLLLDNVRPDMriawEEPFGPVVPVLRINSVEEGINHCNASNFGLQGCVFTKDINKAILISD 436
Cdd:pfam05893 290 -YAFAGERGVWSdfHQRWTVIWSDGQEEL----NSPLNRTVNVVPVPSLSDVVRYVSENRTYLQTCGLAPYSGRLPYLDR 364
|
....*....
gi 15224111 437 AMETGTVQI 445
Cdd:pfam05893 365 KLALAGVSR 373
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
158-450 |
1.57e-03 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 41.32 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 158 PLGVVLAIPPFNYPVNLAVSKiapALIA---GNSLVLKPPTQGAVSCLHMVHCFH----LAGFPKGLISCITGKGSEIGD 230
Cdd:PRK13805 108 PVGVIAGITPTTNPTSTAIFK---ALIAlktRNPIIFSFHPRAQKSSIAAAKIVLdaavAAGAPKDIIQWIEEPSVELTN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 231 FLTMHPAVNCISFTGGdtgisiskkAGMI--------PlqmELG---GKDACIVLDDADLDLVASNII--KgGFSYsGQR 297
Cdd:PRK13805 185 ALMNHPGIALILATGG---------PGMVkaayssgkP---ALGvgaGNVPAYIDKTADIKRAVNDILlsK-TFDN-GMI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 298 CTAVKVVLVMESVADELVEKV------------KAKVAKLTVGPpeENSDITAVVSESSANFIeglvmdAKEKGATFCQE 365
Cdd:PRK13805 251 CASEQAVIVDDEIYDEVKEEFashgayflnkkeLKKLEKFIFGK--ENGALNADIVGQSAYKI------AEMAGFKVPED 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224111 366 YKregnliwpLLLDNVRpdmRIAWEEPFG-----PVVPVLRINSVEEGINHCNA-SNFGLQG---CVFTKDINKAILISD 436
Cdd:PRK13805 323 TK--------ILIAEVK---GVGESEPLSheklsPVLAMYKAKDFEDAVEKAEKlVEFGGLGhtaVIYTNDDELIKEFGL 391
|
330
....*....|....
gi 15224111 437 AMETGTVQINSaPA 450
Cdd:PRK13805 392 RMKACRILVNT-PS 404
|
|
| |
