|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
10-480 |
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: 707.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSeSGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAA-EGHERSELLHRWAEELEKMTDE 88
Cdd:cd07082 2 FKYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 89 IGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDAFPGAsKSTKAMVQKVPHGVVLAISPYNYPVNLAA 168
Cdd:cd07082 81 VANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGT-KGKIAQVRREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 169 SKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKK 248
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 249 ASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSED-A 327
Cdd:cd07082 240 HPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNgV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 328 DITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQE-KNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEK 406
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREgGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651991267 407 RNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVLN 480
Cdd:cd07082 400 KSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-481 |
0e+00 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 546.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 6 DNDLYHTLVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKM 85
Cdd:PLN00412 12 DGDVYKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 86 TDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLR--THGSFIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYP 163
Cdd:PLN00412 92 KAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRilGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 164 VNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGtDTGQ 243
Cdd:PLN00412 172 VNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 244 HIAKKASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS 323
Cdd:PLN00412 251 AISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 324 SEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVD 403
Cdd:PLN00412 331 EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIH 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 404 LEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVLNL 481
Cdd:PLN00412 411 HCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIGSQGITNSINMMTKVKSTVINL 488
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
10-481 |
0e+00 |
|
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: 542.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEI 89
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 90 GYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRthgsfIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAAS 169
Cdd:COG1012 86 AALLTLETGKPLAEARGEVDRAADFLRYYAGEARR-----LYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 170 KIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA 249
Cdd:COG1012 161 KLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 250 S--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSED 326
Cdd:COG1012 241 AenLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDpLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 327 ADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQ----QEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAV 402
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRrpdgEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651991267 403 DLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVLNL 481
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
18-475 |
4.40e-178 |
|
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: 507.07 E-value: 4.40e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 18 WVGSESgETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREV 97
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 98 GKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDafpgasKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALIT 177
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD------PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 178 GNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVV 255
Cdd:pfam00171 154 GNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAqnLKRVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 256 LELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSS-EDADITPMID 334
Cdd:pfam00171 234 LELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLdPDTDMGPLIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 335 QKSADYVTSLIDDAKSKGAVVVHEGQQEK---NLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYG 411
Cdd:pfam00171 314 KAQLERVLKYVEDAKEEGAKLLTGGEAGLdngYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651991267 412 LQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDK 475
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
50-479 |
9.79e-164 |
|
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: 469.77 E-value: 9.79e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 50 DRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRthgsf 129
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 130 IQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGV 209
Cdd:cd07078 76 LHGEVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 210 LNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYS 287
Cdd:cd07078 156 LNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAaeNLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 288 GQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNLL 366
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 367 G----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKT 442
Cdd:cd07078 316 GyfvpPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 651991267 443 SRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVL 479
Cdd:cd07078 396 VGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
29-479 |
3.80e-147 |
|
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: 428.17 E-value: 3.80e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAI---RQTADVQENWEAaegHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGK 105
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIaaaKEGAKEMKSLPA---YERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 106 SEVKRTAQLIRHTAEEGLRTHGSFIQGDAFPGaSKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKP 185
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDASPG-GEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 186 ATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKASMIPVVLELGGKDPAI 265
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 266 VLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVG-RSSEDADITPMIDQKSADYVTSL 344
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGdPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 345 IDDAKSKGAVVVHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENA 424
Cdd:cd07149 319 VEEAVEGGARLLTGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 651991267 425 FALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVL 479
Cdd:cd07149 399 LKAARELEVGGVMINDSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
27-479 |
7.81e-144 |
|
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: 419.83 E-value: 7.81e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 27 VKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKS 106
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 107 EVKRTAQLIRHTAEEGLRTHGSFIQGDAFPGASKSTkAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPA 186
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRI-AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 187 TQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGGKDPA 264
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAggTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 265 IVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADITPMIDQKSADYVTS 343
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 344 LIDDAKSKGAVVVHEGQ-QEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLE 422
Cdd:cd07145 320 LVNDAVEKGGKILYGGKrDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDIN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 651991267 423 NAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVL 479
Cdd:cd07145 400 RALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
48-460 |
1.06e-142 |
|
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: 416.16 E-value: 1.06e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 48 EVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHG 127
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 128 SFIQGDaFPGasksTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVS-GLMMVEALVNAGLP 206
Cdd:cd07104 81 EILPSD-VPG----KESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 207 EGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGAL 284
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGrhLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 285 SYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEK 363
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDpRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 364 NLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTS 443
Cdd:cd07104 316 LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTV 395
|
410
....*....|....*..
gi 651991267 444 RGPDHFPFLGVKNSGQG 460
Cdd:cd07104 396 NDEPHVPFGGVKASGGG 412
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
10-460 |
1.28e-137 |
|
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: 404.71 E-value: 1.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSESGEtvKIYSPDD-HELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDE 88
Cdd:cd07097 1 YRNYIDGEWVAGGDGE--ENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 89 IGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGsfiqgDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAA 168
Cdd:cd07097 79 LARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSG-----ETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 169 SKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKK 248
Cdd:cd07097 154 WKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 249 AS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SE 325
Cdd:cd07097 234 AAarGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAlDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQ-----QEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFE 400
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGErlkrpDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 651991267 401 AVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSrGPD-HFPFLGVKNSGQG 460
Cdd:cd07097 394 ALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTA-GVDyHVPFGGRKGSSYG 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
14-439 |
1.10e-134 |
|
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: 397.02 E-value: 1.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMI 93
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 94 HREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDafpgaSKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAP 173
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSD-----RPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 174 ALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--M 251
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAenI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 252 IPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVG-RSSEDADIT 330
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGdPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 331 PMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNLLG----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEK 406
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGyfyePTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430
....*....|....*....|....*....|...
gi 651991267 407 RNAYGLQASIFTKNLENAFALSDKLNVGTVQVN 439
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
29-479 |
3.86e-133 |
|
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: 392.49 E-value: 3.86e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAaegHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEV 108
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYRSTLTR---YQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAEEGLRTHGSFIQGDAFPGAsKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQ 188
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFSCDLTANG-KARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 189 GAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKASMIPVVLELGGKDPAIVLD 268
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 269 DADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDA-DITPMIDQKSADYVTSLIDD 347
Cdd:cd07146 239 DADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPAtDMGTVIDEEAAIQIENRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 348 AKSKGAVVVHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFAL 427
Cdd:cd07146 319 AIAQGARVLLGNQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 651991267 428 SDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGV-QGIGRSIDSMLRDKVLVL 479
Cdd:cd07146 399 VERLDVGTVNVNEVPGFRSELSPFGGVKDSGLGGkEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
30-475 |
1.68e-132 |
|
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: 390.92 E-value: 1.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 30 YSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVK 109
Cdd:cd07150 4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 110 RTAQLIRHTAEEGLRTHGSFIQGDaFPGasksTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQG 189
Cdd:cd07150 84 FTPELLRAAAGECRRVRGETLPSD-SPG----TVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 190 AVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVL 267
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGrhLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 268 DDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGrSSEDAD--ITPMIDQKSADYVTSLI 345
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVG-DPRDPDtvIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 346 DDAKSKGAVVVHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAF 425
Cdd:cd07150 318 EDAVAKGAKLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 651991267 426 ALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDK 475
Cdd:cd07150 398 KLAERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
29-479 |
1.27e-130 |
|
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: 386.02 E-value: 1.27e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEV 108
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAEEGLRTHGSFIQGDAFPGaSKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQ 188
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIPLDATQG-SDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 189 GAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKASMIPVVLELGGKDPAIVLD 268
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 269 DADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADITPMIDQKSADYVTSLIDD 347
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVERWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 348 AKSKGAVVVHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFAL 427
Cdd:cd07094 322 AVEAGARLLCGGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 651991267 428 SDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVL 479
Cdd:cd07094 402 AEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
29-463 |
3.02e-130 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 384.86 E-value: 3.02e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEV 108
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAEEGLRTHGSFIqgdafPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQ 188
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTI-----PSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 189 GAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIV 266
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAAdtVKRVSLELGGNAPFIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 267 LDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTSLI 345
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNgLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 346 DDAKSKGAVVVHEGQQ---EKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLE 422
Cdd:cd07103 316 EDAVAKGAKVLTGGKRlglGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 651991267 423 NAFALSDKLNVGTVQVNGKTSRGPDhFPFLGVKNSGQGVQG 463
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAE-APFGGVKESGLGREG 435
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
60-479 |
8.91e-130 |
|
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: 380.81 E-value: 8.91e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 60 QENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRthgsfIQGDAFPGAS 139
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADK-----LGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 140 KSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSV 219
Cdd:cd06534 82 PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 220 IGDFVVTHPKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRV 297
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAaeNLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 298 MVVDSVADELVAKLKekvaalkvgrssedaditpmidqksadyvtsliddakskgavvvhegqqeknllgpTVLDSVTED 377
Cdd:cd06534 242 LVHESIYDEFVEKLV--------------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 378 MRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNS 457
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVKNS 345
|
410 420
....*....|....*....|..
gi 651991267 458 GQGVQGIGRSIDSMLRDKVLVL 479
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
27-479 |
5.48e-123 |
|
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: 366.57 E-value: 5.48e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 27 VKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKS 106
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 107 EVKRTAQLIRHTAEEGLRTHGSFIQGDAFPgASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPA 186
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPLDISA-RGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 187 TQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSvIGDFVVTHPKVDMITFTGGTDTGQHIAKKASMIPVVLELGGKDPAIV 266
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCSRD-DADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 267 LDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDA-DITPMIDQKSADYVTSLI 345
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDAtDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 346 DDAKSKGAVVVHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAF 425
Cdd:cd07147 319 NEAVDAGAKLLTGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKAL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 651991267 426 ALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVL 479
Cdd:cd07147 399 RAWDELEVGGVVINDVPTFRVDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
16-460 |
4.80e-122 |
|
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: 364.70 E-value: 4.80e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 16 NKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHR 95
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 96 EVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDAfPGasKSTKamVQKVPHGVVLAISPYNYPVNLAASKIAPAL 175
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDV-PG--KENR--VYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 176 ITGNTVVFKPATQGAVS-GLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MI 252
Cdd:cd07151 156 ALGNAVVLKPASDTPITgGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGrhLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 253 PVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE-DADITP 331
Cdd:cd07151 236 KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDpDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 332 MIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYG 411
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEGATLLVGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYG 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 651991267 412 LQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQG 460
Cdd:cd07151 396 LSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHVPFGGEKNSGLG 444
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
29-462 |
7.21e-122 |
|
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: 363.39 E-value: 7.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEV 108
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAEEGLRTHgsFIQGDAfpgaskSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQ 188
Cdd:cd07106 81 GGAVAWLRYTASLDLPDE--VIEDDD------TRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 189 GAVSGLMMVEaLVNAGLPEGVLNVVTGRGSViGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIV 266
Cdd:cd07106 153 TPLCTLKLGE-LAQEVLPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAktLKRVTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 267 LDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSED-ADITPMIDQKSADYVTSLI 345
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPgTTLGPVQNKMQYDKVKELV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 346 DDAKSKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLE 422
Cdd:cd07106 311 EDAKAKGAKVLAGGEPLDGpgyFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLE 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 651991267 423 NAFALSDKLNVGTVQVNGKTSRGPdHFPFLGVKNSGQGVQ 462
Cdd:cd07106 391 RAEAVARRLEAGTVWINTHGALDP-DAPFGGHKQSGIGVE 429
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
48-477 |
7.73e-118 |
|
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: 352.65 E-value: 7.73e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 48 EVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAeeglrTHG 127
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAA-----SLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 128 SFIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFK-----PATQGAVsglmmVEALVN 202
Cdd:cd07105 76 TQIIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKaselsPRTHWLI-----GRVFHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 203 AGLPEGVLNVVTGRGSVIGDFV---VTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAK 277
Cdd:cd07105 151 AGLPKGVLNVVTHSPEDAPEVVealIAHPAVRKVNFTGSTRVGRIIAETAAkhLKPVLLELGGKAPAIVLEDADLDAAAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 278 EIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGrsseDADITPMIDQKSADYVTSLIDDAKSKGAVVVH 357
Cdd:cd07105 231 AALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG----PVVLGSLVSAAAADRVKELVDDALSKGAKLVV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 358 EGQQEKNLLG----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNV 433
Cdd:cd07105 307 GGLADESPSGtsmpPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIES 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 651991267 434 GTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVL 477
Cdd:cd07105 387 GAVHINGMTVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
32-475 |
6.51e-117 |
|
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: 351.08 E-value: 6.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 32 PDDHELAGSVPALSQEEVDRAIR--QTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVK 109
Cdd:cd07114 4 PATGEPWARVPEASAADVDRAVAaaRAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 110 RTAQLIRHTAeeGL-RThgsfIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQ 188
Cdd:cd07114 84 YLAEWYRYYA--GLaDK----IEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 189 GAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIV 266
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAenLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 267 LDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDA-DITPMIDQKSADYVTSLI 345
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPEtQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 346 DDAKSKGAVVVHEGQQ-EKNLLG------PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFT 418
Cdd:cd07114 318 ARAREEGARVLTGGERpSGADLGagyffePTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 651991267 419 KNLENAFALSDKLNVGTVQVNGKTSRGPdHFPFLGVKNSGQGVQGIGRSIDSMLRDK 475
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSP-SSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
30-478 |
1.90e-115 |
|
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: 347.29 E-value: 1.90e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 30 YSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVK 109
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 110 RTAQLIRH---TAEEGLRTHGSfiqgdAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPA 186
Cdd:cd07099 81 LALEAIDWaarNAPRVLAPRKV-----PTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 187 TQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSViGDFVVTHpKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGGKDPA 264
Cdd:cd07099 156 EVTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDA-GVDKVAFTGSVATGRKVMAAAaeRLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 265 IVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVG-RSSEDADITPMIDQKSADYVTS 343
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGaDDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 344 LIDDAKSKGAVVVHEGQQEK---NLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKN 420
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSNgggPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 651991267 421 LENAFALSDKLNVGTVQVNGKTSRGPDH-FPFLGVKNSGQGVQGIGRSIDSMLRDKVLV 478
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPaLPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
13-460 |
5.41e-115 |
|
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: 347.03 E-value: 5.41e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKIYSP-DDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGY 91
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 92 MIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGsfiqgDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKI 171
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFG-----ETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 172 APALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA-- 249
Cdd:cd07131 157 FPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCar 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 250 SMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDAD 328
Cdd:cd07131 237 PNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGlDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 329 ITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQ-------EKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEA 401
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltgggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 651991267 402 VDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQG 460
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNG 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
14-466 |
3.71e-113 |
|
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: 341.86 E-value: 3.71e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQEN--WEAAEGHERSELLHRWAEELEKMTDEIGY 91
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 92 MIHREVGKTLS-SGKSEVKRTAQLIRHTAEeglrthgsFIQGDAF----PGASKSTkAMVQKVPHGVVLAISPYNYPVNL 166
Cdd:cd07139 83 LWTAENGMPISwSRRAQGPGPAALLRYYAA--------LARDFPFeerrPGSGGGH-VLVRREPVGVVAAIVPWNAPLFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 167 AASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGrGSVIGDFVVTHPKVDMITFTGGTDTGQHIA 246
Cdd:cd07139 154 AALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 247 KKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSS 324
Cdd:cd07139 233 AVCGerLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 325 EDA-DITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNLLG-----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNE 398
Cdd:cd07139 313 DPAtQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRgwfvePTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651991267 399 FEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGktsRGPD-HFPFLGVKNSgqgvqGIGR 466
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNG---FRLDfGAPFGGFKQS-----GIGR 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
13-480 |
1.24e-112 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 341.67 E-value: 1.24e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 IHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIqgdafPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIA 172
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDII-----PSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 173 PALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS-- 250
Cdd:PLN02278 183 PALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAat 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 251 MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADI 329
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGfEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 330 TPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEK---NLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEK 406
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSlggTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651991267 407 RNAYGLQASIFTKNLENAFALSDKLNVGTVQVN-GKTSRgpDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVLN 480
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNeGLIST--EVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLG 495
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
30-461 |
5.90e-112 |
|
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: 338.07 E-value: 5.90e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 30 YSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVK 109
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 110 RTAQLIRH---TAEEGLRTHGsfiqgdafPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPA 186
Cdd:cd07102 81 GMLERARYmisIAEEALADIR--------VPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 187 TQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDfVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPA 264
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAA-LIADPRIDHVSFTGSVAGGRAIQRAAAgrFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 265 IVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE-DADITPMIDQKSADYVTS 343
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDpSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 344 LIDDAKSKGAVVVHEGQ------QEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIF 417
Cdd:cd07102 312 QIADAIAKGARALIDGAlfpedkAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 651991267 418 TKNLENAFALSDKLNVGTVQVNGKTSRGPDhFPFLGVKNSGQGV 461
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPA-LAWTGVKDSGRGV 434
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
36-460 |
1.06e-108 |
|
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: 329.64 E-value: 1.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 36 ELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLI 115
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 116 RHTAeeGLRTHGsfiQGDAFPGASKSTkAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVS-GL 194
Cdd:cd07152 82 HEAA--GLPTQP---QGEILPSAPGRL-SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSgGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 195 MMVEALVNAGLPEGVLNVVTGrGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADL 272
Cdd:cd07152 156 VIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGrhLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 273 DKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTSLIDDAKSK 351
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDpATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 352 GAVVVHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKL 431
Cdd:cd07152 315 GARLEAGGTYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRL 394
|
410 420
....*....|....*....|....*....
gi 651991267 432 NVGTVQVNGKTSRGPDHFPFLGVKNSGQG 460
Cdd:cd07152 395 RTGMLHINDQTVNDEPHNPFGGMGASGNG 423
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
13-460 |
1.06e-108 |
|
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: 330.71 E-value: 1.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAA--EGHERSELLHRWAEELEKMTDEIG 90
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 91 YMIHREVGKTLS-SGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDafpgasKSTKAMVQKVPHGVVLAISPYNYPVNLAAS 169
Cdd:cd07091 87 ALESLDNGKPLEeSAKGDVALSIKCLRYYAGWADKIQGKTIPID------GNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 170 KIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA 249
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 250 S---MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGrSSED 326
Cdd:cd07091 241 AksnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG-DPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 327 ADIT--PMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEA 401
Cdd:cd07091 320 PDTFqgPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSkgyFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 402 VDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNgkTSRGPDHF-PFLGVKNSGQG 460
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN--TYNVFDAAvPFGGFKQSGFG 457
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
29-460 |
1.27e-108 |
|
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: 329.58 E-value: 1.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQE-NWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSE 107
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 108 VKRTAQLIR---HTAEEglrthgsfIQGDAFPGASKSTKAMVqKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFK 184
Cdd:cd07109 81 VEAAARYFEyygGAADK--------LHGETIPLGPGYFVYTV-REPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 185 PATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKD 262
Cdd:cd07109 152 PAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAenVVPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 263 PAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDADITPMIDQKSADYVT 342
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 343 SLIDDAKSKGAVVVHEGQQEKNLLG------PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASI 416
Cdd:cd07109 312 GFVARARARGARIVAGGRIAEGAPAggyfvaPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 651991267 417 FTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQG 460
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGGGIELPFGGVKKSGHG 435
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
49-460 |
3.57e-108 |
|
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: 327.49 E-value: 3.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 49 VDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGlrthGS 128
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENA----EA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 129 FIQGDAFPGASKstKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEG 208
Cdd:cd07100 77 FLADEPIETDAG--KAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 209 VL-NVVTGRGSVigDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALS 285
Cdd:cd07100 155 VFqNLLIDSDQV--EAIIADPRVRGVTLTGSERAGRAVAAEAGknLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 286 YSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQ---Q 361
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDpMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKrpdG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 362 EKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGK 441
Cdd:cd07100 313 PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM 392
|
410
....*....|....*....
gi 651991267 442 TSRGPDhFPFLGVKNSGQG 460
Cdd:cd07100 393 VKSDPR-LPFGGVKRSGYG 410
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
29-466 |
4.70e-107 |
|
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: 325.67 E-value: 4.70e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKS-E 107
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 108 VKRTAQ-------LIRHTAEEGLRTHGSFIqgdafpgaskstkAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNT 180
Cdd:cd07093 81 IPRAAAnfrffadYILQLDGESYPQDGGAL-------------NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 181 VVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLEL 258
Cdd:cd07093 148 VVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAApnLKPVSLEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 259 GGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKS 337
Cdd:cd07093 228 GGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDpLDPDTEVGPLISKEH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 338 ADYVTSLIDDAKSKGAVVV-----HEGQQEK--NLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAY 410
Cdd:cd07093 308 LEKVLGYVELARAEGATILtgggrPELPDLEggYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPY 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 651991267 411 GLQASIFTKNLENAFALSDKLNVGTVQVNgktsrgpDHF------PFLGVKNSgqgvqGIGR 466
Cdd:cd07093 388 GLAAYVWTRDLGRAHRVARRLEAGTVWVN-------CWLvrdlrtPFGGVKAS-----GIGR 437
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
29-463 |
6.73e-107 |
|
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: 325.35 E-value: 6.73e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWE-AAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKS- 106
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 107 EVKRTAQLIRHTAEEGLRTHGSFIQGDAFPGASKSTkAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPA 186
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGR-RVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 187 TQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPA 264
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAatLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 265 IVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTS 343
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDpADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 344 LIDDAKSKGAVVVHEGQQEKNLLG-----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFT 418
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPAGLDKgfyvePTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 651991267 419 KNLENAFALSDKLNVGTVQVNGKTSRGPDHfPFLGVKNSGQGVQG 463
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDA-PFGGYKQSGLGREN 443
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
19-464 |
7.49e-106 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 324.91 E-value: 7.49e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 19 VGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVG 98
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 99 KTLSSGKSEVKRTAQLIRH---TAEEGLRTHGsfIQGdAFPGASKSTkamVQKVPHGVVLAISPYNYPVNLAASKIAPAL 175
Cdd:PRK09407 106 KARRHAFEEVLDVALTARYyarRAPKLLAPRR--RAG-ALPVLTKTT---ELRQPKGVVGVISPWNYPLTLAVSDAIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 176 ITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHpkVDMITFTGGTDTGQHIAKKAS--MIP 253
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGrrLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 254 VVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE-DADITPM 332
Cdd:PRK09407 258 FSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDySADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 333 IDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNlLG-----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKR 407
Cdd:PRK09407 338 ISEAQLETVSAHVDDAVAKGATVLAGGKARPD-LGplfyePTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAND 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 408 NAYGLQASIFTKNLENAFALSDKLNVGTVQVNgktsrgpDHF---------PFLGVKNSG----QGVQGI 464
Cdd:PRK09407 417 TPYGLNASVWTGDTARGRAIAARIRAGTVNVN-------EGYaaawgsvdaPMGGMKDSGlgrrHGAEGL 479
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
14-481 |
1.40e-103 |
|
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: 317.81 E-value: 1.40e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQEN-WEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 IHREVGKTLSSG-KSEVKRTAQLIRHTAeeglrthGSF--IQGDAFPGASKSTkAMVQKVPHGVVLAISPYNYPVNLAAS 169
Cdd:cd07144 92 EALDSGKPYHSNaLGDLDEIIAVIRYYA-------GWAdkIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 170 KIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA 249
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 250 S--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVA-ALKVGRS-SE 325
Cdd:cd07144 244 AqnLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPfDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNLLG------PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEF 399
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGkgyfipPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 400 EAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNgkTSRGPD-HFPFLGVKNSgqgvqGIGR-----SIDSMLR 473
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWIN--SSNDSDvGVPFGGFKMS-----GIGRelgeyGLETYTQ 476
|
....*...
gi 651991267 474 DKVLVLNL 481
Cdd:cd07144 477 TKAVHINL 484
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
13-464 |
1.52e-103 |
|
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: 317.54 E-value: 1.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:cd07085 4 FINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 IHREVGKTLSSGKSEVKRTAQLIRHTAeeGLRTHgsfIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIA 172
Cdd:cd07085 84 ITLEHGKTLADARGDVLRGLEVVEFAC--SIPHL---LKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 173 PALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIgDFVVTHPKVDMITFTGGTDTGQHIAKKASMI 252
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 253 --PVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSS-EDADI 329
Cdd:cd07085 238 gkRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDdPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 330 TPMIDQKSADYVTSLIDDAKSKGAVVV-------HEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAV 402
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVldgrgvkVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 403 DLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNS------GQGVQGI 464
Cdd:cd07085 398 AIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSffgdlhFYGKDGV 465
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
31-470 |
1.96e-103 |
|
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: 316.56 E-value: 1.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 31 SPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKR 110
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 111 TAQLIRH---TAEEGLRTHGsfiQGDAFPGASKSTkamVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPAT 187
Cdd:cd07101 82 VAIVARYyarRAERLLKPRR---RRGAIPVLTRTT---VNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 188 QGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHpkVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAI 265
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGrrLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 266 VLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE-DADITPMIDQKSADYVTSL 344
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDyGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 345 IDDAKSKGAVVVHEGQQEKNL----LGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKN 420
Cdd:cd07101 314 VDDAVAKGATVLAGGRARPDLgpyfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 651991267 421 LENAFALSDKLNVGTVQVNG--KTSRGPDHFPFLGVKNSG----QGVQGIGRSIDS 470
Cdd:cd07101 394 GARGRRIAARLRAGTVNVNEgyAAAWASIDAPMGGMKDSGlgrrHGAEGLLKYTET 449
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-472 |
7.24e-103 |
|
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: 315.07 E-value: 7.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTL-SSGKSE 107
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 108 VKRTAQLIRHTAeeGLrthGSFIQGDAFPGASkSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPAT 187
Cdd:cd07108 81 AAVLADLFRYFG--GL---AGELKGETLPFGP-DVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 188 QGAVSGLMMVEaLVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAI 265
Cdd:cd07108 155 DAPLAVLLLAE-ILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAdrLIPVSLELGGKSPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 266 VLDDADLDKTAKEIVSGA-LSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADITPMIDQKSADYVTS 343
Cdd:cd07108 234 VFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 344 LIDDAKS-KGAVVVHEGQQEKNL-------LGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQAS 415
Cdd:cd07108 314 YIDLGLStSGATVLRGGPLPGEGpladgffVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 651991267 416 IFTKNLENAFALSDKLNVGTVQVNGKTSRGPDhFPFLGVKNSgqgvqGIGR--SIDSML 472
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQGGGQQPG-QSYGGFKQS-----GLGReaSLEGML 446
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
24-460 |
8.53e-103 |
|
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: 314.93 E-value: 8.53e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 24 GETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQEN--WEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTL 101
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 102 S-SGKSEVKRTAQLIRHTAEEGLRthgsfIQGDAFPGASKSTkAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNT 180
Cdd:cd07112 81 SdALAVDVPSAANTFRWYAEAIDK-----VYGEVAPTGPDAL-ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 181 VVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS---MIPVVLE 257
Cdd:cd07112 155 VVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqsnLKRVWLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 258 LGGKDPAIVLDDA-DLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADITPMIDQ 335
Cdd:cd07112 235 CGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPlDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 336 KSADYVTSLIDDAKSKGAVVVHEGQQEKNLLG-----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAY 410
Cdd:cd07112 315 AHFDKVLGYIESGKAEGARLVAGGKRVLTETGgffvePTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 651991267 411 GLQASIFTKNLENAFALSDKLNVGTVQVNGkTSRGPDHFPFLGVKNSGQG 460
Cdd:cd07112 395 GLAASVWTSDLSRAHRVARRLRAGTVWVNC-FDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
29-460 |
3.55e-102 |
|
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: 313.11 E-value: 3.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKS-E 107
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 108 VKRTAQLIRHTAEeGLRTHGSFIQGDAFPGASkstkAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPAT 187
Cdd:cd07092 81 LPGAVDNFRFFAG-AARTLEGPAAGEYLPGHT----SMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 188 QGAVSGLMMVEaLVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAI 265
Cdd:cd07092 156 TTPLTTLLLAE-LAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAdtLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 266 VLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTSL 344
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDpDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 345 IDDAKsKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNL 421
Cdd:cd07092 315 VERAP-AHARVLTGGRRAEGpgyFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 651991267 422 ENAFALSDKLNVGTVQVNgktsrgpDHFPFL------GVKNSGQG 460
Cdd:cd07092 394 GRAMRLSARLDFGTVWVN-------THIPLAaemphgGFKQSGYG 431
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
10-460 |
3.57e-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: 314.93 E-value: 3.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVgsESGETVKIYSP-DDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDE 88
Cdd:cd07124 33 YPLVIGGKEV--RTEEKIESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 89 IGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGsFIQGDAFPGASKSTKamvqkVPHGVVLAISPYNYPVNLAA 168
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRG-FPVEMVPGEDNRYVY-----RPLGVGAVISPWNFPLAILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 169 SKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKK 248
Cdd:cd07124 185 GMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 249 ASMI--------PVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKV 320
Cdd:cd07124 265 AAKVqpgqkwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 321 GRSSE-DADITPMIDQKSADYVTSLIDDAKSKGAVV----VHEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRI 395
Cdd:cd07124 345 GDPEDpEVYMGPVIDKGARDRIRRYIEIGKSEGRLLlggeVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKA 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 651991267 396 SNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGK-TSRGPDHFPFLGVKNSGQG 460
Cdd:cd07124 425 KDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKiTGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
14-466 |
3.83e-102 |
|
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: 313.29 E-value: 3.83e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMI 93
Cdd:cd07138 3 IDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 94 HREVGKTLS-SGKSEVKRTAQLIRHTAEeGLRThgsfiqgdaFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIA 172
Cdd:cd07138 83 TLEMGAPITlARAAQVGLGIGHLRAAAD-ALKD---------FEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 173 PALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS-- 250
Cdd:cd07138 153 PALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAdt 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 251 MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDAD-I 329
Cdd:cd07138 233 VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATtL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 330 TPMIDQKSADYVTSLIDDAKSKGAVVVH------EGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVD 403
Cdd:cd07138 313 GPLASAAQFDRVQGYIQKGIEEGARLVAggpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651991267 404 LEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKtsrGPD-HFPFLGVKNSgqgvqGIGR 466
Cdd:cd07138 393 IANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGA---AFNpGAPFGGYKQS-----GNGR 448
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
14-468 |
2.95e-101 |
|
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: 311.55 E-value: 2.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIR--QTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGY 91
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAaaRRAFDSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 92 MIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGdafPGASKStkaMVQKVPHGVVLAISPYNYPVNLAASKI 171
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV---PPHVIS---RTVREPVGVCGLITPWNYPLLQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 172 APALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS- 250
Cdd:cd07119 156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 251 -MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDAD 328
Cdd:cd07119 236 nVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGlDADTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 329 ITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQ--EKNL-----LGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEA 401
Cdd:cd07119 316 MGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRptGDELakgyfVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651991267 402 VDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNgktSRGP--DHFPFLGVKNSgqgvqGIGRSI 468
Cdd:cd07119 396 IRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN---DYHPyfAEAPWGGYKQS-----GIGREL 456
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
13-460 |
1.27e-99 |
|
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: 307.18 E-value: 1.27e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSeSGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 IHREVGKTLSSGKSEVkrtaQLIRHTAE--EGL-RThgsfIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAAS 169
Cdd:cd07086 81 VSLEMGKILPEGLGEV----QEMIDICDyaVGLsRM----LYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 170 KIAPALITGNTVVFKPATQGAVSGL----MMVEALVNAGLPEGVLNVVTGRGSViGDFVVTHPKVDMITFTGGTDTGQHI 245
Cdd:cd07086 153 NAAIALVCGNTVVWKPSETTPLTAIavtkILAEVLEKNGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVGRRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 246 AKK--ASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS 323
Cdd:cd07086 232 GETvaRRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 324 SEDA-DITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEK-----NLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISN 397
Cdd:cd07086 312 LDEGtLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDggepgNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651991267 398 EFEAVDLEKRNAYGLQASIFTKNLENAF-ALSDK-LNVGTVQVNGKTSRGPDHFPFLGVKNSGQG 460
Cdd:cd07086 392 LEEAIAINNDVPQGLSSSIFTEDLREAFrWLGPKgSDCGIVNVNIPTSGAEIGGAFGGEKETGGG 456
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
10-460 |
3.61e-98 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 303.37 E-value: 3.61e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSEsGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEI 89
Cdd:PRK13473 3 TKLLINGELVAGE-GEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 90 GYMIHREVGKTLSSGKS-EVKRTAQLIRHTAEEGLRTHGSfIQGDAFPGASkstkAMVQKVPHGVVLAISPYNYPVNLAA 168
Cdd:PRK13473 82 ARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGK-AAGEYLEGHT----SMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 169 SKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAgLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKK 248
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 249 A--SMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSE 325
Cdd:PRK13473 236 AadSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDpDDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNLLG----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEA 401
Cdd:PRK13473 316 DTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGyyyePTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651991267 402 VDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNgktsrgpDHFPFL------GVKNSGQG 460
Cdd:PRK13473 396 VRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVN-------THFMLVsemphgGQKQSGYG 453
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-481 |
1.24e-97 |
|
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: 301.60 E-value: 1.24e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEV 108
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAEEGLRTHGSFIqgdAFPGASKStkaMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQ 188
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETI---PVGGRNLH---YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 189 GAVSGLMMVEaLVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIV 266
Cdd:cd07107 155 APLSALRLAE-LAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAegIKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 267 LDDADLDKTAKEIVSGA-LSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTSL 344
Cdd:cd07107 234 FPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDpTDPATTMGPLVSRQQYDRVMHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 345 IDDAKSKGAVVVHEGQQEKN-------LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIF 417
Cdd:cd07107 314 IDSAKREGARLVTGGGRPEGpaleggfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIW 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 651991267 418 TKNLENAFALSDKLNVGTVQVNGkTSRgpdHF---PFLGVKNSGQGVQGIGRSIDSMLRDKVLVLNL 481
Cdd:cd07107 394 TNDISQAHRTARRVEAGYVWING-SSR---HFlgaPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-481 |
1.17e-95 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 297.20 E-value: 1.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 IHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRthgsfIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIA 172
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKR-----IYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 173 PALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTG-QHIAKKASM 251
Cdd:PRK11241 169 PALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGrQLMEQCAKD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 252 I-PVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDADIT 330
Cdd:PRK11241 249 IkKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 331 -PMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEK---NLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEK 406
Cdd:PRK11241 329 gPLIDEKAVAKVEEHIADALEKGARVVCGGKAHElggNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 651991267 407 RNAYGLQASIFTKNLENAFALSDKLNVGTVQVN-GKTSRgpDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVLNL 481
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINtGIISN--EVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
31-460 |
3.19e-95 |
|
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: 295.40 E-value: 3.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 31 SPDDHELAGSVPALSQEEVDRAI---RQTADvQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSE 107
Cdd:cd07118 3 SPAHGVVVARYAEGTVEDVDAAVaaaRKAFD-KGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 108 VKRTAQLIRHTAEEGLRTHGsfiqgDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPAT 187
Cdd:cd07118 82 IEGAADLWRYAASLARTLHG-----DSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 188 QGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGGKDPAI 265
Cdd:cd07118 157 FTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAarNLKKVSLELGGKNPQI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 266 VLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADITPMIDQKSADYVTSL 344
Cdd:cd07118 237 VFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPlDPETKVGAIINEAQLAKITDY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 345 IDDAKSKGAVVVHEGQQEKNLLG----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKN 420
Cdd:cd07118 317 VDAGRAEGATLLLGGERLASAAGlfyqPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 651991267 421 LENAFALSDKLNVGTVQVNGKTSRGPDhFPFLGVKNSGQG 460
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDGSPE-LPFGGFKQSGIG 435
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
31-481 |
8.79e-93 |
|
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: 288.95 E-value: 8.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 31 SPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKS-EVK 109
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 110 RTAQLIRHTAEEGLRTHGSFIQGDAfpgaskSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQG 189
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRG------PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 190 AVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVL 267
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAgnLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 268 DDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDA-DITPMIDQKSADYVTSLID 346
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKtQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 347 DAKSKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLEN 423
Cdd:cd07115 317 VGREEGARLLTGGKRPGArgfFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 424 AFALSDKLNVGTVQVN--GKTSRGPdhfPFLGVKNSGQGVQGIGRSIDSMLRDKVLVLNL 481
Cdd:cd07115 397 AHRVAAALKAGTVWINtyNRFDPGS---PFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
10-474 |
9.94e-93 |
|
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: 289.63 E-value: 9.94e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEI 89
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 90 GymihreVGKTLSSGKSeVKRT---------------AQLIRhtAEEGlrthgSFIQGDafpgasKSTKAMVQKVPHGVV 154
Cdd:cd07559 81 A------VAETLDNGKP-IRETlaadiplaidhfryfAGVIR--AQEG-----SLSEID------EDTLSYHFHEPLGVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 155 LAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEaLVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMIT 234
Cdd:cd07559 141 GQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLME-LIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 235 FTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDA-----DLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADEL 307
Cdd:cd07559 220 FTGSTTVGRLIMQYAAenLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 308 VAKLKEKVAALKVGRSSEDAdiTPM---IDQKSADYVTSLIDDAKSKGAVVVHEGQ--QEKNLLG-----PTVLDSVTED 377
Cdd:cd07559 300 IERAVERFEAIKVGNPLDPE--TMMgaqVSKDQLEKILSYVDIGKEEGAEVLTGGErlTLGGLDKgyfyePTLIKGGNND 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 378 MRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRgPDHFPFLGVKNS 457
Cdd:cd07559 378 MRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQY-PAHAPFGGYKKS 456
|
490
....*....|....*..
gi 651991267 458 gqgvqGIGRSIDSMLRD 474
Cdd:cd07559 457 -----GIGRETHKMMLD 468
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
14-470 |
6.13e-92 |
|
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: 287.89 E-value: 6.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQT-ADVQENW-EAAEGHERSELLHRWAEELEKMTDEIGY 91
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAhAAFETDWgLKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 92 MIHREVGKTLSSGKS-EVKRTAQLIRHTAEEGLRTHGSFIQGDAfpgaskSTKAMVQKVPHGVVLAISPYNYPVNLAASK 170
Cdd:cd07143 91 IEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIETDI------KKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 171 IAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHI---AK 247
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVmeaAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 248 KASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SED 326
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPfAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 327 ADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNL---LGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVD 403
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEgyfIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 651991267 404 LEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPdHFPFLGVKNSgqgvqGIGRSIDS 470
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHH-QVPFGGYKQS-----GIGRELGE 465
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
29-463 |
7.13e-91 |
|
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: 284.20 E-value: 7.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEV 108
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAEEGLRTHGSFIQ--GDAFpgaskstkAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPA 186
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPlpGGSF--------AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 187 TQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSViGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPA 264
Cdd:cd07090 153 PFTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAkgIKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 265 IVLDDADLDktakEIVSGALS---YS-GQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADITPMIDQKSAD 339
Cdd:cd07090 232 IIFDDADLE----NAVNGAMManfLSqGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPlDEDTQMGALISEEHLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 340 YVTSLIDDAKSKGAVV------VHEGQQEKN--LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYG 411
Cdd:cd07090 308 KVLGYIESAKQEGAKVlcggerVVPEDGLENgfYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 651991267 412 LQASIFTKNLENAFALSDKLNVGTVQVNgKTSRGPDHFPFLGVKNSGQGVQG 463
Cdd:cd07090 388 LAAGVFTRDLQRAHRVIAQLQAGTCWIN-TYNISPVEVPFGGYKQSGFGREN 438
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
30-460 |
5.50e-90 |
|
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: 282.27 E-value: 5.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 30 YSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGK-SEV 108
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAEEGLRThgsfIQGDAFPGAS-KSTK-AMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPA 186
Cdd:cd07098 81 LVTCEKIRWTLKHGEKA----LRPESRPGGLlMFYKrARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 187 TQGAVSGL----MMVEALVNAGLPEGVLNVVTGRGSViGDFVVTHPKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGG 260
Cdd:cd07098 157 EQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAaeSLTPVVLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 261 KDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSAD 339
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPpLDGDVDVGAMISPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 340 YVTSLIDDAKSKGAVVV-------HEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGL 412
Cdd:cd07098 316 RLEELVADAVEKGARLLaggkrypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 651991267 413 QASIFTKNLENAFALSDKLNVGTVQVN--GKTSRGPDhFPFLGVKNSGQG 460
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINdfGVNYYVQQ-LPFGGVKGSGFG 444
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
10-474 |
2.45e-89 |
|
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: 280.88 E-value: 2.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEI 89
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 90 GYMIHREVGKTLSSGKS-EVKRTAQLIRHTAEEGLRTHGSFIQGDafpgasKSTKAMVQKVPHGVVLAISPYNYPVNLAA 168
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMID------EDTLSIVLREPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 169 SKIAPALITGNTVVFKPATQGAVSgLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKK 248
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLS-LLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 249 AS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSED 326
Cdd:cd07117 234 AAkkLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 327 AdiTPM---IDQKSADYVTSLIDDAKSKGAVVVHEGQQ-------EKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRIS 396
Cdd:cd07117 314 D--TQMgaqVNKDQLDKILSYVDIAKEEGAKILTGGHRltengldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 397 NEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNgKTSRGPDHFPFLGVKNSgqgvqGIGRSIDSMLRD 474
Cdd:cd07117 392 TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN-TYNQIPAGAPFGGYKKS-----GIGRETHKSMLD 463
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
30-460 |
3.54e-89 |
|
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: 279.61 E-value: 3.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 30 YSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHE-RSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEV 108
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRlRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAEEGLRTHGSFIQGDafPGasksTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQ 188
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPE--PG----SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 189 GAVSGLMMVEALVNA-GLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGGKDPAI 265
Cdd:cd07120 156 TAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAapTLKRLGLELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 266 VLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE-DADITPMIDQKSADYVTSL 344
Cdd:cd07120 236 VFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDpASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 345 IDDAKSKGAVVVH------EGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFT 418
Cdd:cd07120 316 VERAIAAGAEVVLrggpvtEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 651991267 419 KNLENAFALSDKLNVGTVQVNgKTSRGPDHFPFLGVKNSGQG 460
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWIN-DWNKLFAEAEEGGYRQSGLG 436
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
29-466 |
6.67e-89 |
|
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: 278.85 E-value: 6.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 29 IYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEV 108
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 109 KRTAQLIRHTAE--EGLRTHgsfiQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPA 186
Cdd:cd07110 81 DDVAGCFEYYADlaEQLDAK----AERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 187 TQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPA 264
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAqdIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 265 IVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADITPMIDQKSADYVTS 343
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPlEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 344 LIDDAKSKGAVVVHEGQQEKNL-----LGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFT 418
Cdd:cd07110 317 FIARGKEEGARLLCGGRRPAHLekgyfIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 651991267 419 KNLENAFALSDKLNVGTVQVNGKTSRGPdHFPFLGVKNSgqgvqGIGR 466
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFP-QAPWGGYKRS-----GIGR 438
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
14-460 |
1.60e-87 |
|
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: 276.15 E-value: 1.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAI---RQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIG 90
Cdd:cd07141 11 INNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVkaaRAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 91 YMihrevgKTLSSGK-------SEVKRTAQLIRHTAEEGLRTHGSFI--QGDAFpgaskstkAMVQKVPHGVVLAISPYN 161
Cdd:cd07141 91 SL------ETLDNGKpfsksylVDLPGAIKVLRYYAGWADKIHGKTIpmDGDFF--------TYTRHEPVGVCGQIIPWN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 162 YPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDT 241
Cdd:cd07141 157 FPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 242 GQHI---AKKASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAAL 318
Cdd:cd07141 237 GKLIqqaAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 319 KVGRSSE-DADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGPVLPIMR 394
Cdd:cd07141 317 VVGNPFDpKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDkgyFIQPTVFSDVTDDMRIAKEEIFGPVQQIFK 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 651991267 395 ISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPdHFPFLGVKNSGQG 460
Cdd:cd07141 397 FKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSP-QAPFGGYKMSGNG 461
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
13-479 |
3.92e-87 |
|
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: 275.14 E-value: 3.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIR--QTADVQENWEAAEGHERSELLHRWAEELEKMTDEIG 90
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKaaRKAFDEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 91 YMIHREVGKTLSSGK-SEVKRTAQLIRHTAEEGLRTHGSFIQGDAfpgaskSTKAMVQKVPHGVVLAISPYNYPVNLAAS 169
Cdd:cd07142 87 ALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADG------PHHVYTLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 170 KIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHI---A 246
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIImqlA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 247 KKASMIPVVLELGGKDPAIVLDDADLDKtAKEIVSGALSYS-GQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-S 324
Cdd:cd07142 241 AKSNLKPVTLELGGKSPFIVCEDADVDK-AVELAHFALFFNqGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPfR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 325 EDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEA 401
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSkgyYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 402 VDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDhFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVL 479
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDAS-IPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
14-460 |
7.06e-87 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 273.99 E-value: 7.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMI 93
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 94 HREVGKTLS-SGKSEVKRTAQLIRHTAEEGLRTHGSFIQgdaFPGASKstkAMVQKVPHGVVLAISPYNYPVNLAASKIA 172
Cdd:TIGR01804 82 TLDTGKTLQeTIVADMDSGADVFEFFAGLAPALNGEIIP---LGGPSF---AYTIREPLGVCVGIGAWNYPLQIASWKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 173 PALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS-- 250
Cdd:TIGR01804 156 PALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAgh 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 251 MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS-SEDADI 329
Cdd:TIGR01804 236 LKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPfDEATEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 330 TPMIDQKSADYVTSLIDDAKSKGAVVV-------HEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAV 402
Cdd:TIGR01804 316 GPLISAAHRDKVLSYIEKGKAEGATLAtgggrpeNVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 403 DLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNgKTSRGPDHFPFLGVKNSGQG 460
Cdd:TIGR01804 396 ARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWIN-TYNLYPAEAPFGGYKQSGIG 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
4-463 |
6.64e-84 |
|
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: 266.95 E-value: 6.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 4 RQDNDLYHtLVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELE 83
Cdd:cd07111 17 AHDRSFGH-FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 84 KMTDEIGymihreVGKTLSSGKS-------EVKRTAQLIRHTAEEglrthgsfiqgdafpgASKSTKAMVQKVPHGVVLA 156
Cdd:cd07111 96 KHQRLFA------VLESLDNGKPiresrdcDIPLVARHFYHHAGW----------------AQLLDTELAGWKPVGVVGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 157 ISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSViGDFVVTHPKVDMITFT 236
Cdd:cd07111 154 IVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 237 GGTDTGQHIAKK--ASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEK 314
Cdd:cd07111 233 GSTEVGRALRRAtaGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 315 VAALKVGRSSEDA-DITPMIDQKSADYVTSLIDDAKSKGAVVVHEG---QQEKNLLGPTVLDSVTEDMRVAWEEQFGPVL 390
Cdd:cd07111 313 MSHLRVGDPLDKAiDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGadlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVL 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651991267 391 PIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHfPFLGVKNSGQGVQG 463
Cdd:cd07111 393 VVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAA-GFGGYRESGFGREG 464
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
10-465 |
1.46e-83 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 266.73 E-value: 1.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSEsGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEI 89
Cdd:TIGR01237 33 YPLVINGERVETE-NKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 90 GYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDaFPGasKSTKAMVQkvPHGVVLAISPYNYPVNLAAS 169
Cdd:TIGR01237 112 SALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNS-REG--ETNQYVYT--PTGVTVVISPWNFPFAIMVG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 170 KIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA 249
Cdd:TIGR01237 187 MTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 250 SMIP--------VVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVG 321
Cdd:TIGR01237 267 AKVQpgqkhlkrVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 322 RSSE-DADITPMIDQKSADYVTSLIDDAKSKGAVVV-HEGQQEKN-LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNE 398
Cdd:TIGR01237 347 PPDSaDVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSgGCGDDSKGyFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 399 FEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGK-TSRGPDHFPFLGVKNSGQGVQGIG 465
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNiTGAIVGYQPFGGFKMSGTDSKAGG 494
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
14-460 |
4.10e-83 |
|
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: 264.69 E-value: 4.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADV-QENWEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 ihrevgKTLSSGKS-------EVKRTAQLIRHTAEEGLRTHGSFIQgDAFPG-ASKSTKAMVQKVPHGVVLAISPYNYPV 164
Cdd:cd07113 84 ------ETLCSGKSihlsrafEVGQSANFLRYFAGWATKINGETLA-PSIPSmQGERYTAFTRREPVGVVAGIVPWNFSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 165 NLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSViGDFVVTHPKVDMITFTGGTDTGQH 244
Cdd:cd07113 157 MIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 245 IAKKA--SMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR 322
Cdd:cd07113 236 IGRQAasDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 323 S-SEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQ---QEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNE 398
Cdd:cd07113 316 PmDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEalaGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 651991267 399 FEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDhFPFLGVKNSGQG 460
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPA-VPFGGMKQSGIG 456
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
14-460 |
1.12e-82 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 264.38 E-value: 1.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQEN--WEAAEGHERSELLHRWAEELEKMTDEIGY 91
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 92 MIHREVGKTLSSGKS-EVKRTAQLIRHTAEEGLRTHGSFIQgdafpgASKSTKAMVQKVPHGVVLAISPYNYPVNLAASK 170
Cdd:PLN02766 105 LDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLK------MSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 171 IAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHI---AK 247
Cdd:PLN02766 179 VAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKImqaAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 248 KASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE-D 326
Cdd:PLN02766 259 TSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDpR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 327 ADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVD 403
Cdd:PLN02766 339 ARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDkgyYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIK 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 651991267 404 LEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDhFPFLGVKNSGQG 460
Cdd:PLN02766 419 KANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPD-CPFGGYKMSGFG 474
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
75-439 |
1.24e-82 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 261.21 E-value: 1.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 75 LHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDAfPGASkstkAMVQKVPHGVV 154
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDR-PGEN----ILLFKRALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 155 LAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMIT 234
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 235 FTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLK 312
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAknITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 313 EKVAALKVGRSSE--DADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFG 387
Cdd:PRK10090 236 EAMQAVQFGNPAErnDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGkgyYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 651991267 388 PVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVN 439
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
10-423 |
6.73e-81 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 259.87 E-value: 6.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVgsESGETVKIYSP-DDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDE 88
Cdd:PRK03137 37 YPLIIGGERI--TTEDKIVSINPaNKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 89 I-GYMIHrEVGKTLSSGKSEVKRTAQLIRHTAEEGLR-THGSFIQgdAFPGASKSTKAMvqkvPHGVVLAISPYNYPVNL 166
Cdd:PRK03137 115 FsAWLVK-EAGKPWAEADADTAEAIDFLEYYARQMLKlADGKPVE--SRPGEHNRYFYI----PLGVGVVISPWNFPFAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 167 AASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIA 246
Cdd:PRK03137 188 MAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 247 KKASMIP--------VVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAAL 318
Cdd:PRK03137 268 ERAAKVQpgqiwlkrVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 319 KVGRSSEDADITPMIDQKSADYVTSLIDDAKSKGAVVV--HEGQQEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRIS 396
Cdd:PRK03137 348 TVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLggEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427
|
410 420
....*....|....*....|....*..
gi 651991267 397 NEFEAVDLEKRNAYGLQASIFTKNLEN 423
Cdd:PRK03137 428 DFDHALEIANNTEYGLTGAVISNNREH 454
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
22-460 |
1.35e-80 |
|
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: 259.44 E-value: 1.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 22 ESGETVKIYSPDDHE-LAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDE-IGYMIhREVGK 99
Cdd:cd07125 43 ETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGElIALAA-AEAGK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 100 TLSSGKSEVKRTAQLIRHTAEEgLRTHGSfiqGDAFPGASKSTKaMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGN 179
Cdd:cd07125 122 TLADADAEVREAIDFCRYYAAQ-ARELFS---DPELPGPTGELN-GLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 180 TVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKASM-----IPV 254
Cdd:cd07125 197 TVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgpiLPL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 255 VLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE-DADITPMI 333
Cdd:cd07125 277 IAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDlSTDVGPLI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 334 DQKSADYVTSLIDdakskgavvvhEGQQEKNLLGPTVLDSVTEDM---RVAW--------EEQFGPVLPIMRisneFEAV 402
Cdd:cd07125 357 DKPAGKLLRAHTE-----------LMRGEAWLIAPAPLDDGNGYFvapGIIEivgifdltTEVFGPILHVIR----FKAE 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 651991267 403 DLEK----RNA--YGLQASIFTKNLENAFALSDKLNVGTVQVN--------GKTsrgpdhfPFLGVKNSGQG 460
Cdd:cd07125 422 DLDEaiedINAtgYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitgaivGRQ-------PFGGWGLSGTG 486
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
13-481 |
5.89e-79 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 255.50 E-value: 5.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIR--QTADVQENWEAAEGHERSELLHRWAEELEKMTDEIG 90
Cdd:PLN02466 61 LINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAaaRKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 91 YMIHREVGKTLS-SGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDAfpgaskstKAMVQKV--PHGVVLAISPYNYPVNLA 167
Cdd:PLN02466 141 ALETWDNGKPYEqSAKAELPMFARLFRYYAGWADKIHGLTVPADG--------PHHVQTLhePIGVAGQIIPWNFPLLMF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 168 ASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHI-- 245
Cdd:PLN02466 213 AWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVle 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 246 -AKKASMIPVVLELGGKDPAIVLDDADLDKtAKEIVSGALSYS-GQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRS 323
Cdd:PLN02466 293 lAAKSNLKPVTLELGGKSPFIVCEDADVDK-AVELAHFALFFNqGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 324 -SEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQ---EKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEF 399
Cdd:PLN02466 372 fKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRfgsKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLD 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 400 EAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKtsrgpDHF----PFLGVKNSGQGVQGIGRSIDSMLRDK 475
Cdd:PLN02466 452 EVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCF-----DVFdaaiPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
....*.
gi 651991267 476 VLVLNL 481
Cdd:PLN02466 527 AVVTPL 532
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
14-460 |
8.91e-79 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 254.27 E-value: 8.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQ-----TADVQENWEAAEGHERSELLHRWAEELEKMTDE 88
Cdd:PLN02467 12 IGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAarkafKRNKGKDWARTTGAVRAKYLRAIAAKITERKSE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 89 IGYMIHREVGKTLSSGKSEVKRTAQLIRHTAE--EGLrthgsfiqgDAFPGASKST-----KAMVQKVPHGVVLAISPYN 161
Cdd:PLN02467 92 LAKLETLDCGKPLDEAAWDMDDVAGCFEYYADlaEAL---------DAKQKAPVSLpmetfKGYVLKEPLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 162 YPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDT 241
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 242 GQHIAKKASMI--PVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALK 319
Cdd:PLN02467 243 GRKIMTAAAQMvkPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 320 VGRS-SEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNL-----LGPTVLDSVTEDMRVAWEEQFGPVLPIM 393
Cdd:PLN02467 323 ISDPlEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLkkgffIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651991267 394 RISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTsrgP--DHFPFLGVKNSGQG 460
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQ---PcfCQAPWGGIKRSGFG 468
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
23-460 |
1.45e-78 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 252.35 E-value: 1.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 23 SGETVKIYSPddhelagsvpaLSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLS 102
Cdd:PRK09406 10 TGETVKTFTA-----------LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 103 SGKSEVKRTAQLIRHTAEeglrtHGSFIQGD--AFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNT 180
Cdd:PRK09406 79 SAKAEALKCAKGFRYYAE-----HAEALLADepADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 181 VVFKPATQGAVSGLMMVEALVNAGLPEGVL-NVVTGRGSVigDFVVTHPKVDMITFTGGTDTGQHIAKKA--SMIPVVLE 257
Cdd:PRK09406 154 GLLKHASNVPQTALYLADLFRRAGFPDGCFqTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAgdEIKKTVLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 258 LGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDA-DITPMIDQK 336
Cdd:PRK09406 232 LGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDtDVGPLATEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 337 SADYVTSLIDDAKSKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQ 413
Cdd:PRK09406 312 GRDEVEKQVDDAVAAGATILCGGKRPDGpgwFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLG 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 651991267 414 ASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDhFPFLGVKNSGQG 460
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPE-LPFGGVKRSGYG 437
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
27-479 |
1.94e-77 |
|
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: 249.26 E-value: 1.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 27 VKIYSPDDHELAGSVPALSQEEVDRAIrQTADV----QENWEAAegHERSELLHRWAEELEKMTDEIGYMIHREVGKTLS 102
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKAL-DTAHAlfldRNNWLPA--HERIAILERLADLMEERADELALLIAREGGKPLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 103 SGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDAFPgASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVV 182
Cdd:cd07148 78 DAKVEVTRAIDGVELAADELGQLGGREIPMGLTP-ASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 183 FKPATQGAVSGLMMVEALVNAGLPEG-VLNVVTGRGsvIGDFVVTHPKVDMITFTGGTDTGQHI-AKKASMIPVVLELGG 260
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGwCQAVPCENA--VAEKLVTDPRVAFFSFIGSARVGWMLrSKLAPGTRCALEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 261 KDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSS-EDADITPMIDQKSAD 339
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTdPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 340 YVTSLIDDAKSKGAVVVHEGQQ-EKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFT 418
Cdd:cd07148 315 RVEEWVNEAVAAGARLLCGGKRlSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 651991267 419 KNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQGVQGIGRSIDSMLRDKVLVL 479
Cdd:cd07148 395 KDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
14-466 |
2.95e-76 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 247.10 E-value: 2.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMI 93
Cdd:PRK13252 11 IDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 94 HREVGKTLSSGKS-EVKRTAQLIRHTAeeGLRT--HGSFIQ--GDAFpgaskstkAMVQKVPHGVVLAISPYNYPVNLAA 168
Cdd:PRK13252 91 TLDTGKPIQETSVvDIVTGADVLEYYA--GLAPalEGEQIPlrGGSF--------VYTRREPLGVCAGIGAWNYPIQIAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 169 SKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSViGDFVVTHPKVDMITFTGGTDTGQHIAKK 248
Cdd:PRK13252 161 WKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 249 A--SMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSE 325
Cdd:PRK13252 240 AaaSLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDpMDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQ--EKNLLG-----PTVLDSVTEDMRVAWEEQFGPVLPIMRISNE 398
Cdd:PRK13252 320 ATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERltEGGFANgafvaPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 399 FEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVN--GKTsrgPDHFPFLGVKNSgqgvqGIGR 466
Cdd:PRK13252 400 DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINtwGES---PAEMPVGGYKQS-----GIGR 461
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
10-460 |
4.81e-76 |
|
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: 246.64 E-value: 4.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQEN--WEAAEGHERSELLHRWAEELEKMTD 87
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 88 EIGYMihrevgKTLSSG-------KSEVKRTAQLIRHTAEEGLRTHGSFIQ-GDAFPGASKStkaMVQKVPHGVVLAISP 159
Cdd:cd07140 86 ELATI------ESLDSGavytlalKTHVGMSIQTFRYFAGWCDKIQGKTIPiNQARPNRNLT---LTKREPIGVCGIVIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 160 YNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGT 239
Cdd:cd07140 157 WNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGST 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 240 DTGQHIAKKAS---MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVA 316
Cdd:cd07140 237 PIGKHIMKSCAvsnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 317 ALKVGRS-SEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQ---EKNLLGPTVLDSVTEDMRVAWEEQFGPVLPI 392
Cdd:cd07140 317 KMKIGDPlDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQvdrPGFFFEPTVFTDVEDHMFIAKEESFGPIMII 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651991267 393 MRISN-EFEAVdLEKRNA--YGLQASIFTKNLENAFALSDKLNVGTVQVN--GKTSRGPdhfPFLGVKNSGQG 460
Cdd:cd07140 397 SKFDDgDVDGV-LQRANDteYGLASGVFTKDINKALYVSDKLEAGTVFVNtyNKTDVAA---PFGGFKQSGFG 465
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
14-460 |
2.89e-74 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 242.11 E-value: 2.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQEN--WEAAEGHERSELLHRWAEELEKMTDEIGY 91
Cdd:PRK09847 24 INGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 92 MIHREVGKTLS-SGKSEVKRTAQLIRHTAEEGLRTHGsfiqgDAFPGASKSTkAMVQKVPHGVVLAISPYNYPVNLAASK 170
Cdd:PRK09847 104 LETLDTGKPIRhSLRDDIPGAARAIRWYAEAIDKVYG-----EVATTSSHEL-AMIVREPVGVIAAIVPWNFPLLLTCWK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 171 IAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA- 249
Cdd:PRK09847 178 LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 250 --SMIPVVLELGGKDPAIVLDDA-DLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE- 325
Cdd:PRK09847 258 dsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDp 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADITPMIDQKSADYVTSLIDDAKSKGAVVVhEGQQEKN--LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVD 403
Cdd:PRK09847 338 ATTMGTLIDCAHADSVHSFIREGESKGQLLL-DGRNAGLaaAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 651991267 404 LEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSrGPDHFPFLGVKNSGQG 460
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYND-GDMTVPFGGYKQSGNG 472
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
48-458 |
1.29e-69 |
|
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: 228.31 E-value: 1.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 48 EVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLI--------RHTA 119
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIdisikayhERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 120 EEglRTHGSFIQgdafpgaskstkAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEA 199
Cdd:cd07095 81 ER--ATPMAQGR------------AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 200 LVNAGLPEGVLNVVTGRGSViGDFVVTHPKVDMITFTGGTDTGQHIAKKASMIPVV---LELGGKDPAIVLDDADLDKTA 276
Cdd:cd07095 147 WEEAGLPPGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKilaLEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 277 KEIVSGALSYSGQRCTAIKRVMVVDS-VADELVAKLKEKVAALKVGrsSEDADITPM----IDQKSADYVTsLIDDAKSK 351
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIG--APDAEPPFMgpliIAAAAARYLL-AQQDLLAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 352 GAVVVHE---GQQEKNLLGPTVLDsVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALS 428
Cdd:cd07095 303 GGEPLLAmerLVAGTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFL 381
|
410 420 430
....*....|....*....|....*....|
gi 651991267 429 DKLNVGTVQVNGKTSRGPDHFPFLGVKNSG 458
Cdd:cd07095 382 ARIRAGIVNWNRPTTGASSTAPFGGVGLSG 411
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
136-460 |
4.20e-65 |
|
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: 216.24 E-value: 4.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 136 PGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQ-GAVSGLMmvEALVNAGLPEGVLNVVT 214
Cdd:cd07087 86 PLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELaPATSALL--AKLIPKYFDPEAVAVVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 215 GRGSVIGDFVvTHPkVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCT 292
Cdd:cd07087 164 GGVEVATALL-AEP-FDHIFFTGSPAVGKIVMEAAAkhLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 293 AIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDADITPMIDQKSADYVTSLIDDAKskgavVVHEGQ--QEKNLLGPTV 370
Cdd:cd07087 242 APDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK-----VVIGGQvdKEERYIAPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 371 LDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSR-GPDHF 449
Cdd:cd07087 317 LDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHaAIPNL 396
|
330
....*....|.
gi 651991267 450 PFLGVKNSGQG 460
Cdd:cd07087 397 PFGGVGNSGMG 407
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
14-460 |
8.30e-65 |
|
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: 217.45 E-value: 8.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVgsESGETVKIYSPDDH-ELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:cd07083 23 IGGEWV--DTKERMVSVSPFAPsEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 IHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGDAFPGASKSTKAmvqkVPHGVVLAISPYNYPVNLAASKIA 172
Cdd:cd07083 101 LTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFY----VGLGAGVVISPWNFPVAIFTGMIV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 173 PALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS-- 250
Cdd:cd07083 177 APVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAArl 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 251 ------MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSS 324
Cdd:cd07083 257 apgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 325 EDA-DITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKN--LLGPTVLDSVTEDMRVAWEEQFGPVLPIMRI-SNEF- 399
Cdd:cd07083 337 ENGtDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEgyFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYkDDDFa 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 651991267 400 EAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGK-TSRGPDHFPFLGVKNSGQG 460
Cdd:cd07083 417 EALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKiTGALVGVQPFGGFKLSGTN 478
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
14-458 |
2.18e-64 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 215.98 E-value: 2.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVgSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMI 93
Cdd:PRK09457 5 INGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 94 HREVGKTLSSGKSEVK----RTAQLIRHTAEeglRThGSfiQGDAFPGAskstKAMVQKVPHGVVLAISPYNYPVNLAAS 169
Cdd:PRK09457 84 ARETGKPLWEAATEVTaminKIAISIQAYHE---RT-GE--KRSEMADG----AAVLRHRPHGVVAVFGPYNFPGHLPNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 170 KIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGrGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA 249
Cdd:PRK09457 154 HIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 250 SMIP---VVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSV-ADELVAKLKEKVAALKVGRSse 325
Cdd:PRK09457 233 AGQPekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRW-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADITP----MIDQKSADYVTSLIDDAKSKGAVVVHEGQQ---EKNLLGPTVLDsVTEDMRVAWEEQFGPVLPIMRISNE 398
Cdd:PRK09457 311 DAEPQPfmgaVISEQAAQGLVAAQAQLLALGGKSLLEMTQlqaGTGLLTPGIID-VTGVAELPDEEYFGPLLQVVRYDDF 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 399 FEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSG 458
Cdd:PRK09457 390 DEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGASG 449
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
13-443 |
2.37e-64 |
|
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: 215.53 E-value: 2.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSesGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:cd07130 2 VYDGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 IHREVGKTLSSGKSEVkrtaqlirhtaEE---------GL-RThgsfIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNY 162
Cdd:cd07130 80 VSLEMGKILPEGLGEV-----------QEmidicdfavGLsRQ----LYGLTIPSERPGHRMMEQWNPLGVVGVITAFNF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 163 PVNLAASKIAPALITGNTVVFKPATQGAVSGL----MMVEALVNAGLPEGVLNVVTGrGSVIGDFVVTHPKVDMITFTGG 238
Cdd:cd07130 145 PVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 239 TDTGQHIAKK--ASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVA 316
Cdd:cd07130 224 TAVGRQVGQAvaARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 317 ALKVGRSSEDADIT-PMIDQKSADYVTSLIDDAKSKGAVVVHEGQQ---EKNLLGPTVLdSVTEDMRVAWEEQFGPVLPI 392
Cdd:cd07130 304 QVRIGDPLDDGTLVgPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVidgPGNYVEPTIV-EGLSDAPIVKEETFAPILYV 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 651991267 393 MRISNEFEAVDLEKRNAYGLQASIFTKNLENAFAL-----SDklnVGTVQVNGKTS 443
Cdd:cd07130 383 LKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgpkgSD---CGIVNVNIGTS 435
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-474 |
1.60e-62 |
|
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: 210.77 E-value: 1.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 10 YHTLVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEI 89
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 90 GymihreVGKTLSSGKSeVKRT---------------AQLIRhtAEEGlrthgSFIQGDAfpgaskSTKAMVQKVPHGVV 154
Cdd:cd07116 81 A------VAETWDNGKP-VRETlaadiplaidhfryfAGCIR--AQEG-----SISEIDE------NTVAYHFHEPLGVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 155 LAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEaLVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMIT 234
Cdd:cd07116 141 GQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLME-LIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 235 FTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVL------DDADLDKTAKEIVSGALSySGQRCTAIKRVMVVDSVADE 306
Cdd:cd07116 220 FTGETTTGRLIMQYASenIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 307 LVAKLKEKVAALKVGRSsedADITPMID-QKSADY---VTSLIDDAKSKGAVVVHEGqqEKNLLG---------PTVLDS 373
Cdd:cd07116 299 FMERALERVKAIKQGNP---LDTETMIGaQASLEQlekILSYIDIGKEEGAEVLTGG--ERNELGgllgggyyvPTTFKG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 374 vTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRgPDHFPFLG 453
Cdd:cd07116 374 -GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLY-PAHAAFGG 451
|
490 500
....*....|....*....|.
gi 651991267 454 VKNSgqgvqGIGRSIDSMLRD 474
Cdd:cd07116 452 YKQS-----GIGRENHKMMLD 467
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
31-460 |
3.94e-61 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 206.64 E-value: 3.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 31 SPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKR 110
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 111 TAQLIRHTAEEG---LRTHGSFIQgdafpgaskSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPAT 187
Cdd:PRK13968 93 SANLCDWYAEHGpamLKAEPTLVE---------NQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 188 QGAVSGLMMVEALVNAGLPEGVLNVVT----GRGSVIGDfvvthPKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGGK 261
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNadndGVSQMIND-----SRIAAVTVTGSVRAGAAIGAQAgaALKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 262 DPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADY 340
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDpRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 341 VTSLIDDAKSKGAVVVHEGQQ---EKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIF 417
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKiagAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 651991267 418 TKNLENAFALSDKLNVGTVQVNGKTSRGPdHFPFLGVKNSGQG 460
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDA-RVAFGGVKKSGFG 440
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
136-460 |
7.23e-60 |
|
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: 202.84 E-value: 7.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 136 PGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEaLVNAGLPEGVLNVVTG 215
Cdd:cd07135 94 PLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE-LVPKYLDPDAFQVVQG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 216 RGSVIGDfVVTHpKVDMITFTGGTDTGQHIAKKA--SMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTA 293
Cdd:cd07135 173 GVPETTA-LLEQ-KFDKIFYTGSGRVGRIIAEAAakHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 294 IKRVMVVDSVADELVAKLKEKVAALKVGRSSEDADITPMIDQKSADYVTSLIDdaKSKGAVVV-HEGQQEKNLLGPTVLD 372
Cdd:cd07135 251 PDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLD--TTKGKVVIgGEMDEATRFIPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 373 SVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSR-GPDHFPF 451
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHvGVDNAPF 408
|
....*....
gi 651991267 452 LGVKNSGQG 460
Cdd:cd07135 409 GGVGDSGYG 417
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
23-439 |
1.20e-58 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 208.51 E-value: 1.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 23 SGETVKIYSPDDHELA-GSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTL 101
Cdd:PRK11904 560 EGEARPVVSPADRRRVvGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 102 SSGKSEVKRTAQLIRHTAEEGLRThgsFIQGDAFPG-ASKSTKAMVQkvPHGVVLAISPYNYPVNLAASKIAPALITGNT 180
Cdd:PRK11904 640 QDAIAEVREAVDFCRYYAAQARRL---FGAPEKLPGpTGESNELRLH--GRGVFVCISPWNFPLAIFLGQVAAALAAGNT 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 181 VVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHI-----AKKASMIPVV 255
Cdd:PRK11904 715 VIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInrtlaARDGPIVPLI 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 256 LELGGKDPAIVlddadlDKTA------KEIVSGALSYSGQRCTAIkRVMVV-DSVADELVAKLKEKVAALKVGRSSE-DA 327
Cdd:PRK11904 795 AETGGQNAMIV------DSTAlpeqvvDDVVTSAFRSAGQRCSAL-RVLFVqEDIADRVIEMLKGAMAELKVGDPRLlST 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 328 DITPMIDQKSADYVTSLIDDAKSKGAVVVH----EGQQEKNLLGPTV--LDSVtEDMRvawEEQFGPVLPIMRisneFEA 401
Cdd:PRK11904 868 DVGPVIDAEAKANLDAHIERMKREARLLAQlplpAGTENGHFVAPTAfeIDSI-SQLE---REVFGPILHVIR----YKA 939
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 651991267 402 VDLEKR----NA--YGLQASIFTKNLENAFALSDKLNVGTVQVN 439
Cdd:PRK11904 940 SDLDKVidaiNAtgYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
135-460 |
6.75e-58 |
|
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: 197.73 E-value: 6.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 135 FPGaskstKAMVQKVPHGVVLAISPYNYPVNLAaskIAP---ALITGNTVVFKP-ATQGAVSGLMmvEALVNAGLPEGVL 210
Cdd:cd07136 90 FPS-----KSYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPsELTPNTSKVI--AKIIEETFDEEYV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 211 NVVTGRGSVIGDfvVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSG 288
Cdd:cd07136 160 AVVEGGVEENQE--LLDQKFDYIFFTGSVRVGKIVMEAAAkhLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 289 QRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDADITPMIDQKSADYVTSLIDDAKskgavVVHEGQQEKNLL-- 366
Cdd:cd07136 238 QTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGK-----IVFGGNTDRETLyi 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 367 GPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNgktsrgp 446
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN------- 385
|
330 340
....*....|....*....|..
gi 651991267 447 D--------HFPFLGVKNSGQG 460
Cdd:cd07136 386 DtimhlanpYLPFGGVGNSGMG 407
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
142-460 |
4.89e-57 |
|
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: 195.14 E-value: 4.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 142 TKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQG-AVSGLMmvEALVNAGLPEGVLNVVTGrGSVI 220
Cdd:cd07134 92 TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTpHTSAVI--AKIIREAFDEDEVAVFEG-DAEV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 221 GDFVVTHPkVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVM 298
Cdd:cd07134 169 AQALLELP-FDHIFFTGSPAVGKIVMAAAAkhLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 299 VVDSVADELVAKLKEKVAAL--KVGRSSEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQ--QEKNLLGPTVLDSV 374
Cdd:cd07134 248 VHESVKDAFVEHLKAEIEKFygKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQfdAAQRYIAPTVLTNV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 375 TEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSrgpdHF----- 449
Cdd:cd07134 328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVL----HFlnpnl 403
|
330
....*....|.
gi 651991267 450 PFLGVKNSGQG 460
Cdd:cd07134 404 PFGGVNNSGIG 414
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
14-458 |
6.82e-57 |
|
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 274486 Cd Length: 484 Bit Score: 196.09 E-value: 6.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSEsGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMI 93
Cdd:TIGR03240 3 IDGKWRAGQ-GESFASRNPATQEVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 94 HREVGKTLSSGKSEVK----RTAQLIRHTAEeglRTHgsfIQGDAFPGAskstKAMVQKVPHGVVLAISPYNYPVNLAAS 169
Cdd:TIGR03240 82 ARETGKPLWETRTEVAsmigKVAISIKAYHE---RTG---ESENPMPDG----RAVLRHRPHGVVAVFGPYNFPGHLPNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 170 KIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGrGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKA 249
Cdd:TIGR03240 152 HIVPALIAGNTVVFKPSELTPWVAEETVKLWEKAGLPAGVLNLVQG-ARETGVALAAHPQIDGLLFTGSSNTGTLLHRQF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 250 SMIP---VVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSV-ADELVAKLKEKVAALKVGRSSE 325
Cdd:TIGR03240 231 GGRPekiLALEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRLLVPDGAqGDAFLARLVEVAERLTVGAWDA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DAD--ITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQ---EKNLLGPTVLDsVTEDMRVAWEEQFGPVLPIMRISNEFE 400
Cdd:TIGR03240 311 EPQpfMGAVISLRAAQRLLAAQAKLLALGGKSLLEMRQldpGAAFLTPGIID-VTGVAELPDEEHFGPLLQVIRYTDFDE 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 401 AVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSG 458
Cdd:TIGR03240 390 AIAIANNTRFGLSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGASSAAPFGGIGASG 447
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
13-460 |
7.45e-57 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 198.82 E-value: 7.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYM 92
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 93 IHREVGKTLSSGKSEVKRTAQLIRHTAeeGLRThgsFIQGDAFPGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIA 172
Cdd:PLN02419 197 ITTEQGKTLKDSHGDIFRGLEVVEHAC--GMAT---LQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 173 PALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIgDFVVTHPKVDMITFTGGTDTGQHIAKKASMI 252
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 253 PVVLE--LGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSvADELVAKLKEKVAALKVGRSSE-DADI 329
Cdd:PLN02419 351 GKRIQsnMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEpDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 330 TPMIDQKSADYVTSLIDDAKSKGAVVVHEGQ-------QEKNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAV 402
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRdivvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAI 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 403 DLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDHFPFLGVKNSGQG 460
Cdd:PLN02419 510 SIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAG 567
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
20-439 |
1.15e-54 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 197.39 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 20 GSESGETVKIYSPDDH-ELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVG 98
Cdd:PRK11905 562 GDVDGGTRPVLNPADHdDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 99 KTLSSGKSEVKRTAQLIRHTAEEGlrthgsfiqgdafpgasKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITG 178
Cdd:PRK11905 642 KTLANAIAEVREAVDFLRYYAAQA-----------------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAG 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 179 NTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKK-----ASMIP 253
Cdd:PRK11905 705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTlakrsGPPVP 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 254 VVLELGGKDPAIVlddadlDKTA------KEIVSGALSYSGQRCTAIkRVMVV-DSVADELVAKLKEKVAALKVGRSSE- 325
Cdd:PRK11905 785 LIAETGGQNAMIV------DSSAlpeqvvADVIASAFDSAGQRCSAL-RVLCLqEDVADRVLTMLKGAMDELRIGDPWRl 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADITPMIDQKSADYVTSLIDDAKSKGAVV----VHEGQQEKNLLGPTVLDsvTEDMRVAWEEQFGPVLPIMRI-SNEFE 400
Cdd:PRK11905 858 STDVGPVIDAEAQANIEAHIEAMRAAGRLVhqlpLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFkADELD 935
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 651991267 401 AVdLEKRNA--YGLQASIFTKNLENAFALSDKLNVGTVQVN 439
Cdd:PRK11905 936 RV-IDDINAtgYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
135-460 |
1.40e-54 |
|
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: 188.46 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 135 FPGAskstKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFK-----PATqgavSGLMmvEALVNAGLPEGV 209
Cdd:cd07133 90 FLPA----KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKpseftPRT----SALL--AELLAEYFDEDE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 210 LNVVTGRGSVIGDFvvTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYS 287
Cdd:cd07133 160 VAVVTGGADVAAAF--SSLPFDHLLFTGSTAVGRHVMRAAAenLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 288 GQRCTAIKRVMVVDSVADELVAKLKEKVAALkVGRSSEDADITPMIDQKSADYVTSLIDDAKSKGAVVV-----HEGQQE 362
Cdd:cd07133 238 GQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNPDYTSIINERHYARLQGLLEDARAKGARVIelnpaGEDFAA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 363 KNLLGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKT 442
Cdd:cd07133 317 TRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTL 396
|
330
....*....|....*....
gi 651991267 443 SR-GPDHFPFLGVKNSGQG 460
Cdd:cd07133 397 LHvAQDDLPFGGVGASGMG 415
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
71-461 |
4.13e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 186.00 E-value: 4.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 71 RSELLHRWAEELEKMTDEIGYMIHREVGKT--------LSSGKSEVKRT-AQLIRHTAEEGLRTHGSFiqgdaFPGASKs 141
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHpfetkmteVLLTVAEIEHLlKHLDEYLKPEKVDTVGVF-----GPGKSY- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 142 tkamVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQG-AVSGLMmvEALVNAGLPEGVLNVVTGRGSVI 220
Cdd:PTZ00381 105 ----IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSpHTSKLM--AKLLTKYLDPSYVRVIEGGVEVT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 221 GDfvVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVM 298
Cdd:PTZ00381 179 TE--LLKEPFDHIFFTGSPRVGKLVMQAAAenLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 299 VVDSVADELVAKLKEKVAALKVGRSSEDADITPMIDQKSADYVTSLIDDAKSKgavVVHEGQQEKN--LLGPTVLDSVTE 376
Cdd:PTZ00381 257 VHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGK---VVYGGEVDIEnkYVAPTIIVNPDL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 377 DMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSR-GPDHFPFLGVK 455
Cdd:PTZ00381 334 DSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHlLNPNLPFGGVG 413
|
....*.
gi 651991267 456 NSGQGV 461
Cdd:PTZ00381 414 NSGMGA 419
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
23-439 |
1.65e-50 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 185.14 E-value: 1.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 23 SGETVKIYSPDDH-ELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTL 101
Cdd:COG4230 568 SGEARPVRNPADHsDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTL 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 102 SSGKSEVKRTAQLIRHTAEEGLRThgsFIQGDAFPgaskstkamvqkvPHGVVLAISPYNYPvnLA--ASKIAPALITGN 179
Cdd:COG4230 648 PDAIAEVREAVDFCRYYAAQARRL---FAAPTVLR-------------GRGVFVCISPWNFP--LAifTGQVAAALAAGN 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 180 TVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHI-----AKKASMIPV 254
Cdd:COG4230 710 TVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInrtlaARDGPIVPL 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 255 VLELGGKDPAIVlddadlDKTA------KEIVSGALSYSGQRCTAIkRVMVV-DSVADELVAKLKEKVAALKVGRSSE-D 326
Cdd:COG4230 790 IAETGGQNAMIV------DSSAlpeqvvDDVLASAFDSAGQRCSAL-RVLCVqEDIADRVLEMLKGAMAELRVGDPADlS 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 327 ADITPMIDQKSADYVTSLIDDAKSKGAvVVHEGQQEKNLLG-----PTV--LDSVtEDMRvawEEQFGPVLPIMRisneF 399
Cdd:COG4230 863 TDVGPVIDAEARANLEAHIERMRAEGR-LVHQLPLPEECANgtfvaPTLieIDSI-SDLE---REVFGPVLHVVR----Y 933
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 651991267 400 EAVDLEKR----NA--YGLQASIFTKNLENAFALSDKLNVGTVQVN 439
Cdd:COG4230 934 KADELDKVidaiNAtgYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
13-439 |
2.21e-48 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 173.56 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSESGETVKiySPDDHE-LAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGY 91
Cdd:TIGR01238 41 IIGHSYKADGEAQPVT--NPADRRdIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 92 MIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIQGdafpgaskstkamvqkvPHGVVLAISPYNYPVNLAASKI 171
Cdd:TIGR01238 119 LCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVE-----------------SRGVFVCISPWNFPLAIFTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 172 APALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKK--- 248
Cdd:TIGR01238 182 SAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTlaq 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 249 --ASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE- 325
Cdd:TIGR01238 262 reDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLl 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADITPMIDQKSADYVTSLIDDAKSKGAVVVH------EGQQEKNLLGPTV--LDSVTEdmrvAWEEQFGPVLPIMRI-S 396
Cdd:TIGR01238 342 TTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQltlddsRACQHGTFVAPTLfeLDDIAE----LSEEVFGPVLHVVRYkA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 651991267 397 NEFEAVdLEKRNA--YGLQASIFTKNLENAFALSDKLNVGTVQVN 439
Cdd:TIGR01238 418 RELDQI-VDQINQtgYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
21-439 |
2.26e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 173.24 E-value: 2.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 21 SESGETVKIYSPDDH-ELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGK 99
Cdd:PRK11809 655 VAAGEMSPVINPADPrDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 100 TLSSGKSEVKRTAQLIRHTAEEgLRthgsfiqgDAFPGASKStkamvqkvPHGVVLAISPYNYPVNLAASKIAPALITGN 179
Cdd:PRK11809 735 TFSNAIAEVREAVDFLRYYAGQ-VR--------DDFDNDTHR--------PLGPVVCISPWNFPLAIFTGQVAAALAAGN 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 180 TVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKAS--------M 251
Cdd:PRK11809 798 SVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAgrldpqgrP 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 252 IPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVG---RSSedAD 328
Cdd:PRK11809 878 IPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGnpdRLS--TD 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 329 ITPMIDQKSADYVTSLIDDAKSKGAVVVH------EGQQEKNLLGPTV--LDSVTEDMRvaweEQFGPVLPIMRI-SNEF 399
Cdd:PRK11809 956 IGPVIDAEAKANIERHIQAMRAKGRPVFQaarensEDWQSGTFVPPTLieLDSFDELKR----EVFGPVLHVVRYnRNQL 1031
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 651991267 400 EAVdLEKRNA--YGLQASIFTKNLENAFALSDKLNVGTVQVN 439
Cdd:PRK11809 1032 DEL-IEQINAsgYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1072
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
13-417 |
2.26e-44 |
|
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: 163.14 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVgsESGETVKIYSPDDHELA-GSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELE-KMTDEI- 89
Cdd:cd07123 36 VIGGKEV--RTGNTGKQVMPHDHAHVlATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgKYRYELn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 90 -GYMIHRevGKTLssGKSEVKRTAQLIrhtaeEGLRTHGSF---IQGDAFPGASKSTKAMVQKVP-HGVVLAISPYNYPV 164
Cdd:cd07123 114 aATMLGQ--GKNV--WQAEIDAACELI-----DFLRFNVKYaeeLYAQQPLSSPAGVWNRLEYRPlEGFVYAVSPFNFTA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 165 ---NLAAskiAPALItGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDT 241
Cdd:cd07123 185 iggNLAG---APALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 242 GQHIAKK-ASMIP-------VVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKE 313
Cdd:cd07123 261 FKSLWKQiGENLDryrtyprIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 314 KVAALKVGRSSEDAD-ITPMIDQKSADYVTSLIDDAK-SKGAVVVHEGQQEKN---LLGPTVLDSVTEDMRVAWEEQFGP 388
Cdd:cd07123 341 ELKEIKMGDPDDFSNfMGAVIDEKAFDRIKGYIDHAKsDPEAEIIAGGKCDDSvgyFVEPTVIETTDPKHKLMTEEIFGP 420
|
410 420 430
....*....|....*....|....*....|....
gi 651991267 389 VL-----PIMRISNEFEAVDleKRNAYGLQASIF 417
Cdd:cd07123 421 VLtvyvyPDSDFEETLELVD--TTSPYALTGAIF 452
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
14-460 |
1.28e-41 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 155.38 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 14 VNNKWVGSesGETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMI 93
Cdd:PLN02315 25 VGGEWRAN--GPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 94 HREVGKTLSSGKSEVKRTAQLIRHTAEEGLRTHGSFIqgdafpgASKSTKAMVQKV--PHGVVLAISPYNYPVNLAASKI 171
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSII-------PSERPNHMMMEVwnPLGIVGVITAFNFPCAVLGWNA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 172 APALITGNTVVFKPATQGAVSGLMMV----EALVNAGLPEGVLNVVTGrGSVIGDFVVTHPKVDMITFTGGTDTGQHIAK 247
Cdd:PLN02315 176 CIALVCGNCVVWKGAPTTPLITIAMTklvaEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 248 --KASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSE 325
Cdd:PLN02315 255 tvNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 326 DADIT-PMIDQKSADYVTSLIDDAKSKGAVVVHEG---QQEKNLLGPTVLDsVTEDMRVAWEEQFGPVLPIMRISNEFEA 401
Cdd:PLN02315 335 KGTLLgPLHTPESKKNFEKGIEIIKSQGGKILTGGsaiESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEA 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651991267 402 VDLEKRNAYGLQASIFTKNLENAFAL-----SDklnVGTVQVNGKTSRGPDHFPFLGVKNSGQG 460
Cdd:PLN02315 414 IEINNSVPQGLSSSIFTRNPETIFKWigplgSD---CGIVNVNIPTNGAEIGGAFGGEKATGGG 474
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
144-460 |
6.14e-39 |
|
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: 146.60 E-value: 6.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 144 AMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEAL-----------VNAGLPEgvlnv 212
Cdd:cd07132 94 VYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyldkecypvVLGGVEE----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 213 vTGRgsvigdfvVTHPKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQR 290
Cdd:cd07132 169 -TTE--------LLKQRFDYIFYTGSTSVGKIVMQAAAkhLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 291 CTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDADITPMIDQKSADYVTSLIDDAKskgavVVHEGQQEKN--LLGP 368
Cdd:cd07132 240 CIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGK-----VAIGGQTDEKerYIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 369 TVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVN-GKTSRGPD 447
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdTIMHYTLD 394
|
330
....*....|...
gi 651991267 448 HFPFLGVKNSGQG 460
Cdd:cd07132 395 SLPFGGVGNSGMG 407
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
49-440 |
1.47e-38 |
|
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: 145.46 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 49 VDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGkSEVKRTAQLIRhtAEEGLRTHGS 128
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQVQLR--ARAFVIYSYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 129 FIQGDAF-PGASKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATqgAVSGLM--MVEALVNAG- 204
Cdd:cd07084 78 IPHEPGNhLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHT--AVSIVMqiMVRLLHYAGl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 205 LPEGVLNVVTGRGSViGDFVVTHPKVDMITFTGGTDTGQHIAKKASMIPVVLELGGKDPAIVLDDAD-LDKTAKEIVSGA 283
Cdd:cd07084 156 LPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 284 LSYSGQRCTAIKRVMVVDSVADE-LVAKLKEKVAAlkvgRSSEDADITPMIdqkSADYVTSLIDDAKSKGAVVVHEGQQE 362
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKTpLVEKLKALLAR----RKLEDLLLGPVQ---TFTTLAMIAHMENLLGSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 363 KN---------LLGPTVLDSVTEDMRV--AW-EEQFGPVLPIMRISNEFEA--VDLEKRNAYGLQASIFTKNLENAFALS 428
Cdd:cd07084 308 KNhsipsiygaCVASALFVPIDEILKTyeLVtEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELI 387
|
410
....*....|...
gi 651991267 429 DKLNV-GTVQVNG 440
Cdd:cd07084 388 GNLWVaGRTYAIL 400
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
96-460 |
2.98e-38 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 144.48 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 96 EVGKTLSSGKSEVKrtaQLIRHTAEEGLRTHGSFiqgdaFPgasksTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPAL 175
Cdd:cd07137 60 EVSVLVSSCKLAIK---ELKKWMAPEKVKTPLTT-----FP-----AKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 176 ITGNTVVFKPATQG-AVSGLMmvEALVNAGLPEGVLNVVTGrGSVIGDFVVTHpKVDMITFTGGTDTGQHIAKKAS--MI 252
Cdd:cd07137 127 AAGNAVVLKPSELApATSALL--AKLIPEYLDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAkhLT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 253 PVVLELGGKDPAIVLDDADLDKTAKEIVSGAL-SYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDADITP 331
Cdd:cd07137 203 PVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 332 MIDQKSADYVTSLIDDaKSKGAVVVHEGQQ-EKNL-LGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNA 409
Cdd:cd07137 283 IVNSHHFQRLSRLLDD-PSVADKIVHGGERdEKNLyIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRP 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 651991267 410 YGLQASIFTKN--LENAFAlsDKLNVGTVQVNGKTSR-GPDHFPFLGVKNSGQG 460
Cdd:cd07137 362 KPLAAYVFTKNkeLKRRIV--AETSSGGVTFNDTVVQyAIDTLPFGGVGESGFG 413
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
150-478 |
3.22e-32 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 128.63 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 150 PHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEaLVNAGLPEGVLNVVtgRGSVIGDFVVTHPK 229
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAK-LLEQYLDSSAVRVV--EGAVTETTALLEQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 230 VDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALS-YSGQRCTAIKRVMVVDSVADE 306
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAkhLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 307 LVAKLKEKVAALKVGRSSEDADITPMIDQKSADYVTSLIDDAKSKGAVVVHEGQQEKNL-LGPTVLDSVTEDMRVAWEEQ 385
Cdd:PLN02174 269 VIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLkIAPTILLDVPLDSLIMSEEI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 386 FGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRGPDH-FPFLGVKNSGQGVQGI 464
Cdd:PLN02174 349 FGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHtLPFGGVGESGMGAYHG 428
|
330
....*....|....
gi 651991267 465 GRSIDSMLRDKVLV 478
Cdd:PLN02174 429 KFSFDAFSHKKAVL 442
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
151-424 |
1.88e-29 |
|
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: 120.84 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 151 HGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAG-LPEGVLNVVTGRGsviGDFVVTHPK 229
Cdd:cd07128 145 RGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSV---GDLLDHLGE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 230 VDMITFTGGTDTGQ----HIAKKASMIPVVLE--------LGgkdPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRV 297
Cdd:cd07128 222 QDVVAFTGSAATAAklraHPNIVARSIRFNAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 298 MVVDSVADELVAKLKEKVAALKVGRSSEDA-DITPMIDQKSADYVTSLIdDAKSKGAVVVHEGQQEKNLLG--------- 367
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGvRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEVVGadaekgaff 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 368 -PTVL--DSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENA 424
Cdd:cd07128 378 pPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFA 437
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
134-460 |
3.64e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 119.83 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 134 AFPGaskstKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEAlVNAGLPEGVLNVV 213
Cdd:PLN02203 97 AFPA-----TAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAAN-IPKYLDSKAVKVI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 214 TGrGSVIGDFVVTHpKVDMITFTGGTDTGQHIAKKAS--MIPVVLELGGKDPAIV--LDDA-DLDKTAKEIVSGALSY-S 287
Cdd:PLN02203 171 EG-GPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAkhLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 288 GQRCTAIKRVMVVDSVADELVAKLKEKVAALKVGRSSEDADITPMIDQKSADYVTSLIDDaKSKGAVVVHEGQ-QEKNL- 365
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKD-PRVAASIVHGGSiDEKKLf 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 366 LGPTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQVNGKTSR- 444
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQy 407
|
330
....*....|....*.
gi 651991267 445 GPDHFPFLGVKNSGQG 460
Cdd:PLN02203 408 ACDSLPFGGVGESGFG 423
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
149-418 |
1.75e-25 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 109.41 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 149 VP-HGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAG-LPEGVLNVVTGRGsviGDFVVT 226
Cdd:PRK11903 146 VPtRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS---AGLLDH 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 227 HPKVDMITFTGGTDTGQ----HIAKKASMIPVVLELGGKDPAIVLDDADLDKTA-----KEIVSGALSYSGQRCTAIKRV 297
Cdd:PRK11903 223 LQPFDVVSFTGSAETAAvlrsHPAVVQRSVRVNVEADSLNSALLGPDAAPGSEAfdlfvKEVVREMTVKSGQKCTAIRRI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 298 MVVDSVADELVAKLKEKVAALKVGR-SSEDADITPMIDQKSADYVTSLIdDAKSKGAVVVHEGQQEKNL---------LG 367
Cdd:PRK11903 303 FVPEALYDAVAEALAARLAKTTVGNpRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGGFALVdadpavaacVG 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 651991267 368 PTVLDSVTED--MRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASIFT 418
Cdd:PRK11903 382 PTLLGASDPDaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
49-440 |
7.28e-24 |
|
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: 103.78 E-value: 7.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 49 VDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEgLRThGS 128
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADL-VRE-GS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 129 FIQG---DAFPGASKSTKAMV--QKVPHGVVLAISPYNYPvnLAASKI----APALITGNTVVFK-----PATQGAVSGL 194
Cdd:cd07129 79 WLDAridPADPDRQPLPRPDLrrMLVPLGPVAVFGASNFP--LAFSVAggdtASALAAGCPVVVKahpahPGTSELVARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 195 MmVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKASM----IPVVLELGGKDPAIVLDDA 270
Cdd:cd07129 157 I-RAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpepIPFYAELGSVNPVFILPGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 271 ---DLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVA-DELVAKLKEKVAALKVG-------RSSEDADITPMIDQKSAD 339
Cdd:cd07129 236 laeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQtmltpgiAEAYRQGVEALAAAPGVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 340 YVTS---LIDDAKSKGAVVVHEGQQeknLLGPTVLDsvtedmrvawEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQASI 416
Cdd:cd07129 316 VLAGgaaAEGGNQAAPTLFKVDAAA---FLADPALQ----------EEVFGPASLVVRYDDAAELLAVAEALEGQLTATI 382
|
410 420 430
....*....|....*....|....*....|
gi 651991267 417 FTKNLENAFA------LSDKlnVGTVQVNG 440
Cdd:cd07129 383 HGEEDDLALArellpvLERK--AGRLLFNG 410
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
47-423 |
3.21e-19 |
|
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: 89.60 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 47 EEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKtlssGKSE---VKRTAQLIRHTAEEGL 123
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGM----GRVEdkiAKNHLAAEKTPGTEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 124 RTHGsfIQGDAfpGASkstkaMVQKVPHGVVLAISPYNYP----VNLAASKIApaliTGNTVVFKPATQGAVSGLMMVE- 198
Cdd:cd07121 80 TTTA--WSGDN--GLT-----LVEYAPFGVIGAITPSTNPtetiINNSISMLA----AGNAVVFNPHPGAKKVSAYAVEl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 199 ---ALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGG---TDTGQHIAKKAsmipvvleLG---GKDPAIVLDD 269
Cdd:cd07121 147 inkAIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGpavVKAALSSGKKA--------IGagaGNPPVVVDET 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 270 ADLDKTAKEIVSGAlSYSGQ-RCTAIKRVMVVDSVADELVAKLKeKVAALKVGRssedaditPMIDQKsadyVTSLIDDA 348
Cdd:cd07121 219 ADIEKAARDIVQGA-SFDNNlPCIAEKEVIAVDSVADYLIAAMQ-RNGAYVLND--------EQAEQL----LEVVLLTN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 349 KSKGAVVVHEGQQEKNLLG----------PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNAYGLQ--ASI 416
Cdd:cd07121 285 KGATPNKKWVGKDASKILKaagievpadiRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNRhtAII 364
|
....*..
gi 651991267 417 FTKNLEN 423
Cdd:cd07121 365 HSKNVEN 371
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
47-423 |
1.62e-18 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 87.65 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 47 EEVDRAIRQTADVQENWEAAEGHERSELLHRWAEELEKMTDEIGYMIHREVGKtlssGKSEVKrtaqLIRHTAEeGLRTH 126
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGM----GRVEDK----IAKNVAA-AEKTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 127 G-SFIQGDAFPGASKSTkaMVQKVPHGVVLAISPYNYP----VNLAASKIApaliTGNTVVFKP------ATQGAVSglM 195
Cdd:PRK15398 107 GvEDLTTEALTGDNGLT--LIEYAPFGVIGAVTPSTNPtetiINNAISMLA----AGNSVVFSPhpgakkVSLRAIE--L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 196 MVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGtdtgqhiakkASMIPVVLELG--------GKDPAIVL 267
Cdd:PRK15398 179 LNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGG----------PAVVKAAMKSGkkaigagaGNPPVVVD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 268 DDADLDKTAKEIVSGAlSYSGQ-RCTAIKRVMVVDSVADELVAKLKEKVAALkvgrssedadITPmidqksadyvtsliD 346
Cdd:PRK15398 249 ETADIEKAARDIVKGA-SFDNNlPCIAEKEVIVVDSVADELMRLMEKNGAVL----------LTA--------------E 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 347 DAKSKGAVVVHEGQQ-EKNLLG---PTVLD----SVTEDMRV-----------AWEEQFGPVLPIMRISNEFEAVDLEKR 407
Cdd:PRK15398 304 QAEKLQKVVLKNGGTvNKKWVGkdaAKILEaagiNVPKDTRLlivetdanhpfVVTELMMPVLPVVRVKDVDEAIALAVK 383
|
410
....*....|....*...
gi 651991267 408 NAYGLQ--ASIFTKNLEN 423
Cdd:PRK15398 384 LEHGNRhtAIMHSRNVDN 401
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
44-479 |
6.62e-17 |
|
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: 82.27 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 44 LSQEEVDRAIRQTADvqenweAAEGHERsellhRWAEELEKMTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGL 123
Cdd:cd07077 13 NHDEQRDLIINAIAN------ALYDTRQ-----RLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 124 RTHGSfIQGDAFpgaskstKAMVQKVPHGVVLAISPYNYPVnLAASKIAPALITGNTVVFKPATQGAVSG---LMMVEAL 200
Cdd:cd07077 82 HIQDV-LLPDNG-------ETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNralALLFQAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 201 VNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGTDTGQHIAKKASMIPVVLELGGKDPAIVLDDADLDKTAKEIV 280
Cdd:cd07077 153 DAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 281 SGAlSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALKVgrsSEDADITPMIDQKSADYVtsliddakskgavvvhegq 360
Cdd:cd07077 233 DSK-FFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGL---KVPQETKPLSKETTPSFD------------------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 361 qeknllgptvlDSVTEDMrvaweeqfGPVLPIMRISNEFEAV----DLEKRNAYGLQASIFTKNLENAFALSDKLNVGTV 436
Cdd:cd07077 290 -----------DEALESM--------TPLECQFRVLDVISAVenawMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASF 350
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 651991267 437 QVNGKTSRGPDHFPFLGVK---NSGQG-VQGIGRSIDSMLRDKVLVL 479
Cdd:cd07077 351 YPNESSKKGRGAFAGKGVErivTSGMNnIFGAGVGHDALRPLKRLVR 397
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
13-404 |
4.34e-15 |
|
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: 77.54 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 13 LVNNKWVGSEsgETVKIYSPDDHELAGSVPALSQEEVDRAIRQTADVQEN--WEAAEGHER----SELLHRWAEELEK-- 84
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSglHNPLKNPERyllyGDVSHRVAHELRKpe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 85 MTDEIGYMIHREVGKTLSSGKSEVKRTAQLIRHTAEEGLRthgsFI-QGDAFPGASKSTKAMVQKVPHGVVLAISPYNYP 163
Cdd:cd07126 80 VEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVR----FLaRSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 164 VNLAASKIAPALITGNTVVFKPATQGAVSGLMMVEALVNAGLPEGVLNVVTGRGSVIGDFVV-THPKvdMITFTGGTDTG 242
Cdd:cd07126 156 LEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANPR--MTLFTGSSKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 243 QHIAKKASMiPVVLELGGKDPAIVLDD-ADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADelvAKLKEKVAALKVG 321
Cdd:cd07126 234 ERLALELHG-KVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQ---AGILDKLKALAEQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 322 RSSEDADITPMI---DQKSADYVTSLiddAKSKGAVVVHEGQQEKNLLGPTVLDSV--------------TEDMRVAWEE 384
Cdd:cd07126 310 RKLEDLTIGPVLtwtTERILDHVDKL---LAIPGAKVLFGGKPLTNHSIPSIYGAYeptavfvpleeiaiEENFELVTTE 386
|
410 420
....*....|....*....|
gi 651991267 385 QFGPvlpiMRISNEFEAVDL 404
Cdd:cd07126 387 VFGP----FQVVTEYKDEQL 402
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
149-409 |
1.01e-14 |
|
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: 76.36 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 149 VPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPAtQGAVSGLMMV-----EALVNAGL-PEGVLNVVTGRGSVIGD 222
Cdd:cd07127 192 VPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPH-PAAILPLAITvqvarEVLAEAGFdPNLVTLAADTPEEPIAQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 223 FVVTHPKVDMITFTGGTDTGQHIAKKASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMV-VD 301
Cdd:cd07127 271 TLATRPEVRIIDFTGSNAFGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 302 SVA--------DELVAKLKEKVAALkvgrSSEDADITPMIDQKSADYVTSLIDDAKSKGAVVV------HEGQQEKNLLG 367
Cdd:cd07127 351 GIQtddgrksfDEVAADLAAAIDGL----LADPARAAALLGAIQSPDTLARIAEARQLGEVLLaseavaHPEFPDARVRT 426
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 651991267 368 PTVLDSVTEDMRVAWEEQFGPVLPIMRISNEFEAVDLEKRNA 409
Cdd:cd07127 427 PLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESV 468
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
150-445 |
1.08e-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: 75.77 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 150 PHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKP------ATQGAVSglMMVEALVNAGLPEGVLNVVTGRGSVIGDF 223
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprakkVTQRAAT--LLLQAAVAAGAPENLIGWIDNPSIELAQR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 224 VVTHPKVDMITFTGGTDTGQhiAKKASMIPVVLELGGKDPAIVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSV 303
Cdd:cd07081 173 LMKFPGIGLLLATGGPAVVK--AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 304 ADELVAKLKEKVAALKVGRSSE--------DADITPMIDQKSADYVTSLIddakskGAVVvheGQQEKNLLGPTvldSVT 375
Cdd:cd07081 251 YDEVMRLFEGQGAYKLTAEELQqvqpvilkNGDVNRDIVGQDAYKIAAAA------GLKV---PQETRILIGEV---TSL 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651991267 376 EDMRVAWEEQFGPVLPIMRISNeFE-----AVDLEKRNAYGLQASIFTKNL---ENAFALSDKLNVGTVQVNGKTSRG 445
Cdd:cd07081 319 AEHEPFAHEKLSPVLAMYRAAN-FAdadakALALKLEGGCGHTSAMYSDNIkaiENMNQFANAMKTSRFVKNGPCSQG 395
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
44-445 |
2.60e-14 |
|
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: 74.84 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 44 LSQEEVDRAIRQTADvqenweAAEGHersellhrwAEELEKMT-DEIGYmihrevgktlssGKSEVKRTAqliRHTAEEG 122
Cdd:cd07122 18 FSQEQVDKIVEAVAW------AAADA---------AEELAKMAvEETGM------------GVVEDKVIK---NHFASEY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 123 LRTHgsfIQGDAFPGA---SKSTKAMVQKVPHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGL----M 195
Cdd:cd07122 68 VYND---IKDMKTVGVieeDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIeaakI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 196 MVEALVNAGLPEGVLNVVTGRGSVIGDFVVTHPKVDMITFTGGtdtgqhiakkASMI--------PVvleLG---GKDPA 264
Cdd:cd07122 145 MREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGG----------PGMVkaayssgkPA---IGvgpGNVPA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 265 IVLDDADLDKTAKEIVSGALSYSGQRCTAIKRVMVVDSVADELVAKLKEKVAALkvgrssedaditpmIDQKSADYVTSL 344
Cdd:cd07122 212 YIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEIYDEVRAELKRRGAYF--------------LNEEEKEKLEKA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 345 I--DDAKSKGAVVVHEGQQEKNLLGptvlDSVTEDMRVAWEEQFG-------------PVLPIMRISNEFEAVDLEKR-- 407
Cdd:cd07122 278 LfdDGGTLNPDIVGKSAQKIAELAG----IEVPEDTKVLVAEETGvgpeeplsreklsPVLAFYRAEDFEEALEKAREll 353
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 651991267 408 NAYGL--QASIFTKNLENAFALSDKLNVGTVQVNGKTSRG 445
Cdd:cd07122 354 EYGGAghTAVIHSNDEEVIEEFALRMPVSRILVNTPSSLG 393
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
150-445 |
4.09e-05 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 46.33 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 150 PHGVVLAISPYNYPVNLAASKIAPALITGNTVVFKPATQGAVSGLM----MVEALVNAGLPEGVLNVVTGRGSVIGDFVV 225
Cdd:PRK13805 108 PVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAaakiVLDAAVAAGAPKDIIQWIEEPSVELTNALM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 226 THPKVDMITFTGGtdTGQHIAKKASMIPVvleLG---GKDPAIVLDDADLDKTAKEIVsgaLSYS---GQRCTAIKRVMV 299
Cdd:PRK13805 188 NHPGIALILATGG--PGMVKAAYSSGKPA---LGvgaGNVPAYIDKTADIKRAVNDIL---LSKTfdnGMICASEQAVIV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 300 VDSVADELVAKLKEKVAAL-------KVGR---SSEDADITPMIDQKSADYVtsliddAKSKGaVVVHEGQqeKNLLGPt 369
Cdd:PRK13805 260 DDEIYDEVKEEFASHGAYFlnkkelkKLEKfifGKENGALNADIVGQSAYKI------AEMAG-FKVPEDT--KILIAE- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 370 vLDSVTEDMRVAwEEQFGPVLPIMRISNEFEAVDL-EKRNAY---GLQASIFTKNLENAFALSDKLNVGTVQVNGKTSRG 445
Cdd:PRK13805 330 -VKGVGESEPLS-HEKLSPVLAMYKAKDFEDAVEKaEKLVEFgglGHTAVIYTNDDELIKEFGLRMKACRILVNTPSSQG 407
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
149-437 |
1.47e-03 |
|
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: 40.89 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 149 VPHGVVLAISPYNYPVnLAASKIAPALITGNTVVFKPAT--QGAVSGLMMVEALVNAGLP-EGVLNVVTGRGS--VIGDF 223
Cdd:pfam05893 87 FPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSsdPFTAAALLASFADLDPTHPlADSLSVVYWDGGstQLEDL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 224 VVTHpkVDMITFTGGTDTGQHIAKKASMIPVVLELGGKDPAIVLD-DADLDKTAKEIVSGALSYSGQRCTAiKRVMVVDS 302
Cdd:pfam05893 166 IVAN--ADVVIAWGGEDAINAIRECLKPGKQWIDFGAKISFAVVDrEAALDKAAERAADDICVFDQQACLS-PQTVFVES 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 303 ----VADELVAKLKEKVA--ALKVGRSSEDADITPMI--DQKSADYVTSLIDDAKskgaVVVHEGQqeknllgptvldsv 374
Cdd:pfam05893 243 ddkiTPDEFAERLAAALAkrARILPKAVLDIDEAAKIssDRAECKLDYAFAGERG----VWSDFHQ-------------- 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651991267 375 teDMRVAWEEQ-------FGPVLPIMRISNEFEAVDLEKRNAYGLQASIFTKNLENAFALSDKLNVGTVQ 437
Cdd:pfam05893 305 --RWTVIWSDGqeelnspLNRTVNVVPVPSLSDVVRYVSENRTYLQTCGLAPYSGRLPYLDRKLALAGVS 372
|
|
| |
