|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
19-441 |
0e+00 |
|
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: 664.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 19 YGPVPESHACALAWLDTQDRCLGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPG 98
Cdd:cd07111 1 YGPAPESAACALAWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 99 VVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFS 178
Cdd:cd07111 81 HVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAGWKPVGVVGQIVPWNFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 179 FLEMMWRICPALAVGCTVVALVPPA-SPAPLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPE---- 253
Cdd:cd07111 161 LLMLAWKICPALAMGNTVVLKPAEYtPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEvgra 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 --------------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGR 283
Cdd:cd07111 241 lrratagtgkklslelggkspfivfddadldsavegivdaiwfnqgqvccAGSRLLVQESVAEELIRKLKERMSHLRVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 284 GLDGAVDMGARGAAACDLVQRFVREAQ-SQGAQVFQAGDV-PSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07111 321 PLDKAIDMGAIVDPAQLKRIRELVEEGrAEGADVFQPGADlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRPSGTPA 441
Cdd:cd07111 401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEPA 480
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
87-437 |
1.42e-104 |
|
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: 327.24 E-value: 1.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 87 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST----------- 155
Cdd:cd07078 8 RAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRlhgevipspdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 156 QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLV 234
Cdd:cd07078 87 GELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPlTALLLAELLAEAGLPPGVLNVVTGDGDEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 235 -PILASQPGIRKVAFCGAPEGG------------------------------------------------------LRLL 259
Cdd:cd07078 167 gAALASHPRVDKISFTGSTAVGkaimraaaenlkrvtlelggksplivfddadldaavkgavfgafgnagqvctaaSRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 260 IQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSN 336
Cdd:cd07078 247 VHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLiSAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKgyFVPPTVLTD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 337 LPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGG 415
Cdd:cd07078 327 VDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPFGG 406
|
410 420
....*....|....*....|..
gi 223972653 416 CKESGCSWHGGPDGLYEYLRPS 437
Cdd:cd07078 407 VKQSGIGREGGPYGLEEYTEPK 428
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
87-437 |
5.39e-76 |
|
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: 249.84 E-value: 5.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 87 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------ST 155
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLAdklggpelpspDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 156 QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP-LLLAQLAGELGPFPGILNVLSGPASLV 234
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTaLALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 235 -PILASQPGIRKVAFCGAPEGGLRLliqesvwdeaMRRLQERMGRLR------------SGRGLDGAVDMGARGA----- 296
Cdd:cd06534 163 gAALLSHPRVDKISFTGSTAVGKAI----------MKAAAENLKPVTlelggkspvivdEDADLDAAVEGAVFGAffnag 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 297 AACDLVQR-FVreaqsqgaqvfqagdvpsERPFYPP------TLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 369
Cdd:cd06534 233 QICTAASRlLV------------------HESIYDEfveklvTVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALAN 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 370 GTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGGCKESGCSWHGGPDGLYEYLRPS 437
Cdd:cd06534 295 DTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKNSGIGREGGPYGLEEYTRTK 363
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
40-436 |
4.31e-71 |
|
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: 240.41 E-value: 4.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRdGDVQLAQQLLHYHA-----IQASTQEEALAG------WEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:COG1012 86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAgearrLYGETIPSDAPGtrayvrREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPAS-LVPILASQPGIRKVAFCGAPE----------- 253
Cdd:COG1012 165 ALAAGNTVV--LKPAEQTPLsalLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAvgrriaaaaae 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------GGL----------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 290
Cdd:COG1012 243 nlkrvtlelGGKnpaivlddadldaaveaavrgafgnagqrctaasRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 291 MGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLV 367
Cdd:COG1012 323 MGPLiSEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 368 ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTET 472
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
48-435 |
7.49e-67 |
|
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: 228.18 E-value: 7.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 48 WLKPEHRnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVT 127
Cdd:pfam00171 1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 128 GRAVREVRdGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVV 197
Cdd:pfam00171 80 GKPLAEAR-GEVDRAIDVLRYYAglarrldgetLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 198 alVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE-------------------- 253
Cdd:pfam00171 159 --LKPSELTPLtalLLAELFEEAGLPAGVLNVVTGSGAEVgEALVEHPDVRKVSFTGSTAvgrhiaeaaaqnlkrvtlel 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 GGL----------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAA 298
Cdd:pfam00171 237 GGKnplivledadldaaveaavfgafgnagqvctatsRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPlISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 299 CDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSA 377
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGGEAGLDNGyFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 378 SVWSERLGQALELGYGLQVGTVWINAHGLRDP-SVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTE 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
61-436 |
1.17e-64 |
|
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: 222.31 E-value: 1.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQASTQEEAL----AGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL-- 208
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVipvrGPFlnytvrEPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVV--LKPAELTPLsa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 209 -LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE--------------------------------- 253
Cdd:cd07115 161 lRIAELMAEAGFPAGVLNVVTGFGEVAgAALVEHPDVDKITFTGSTAvgrkimqgaagnlkrvslelggksanivfadad 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQS 311
Cdd:cd07115 241 ldaavraaatgifynqgqmctAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLvSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 312 QGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALEL 390
Cdd:cd07115 321 EGARLLTGGKRPGARGFFvEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 223972653 391 GYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07115 401 AAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEV 446
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
61-436 |
2.16e-61 |
|
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: 213.57 E-value: 2.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGD 138
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR-AQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 139 VQLAQQLLHYHAIQASTQEEALAG-----------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP 207
Cdd:cd07114 82 VRYLAEWYRYYAGLADKIEGAVIPvdkgdylnftrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 208 LL-LAQLAGELGPFPGILNVLSGPASLVPI-LASQPGIRKVAFCGAPEG------------------------------- 254
Cdd:cd07114 162 TLeLAKLAEEAGFPPGVVNVVTGFGPETGEaLVEHPLVAKIAFTGGTETgrhiaraaaenlapvtlelggkspnivfdda 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 255 -----------------------GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQ 310
Cdd:cd07114 242 dldaavngvvagifaaagqtcvaGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGpLATERQLEKVERYVARAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 311 SQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLG 385
Cdd:cd07114 322 EEGARVLTGGERPSGADlgagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 223972653 386 QALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07114 402 RAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQT 452
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
41-420 |
2.14e-59 |
|
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: 208.74 E-value: 2.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEE----------ALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGslseidedtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCG---------------- 250
Cdd:cd07559 162 AAGNTVV--LKPASQTPlsiLVLMELIGDLLP-KGVVNVVTGFGSEAgKPLASHPRIAKLAFTGsttvgrlimqyaaenl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ----------------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 287
Cdd:cd07559 239 ipvtlelggkspniffddamdadddfddKAEEGQlgfafnqgevctcpsRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 288 AVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07559 319 ETMMGAQvSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGldkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
61-436 |
2.47e-58 |
|
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: 204.68 E-value: 2.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07106 3 NPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHA--------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLLLA 211
Cdd:cd07106 82 GAVAWLRYTAsldlpdevIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPlCTLKLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 212 QLAGELGPfPGILNVLSGPASLVPILASQPGIRKVAFCGAPE--------------------GG---------------- 255
Cdd:cd07106 162 ELAQEVLP-PGVLNVVSGGDELGPALTSHPDIRKISFTGSTAtgkkvmasaaktlkrvtlelGGndaaivlpdvdidava 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 ------------------LRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQSQGAQV 316
Cdd:cd07106 241 pklfwgafinsgqvcaaiKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGpVQNKMQYDKVKELVEDAKAKGAKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 317 FQAGDVPsERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGL 394
Cdd:cd07106 321 LAGGEPL-DGPgyFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 223972653 395 QVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07106 400 EAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQT 441
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
43-434 |
2.00e-55 |
|
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: 197.53 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAF--KGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRdGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07119 81 RLETLNTGKTLRESE-IDIDDVANCFRYYAglatketgevYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE------------- 253
Cdd:cd07119 160 AAGNTVV--IKPSEVTPLTtiaLFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTAtgrsimraaagnv 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -----------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 292
Cdd:cd07119 238 kkvalelggknpnivfadadfetavdqalngvffnagqvcsAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 293 A-RGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 366
Cdd:cd07119 318 PlVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 367 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
41-435 |
5.55e-55 |
|
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: 196.28 E-value: 5.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH--PGVVRAQHLTRLAEVIQKHQRL 118
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 119 LWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAgwadkiqgktIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE----------- 253
Cdd:cd07091 165 ALAAGNTVV--LKPAEQTPLsalYLAELIKEAGFPPGVVNIVPGFGPTAgAAISSHMDVDKIAFTGSTAvgrtimeaaak 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 --------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAV 289
Cdd:cd07091 243 snlkkvtlelggkspnivfddadldkavewaafgiffnqgqcccAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 290 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLV 367
Cdd:cd07091 323 FQGPQvSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFiQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 368 ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQ 470
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
61-420 |
1.43e-54 |
|
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: 194.71 E-value: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQASTQE----EALAGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL-- 208
Cdd:cd07093 83 RAAANFRFFADYILQLDgesyPQDGGAlnyvlrQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVV--LKPSEWTPLta 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 209 -LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE--------------------------------- 253
Cdd:cd07093 161 wLLAELANEAGLPPGVVNVVHGFGPEAgAALVAHPDVDLISFTGETAtgrtimraaapnlkpvslelggknpnivfadad 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDLVQRFVREAQS 311
Cdd:cd07093 241 ldravdaavrssfsnngevclAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEhLEKVLGYVELARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 312 QGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQ 386
Cdd:cd07093 321 EGATILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400
|
410 420 430
....*....|....*....|....*....|....
gi 223972653 387 ALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07093 401 AHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASG 434
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-433 |
3.94e-54 |
|
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: 194.20 E-value: 3.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG-WSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQA-------------STQEEALAGW---EPMGVIGLILPPTFSFLEMM 183
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWAtkingetlapsipSMQGERYTAFtrrEPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 184 WRICPALAVGCTVValVPPASPAPLLL---AQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAF------------ 248
Cdd:cd07113 161 WKIGAALATGCTIV--IKPSEFTPLTLlrvAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFtgsvatgkkigr 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 249 ---------------------------------------------CGAPEgglRLLIQESVWDEAMRRLQERMGRLRSGR 283
Cdd:cd07113 239 qaasdltrvtlelggknaaaflkdadidwvveglltagflhqgqvCAAPE---RFYVHRSKFDELVTKLKQALSSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 284 GLDGAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07113 316 PMDESVMFGPlANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFvQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDY 467
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
89-434 |
4.88e-53 |
|
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: 190.34 E-value: 4.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAiqastqEEA--LAG---- 162
Cdd:cd07103 31 AFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEVDYAASFLEWFA------EEArrIYGrtip 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 163 -----------WEPMGVIGLILPPTFSFLeMMWR-ICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVL 227
Cdd:cd07103 104 spapgkrilviKQPVGVVAAITPWNFPAA-MITRkIAPALAAGCTVV--LKPAEETPlsaLALAELAEEAGLPAGVLNVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 228 SG-PASLVPILASQPGIRKVAFCG--------------------------AP-------------EGGL----------- 256
Cdd:cd07103 181 TGsPAEIGEALCASPRVRKISFTGstavgkllmaqaadtvkrvslelggnAPfivfddadldkavDGAIaskfrnagqtc 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ----RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-FYP 330
Cdd:cd07103 261 vcanRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLiNERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGyFYE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 331 PTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPS 410
Cdd:cd07103 341 PTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE 420
|
410 420
....*....|....*....|....
gi 223972653 411 VPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07103 421 APFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
61-436 |
6.17e-53 |
|
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: 189.85 E-value: 6.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQASTQEEALAG-----------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP-- 207
Cdd:cd07092 83 GAVDNFRFFAGAARTLEGPAAGeylpghtsmirREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVV--LKPSETTPlt 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 208 -LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL----------------------------- 256
Cdd:cd07092 161 tLLLAELAAEVLP-PGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKkvaraaadtlkrvhlelggkapvivfdda 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDLVQRFVREAq 310
Cdd:cd07092 240 dldaavagiatagyynagqdctaacRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAqRERVAGFVERA- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 311 SQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALE 389
Cdd:cd07092 319 PAHARVLTGGRRAEGPGyFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 223972653 390 LGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRI 445
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
58-420 |
1.02e-51 |
|
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: 187.04 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 58 PCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVR 135
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 136 DGDVQLAQQLLHYHA--IQ------ASTQEEALA--GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASP 205
Cdd:cd07112 85 AVDVPSAANTFRWYAeaIDkvygevAPTGPDALAliTREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV--LKPAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 206 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE---------------------------- 253
Cdd:cd07112 163 SPLtalRLAELALEAGLPAGVLNVVPGFGHTAgEALGLHMDVDALAFTGSTEvgrrfleysgqsnlkrvwlecggkspni 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ----------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQR 304
Cdd:cd07112 243 vfadapdldaaaeaaaagifwnqgevcsAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALvSEAHFDKVLG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 305 FVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS 381
Cdd:cd07112 323 YIESGKAEGARLVAGGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWT 402
|
410 420 430
....*....|....*....|....*....|....*....
gi 223972653 382 ERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07112 403 SDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSG 441
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
41-420 |
2.86e-50 |
|
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: 183.04 E-value: 2.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA--IQAST--------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAgvIRAEEgsanmideDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCG---------------- 250
Cdd:cd07117 162 AAGNTVV--IKPSSTTSlslLELAKIIQDVLP-KGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGstevgrdvaiaaakkl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 -----------------------APEG---------------GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 292
Cdd:cd07117 239 ipatlelggksaniifddanwdkALEGaqlgilfnqgqvccaGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 293 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 366
Cdd:cd07117 319 AQvNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldkgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 223972653 367 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
61-435 |
1.12e-49 |
|
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: 180.89 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH-PGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDV 139
Cdd:cd07109 3 DPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-ADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 140 QLAQQLLHYHAIQAST-------QEEALAGW---EPMGVIGLILPPTFSfLEMMWR-ICPALAVGCTVValVPPASPAPL 208
Cdd:cd07109 82 EAAARYFEYYGGAADKlhgetipLGPGYFVYtvrEPHGVTGHIIPWNYP-LQITGRsVAPALAAGNAVV--VKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 209 ---LLAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPEGGL---------------------------- 256
Cdd:cd07109 159 talRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIavmraaaenvvpvtlelggkspqivfad 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 --------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGaVDMGA-RGAAACDLVQRFVREA 309
Cdd:cd07109 239 adleaalpvvvnaiiqnagqtcsagsRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPlISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 310 QSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLG 385
Cdd:cd07109 318 RARGARIVAGGRIAEGAPaggyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 223972653 386 QALELGYGLQVGTVWINAHGLRDP-SVPTGGCKESGcswHG---GPDGLYEYLR 435
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSG---HGrekGLEALYNYTQ 448
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
40-433 |
1.66e-48 |
|
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: 178.49 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG-WSAH-PGVVRAQHLTRLAEVIQKHQR 117
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGLKvSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 118 LLWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRIC 187
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGgwadkihgqvIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 188 PALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE---------- 253
Cdd:cd07143 167 PALAAGNTIV--LKPSELTPLsalYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLvgrkvmeaaa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGA 288
Cdd:cd07143 245 ksnlkkvtlelggkspnivfddadlesavvwtaygiffnhgqvccAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 289 VDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGD-VPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 366
Cdd:cd07143 325 TFQGPQvSQIQYERIMSYIESGKAEGATVETGGKrHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 367 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENY 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
43-420 |
1.87e-47 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 175.10 E-value: 1.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:PRK13473 6 LINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQASTQEEALAGW------EPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:PRK13473 85 ESLNCGKPLHLALNDEIPAIVDVFRFFAgaarcLEGKAAGEYLEGHtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCG----------------- 250
Cdd:PRK13473 165 AGNTVV--LKPSEITPltaLKLAELAADILP-PGVLNVVTGRGATVgDALVGHPKVRMVSLTGsiatgkhvlsaaadsvk 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ---------AP-----------------EGGL-----------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:PRK13473 242 rthlelggkAPvivfddadldavvegirTFGYynagqdctaacRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:PRK13473 322 LiSAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKgyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAND 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:PRK13473 402 SDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSG 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
87-433 |
7.94e-46 |
|
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: 170.21 E-value: 7.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 87 RMAF-KG-WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST--------- 155
Cdd:cd07118 29 RKAFdKGpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQAR-GEIEGAADLWRYAASLARTlhgdsynnl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 156 --QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPA---SPAPLLLAQLAGELGPFPGILNVLSGP 230
Cdd:cd07118 108 gdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVV--VKPSeftSGTTLMLAELLIEAGLPAGVVNIVTGY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 231 ASLV-PILASQPGIRKVAFCG---------------------------------------APEGGL-------------- 256
Cdd:cd07118 186 GATVgQAMTEHPDVDMVSFTGstrvgkaiaaaaarnlkkvslelggknpqivfadadldaAADAVVfgvyfnageccnsg 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPT 332
Cdd:cd07118 266 sRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIiNEAQLAKITDYVDAGRAEGATLLLGGERLASAAglFYQPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 333 LVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVP 412
Cdd:cd07118 346 IFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELP 425
|
410 420
....*....|....*....|.
gi 223972653 413 TGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07118 426 FGGFKQSGIGRELGRYGVEEY 446
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
61-434 |
2.13e-45 |
|
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: 169.07 E-value: 2.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVR-D-GD 138
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwDvDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 139 V--------QLAQQLLHYHAIQASTQEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVaLVPP--ASP 205
Cdd:cd07110 83 VagcfeyyaDLAEQLDAKAERAVPLPSEDFKARvrrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVV-LKPSelTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 206 APLLLAQLAGELGPFPGILNVLSGPASLVPI-LASQPGIRKVAFCGAPEGGL---------------------------- 256
Cdd:cd07110 162 TELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSqvmqaaaqdikpvslelggkspiivfdd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 --------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREA 309
Cdd:cd07110 242 adlekavewamfgcfwnngqicsatsRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPlVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 310 QSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQ 386
Cdd:cd07110 322 KEEGARLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAER 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 223972653 387 ALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07110 402 CDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYL 449
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
61-420 |
4.76e-45 |
|
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: 167.92 E-value: 4.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQASTQE-EALAG---------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP--- 207
Cdd:cd07108 83 VLADLFRYFGGLAGELKgETLPFgpdvltytvREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVV--LKAAEDAPlav 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 208 LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE--------------------------------- 253
Cdd:cd07108 161 LLLAEILAQVLP-AGVLNVITGYGEECgAALVDHPDVDKVTFTGSTEvgkiiyraaadrlipvslelggkspmivfpdad 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ----------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREAQ 310
Cdd:cd07108 240 lddavdgaiagmrftrqgqsctAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAiISEKQFAKVCGYIDLGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 311 S-QGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERL 384
Cdd:cd07108 320 StSGATVLRGGPLPGEGPladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDL 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 223972653 385 GQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07108 400 GRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSG 435
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
40-436 |
1.84e-44 |
|
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: 166.81 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH-PGVVRAQHLTRLAEVIQKHQRL 118
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 119 LWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAgwadkiqgktIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPLLL---AQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL-------- 256
Cdd:cd07144 168 ALAAGNTVV--IKPAENTPLSLlyfANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRlvmkaaaq 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ----------------------------------------------RLLIQESVWDEAMRRLQERMG-RLRSGRGLDGAV 289
Cdd:cd07144 246 nlkavtlecggkspalvfedadldqavkwaaagimynsgqnctatsRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 290 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEA 364
Cdd:cd07144 326 VVGPQvSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLgkgyFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 365 LLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQT 477
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
43-435 |
1.69e-43 |
|
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: 163.98 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWArriegeiipsdRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL----------- 256
Cdd:cd07088 160 TGNTIV--IKPSEETPLNaleFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQkimeaaaenit 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:cd07088 238 kvslelggkapaivmkdadldlavkaivdsriincgqvctcaeRVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:cd07088 318 LvNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGlrdPSVPTG---GCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINREN---FEAMQGfhaGWKKSGLGGADGKHGLEEYLQ 462
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
61-435 |
2.74e-43 |
|
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: 162.93 E-value: 2.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAML-GDVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLL 209
Cdd:cd07107 82 VAAALLDYFAglvtelkgetIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPlSALR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 210 LAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL-------------------------------- 256
Cdd:cd07107 162 LAELAREVLP-PGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRaimraaaegikhvtlelggknalivfpdadpe 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -----------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREAQSQ 312
Cdd:cd07107 241 aaadaavagmnftwcgqscgstsRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPlVSRQQYDRVMHYIDSAKRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 313 GAQVFQAGDVPS----ERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQA 387
Cdd:cd07107 321 GARLVTGGGRPEgpalEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 223972653 388 LELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07107 401 HRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQ 448
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
44-434 |
3.86e-43 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 163.32 E-value: 3.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 44 VNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLE 123
Cdd:PLN02278 29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 124 SLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSfLEMMWR-ICPALA 191
Cdd:PLN02278 109 TLEQGKPLKEAI-GEVAYGASFLEYFAEEAkrvygdiipspFPDRRLLVLKQPVGVVGAITPWNFP-LAMITRkVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV--PILASqPGIRKVAFCG---------------- 250
Cdd:PLN02278 187 AGCTVV--VKPSELTPLTalaAAELALQAGIPPGVLNVVMGDAPEIgdALLAS-PKVRKITFTGstavgkklmagaaatv 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ----------AP-------------EGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 292
Cdd:PLN02278 264 krvslelggnAPfivfddadldvavKGALaskfrnsgqtcvcanRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 293 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:PLN02278 344 PLiNEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGtFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
61-434 |
5.35e-43 |
|
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: 162.13 E-value: 5.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVvRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGD 138
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEAR-FE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 139 VQLAQQLLHY----------HAIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL 208
Cdd:cd07120 81 ISGAISELRYyaglarteagRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVV--VKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 209 L---LAQLAGELGPFP-GILNVLSGPAS----------LVPIL--------------ASQPGIRKVA------------- 247
Cdd:cd07120 159 InaaIIRILAEIPSLPaGVVNLFTESGSegaahlvaspDVDVIsftgstatgraimaAAAPTLKRLGlelggktpcivfd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 248 ---------------------FCGApegGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRF 305
Cdd:cd07120 239 dadldaalpkleraltifagqFCMA---GSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLiDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 306 VREAQSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS 381
Cdd:cd07120 316 VERAIAAGAEVVLRGGPVTEGLakgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 223972653 382 ERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
41-420 |
6.24e-43 |
|
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: 162.62 E-value: 6.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07116 2 DNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAG----------WEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEidentvayhfHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGP-ASLVPILASQPGIRKVAFCGAPEGGL---------- 256
Cdd:cd07116 162 AAGNCVV--LKPAEQTPasiLVLMELIGDLLP-PGVVNVVNGFgLEAGKPLASSKRIAKVAFTGETTTGRlimqyaseni 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 287
Cdd:cd07116 239 ipvtlelggkspniffadvmdaddaffdkalegfvmfalnqgevctcpsRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 288 AVDMGARGAAA-CDLVQRFVREAQSQGAQVFQAGD-----VPSERPFYPPTLVSNLPPASpCAQVEVPWPVVVASPFRTA 361
Cdd:cd07116 319 ETMIGAQASLEqLEKILSYIDIGKEEGAEVLTGGErnelgGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDE 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07116 398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
61-434 |
8.19e-43 |
|
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: 161.64 E-value: 8.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWS-AHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDV 139
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 140 QLAQQLLHYHAIQAS--TQEEALAGW-------------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPAS 204
Cdd:cd07089 83 DGPIGHLRYFADLADsfPWEFDLPVPalrggpgrrvvrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVV--LKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 205 PAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE--------------------GG----- 255
Cdd:cd07089 161 DTPLsalLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAvgrrimaqaaatlkrvllelGGksani 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 -----------------------------LRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRF 305
Cdd:cd07089 241 vlddadlaaaapaavgvcmhnagqgcaltTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLiSAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 306 VREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSE 382
Cdd:cd07089 321 IARGRDEGARLVTGGGRPAGLDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 223972653 383 RLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
43-434 |
2.48e-42 |
|
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: 160.59 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFK---GWSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAgwadkihgktIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSG--PASLVPIlASQPGIRKVAFCGAPE----------- 253
Cdd:cd07141 170 LACGNTVV--LKPAEQTPLtalYLASLIKEAGFPPGVVNVVPGygPTAGAAI-SSHPDIDKVAFTGSTEvgkliqqaagk 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 --------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAV 289
Cdd:cd07141 247 snlkrvtlelggkspnivfadadldyaveqahealffnmgqcccAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 290 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLV 367
Cdd:cd07141 327 EQGPQiDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFiQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 368 ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
43-435 |
2.90e-42 |
|
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: 160.35 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFK--GWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST--QEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAgwadkIHGMTlpADGPHHVYtlhEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLS--GPASLVPIlASQPGIRKVAFCGAPE------------ 253
Cdd:cd07142 167 ACGNTIV--LKPAEQTPLsalLAAKLAAEAGLPDGVLNIVTgfGPTAGAAI-ASHMDVDKVAFTGSTEvgkiimqlaaks 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 290
Cdd:cd07142 244 nlkpvtlelggkspfivcedadvdkavelahfalffnqgqcccAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 291 MGARGA-AACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVA 368
Cdd:cd07142 324 QGPQVDkEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYiQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 369 NGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
43-434 |
1.53e-40 |
|
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: 155.43 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAalardfpfeerRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGL------------ 256
Cdd:cd07139 162 LAAGCTVVLKPSPETPlDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRriaavcgerlar 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR 294
Cdd:cd07139 242 vtlelggksaaivlddadldaavpglvpaslmnngqvcvaltRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 295 GAAA-CDLVQRFVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:cd07139 322 ASARqRERVEGYIAKGRAEGARLVTGGGRPAGLDrgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAND 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLrDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07139 402 SDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL-DFGAPFGGFKQSGIGREGGPEGLDAYL 464
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
61-433 |
7.50e-40 |
|
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: 153.23 E-value: 7.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQAST---QEEALAG-------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPA-PLL 209
Cdd:cd07090 82 SSADCLEYYAGLAPTlsgEHVPLPGgsfaytrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLtALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 210 LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGA-PEG---------------------------------- 254
Cdd:cd07090 162 LAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSvPTGkkvmsaaakgikhvtlelggkspliifddadlen 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 255 -------------------GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGA 314
Cdd:cd07090 242 avngammanflsqgqvcsnGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALiSEEHLEKVLGYIESAKQEGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 315 QVFQAGDVPS-----ERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQAL 388
Cdd:cd07090 322 KVLCGGERVVpedglENGFYvSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAH 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 223972653 389 ELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07090 402 RVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHY 446
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
42-434 |
8.65e-40 |
|
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: 153.04 E-value: 8.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 42 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGRAVREVRDGDVQLAQQLLHyHAIQA-------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGC 194
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLR-AAADAlkdfefeERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 195 TVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAF---------------------- 248
Cdd:cd07138 160 TVV--LKPSEVAPLsaiILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFtgstragkrvaeaaadtvkrva 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 249 -----------------------------------CGAPEgglRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:cd07138 238 lelggksaniilddadlekavprgvaacfansgqsCNAPT---RMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 -RGAAACDLVQRFVREAQSQGAQVFQAGdvpSERP-------FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEAL 365
Cdd:cd07138 315 lASAAQFDRVQGYIQKGIEEGARLVAGG---PGRPeglergyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 366 LVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINaHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07138 392 AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFL 459
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
43-434 |
1.01e-39 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 153.73 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAF-----KGWSAHPGVVRAQHLTRLAEVIQKHQR 117
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 118 LLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQAstqeEALAG------------------WEPMGVIGLILPPTFSF 179
Cdd:PLN02467 91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLA----EALDAkqkapvslpmetfkgyvlKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 180 LEMMWRICPALAVGCTVVaLVPP--ASPAPLLLAQLAGELGPFPGILNVLS--GPASLVPiLASQPGIRKVAFCGAPEGG 255
Cdd:PLN02467 166 LMATWKVAPALAAGCTAV-LKPSelASVTCLELADICREVGLPPGVLNVVTglGTEAGAP-LASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 L------------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRS 281
Cdd:PLN02467 244 RkimtaaaqmvkpvslelggkspiivfddvdldkavewamfgcfwtngqicsatsRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 282 GRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPS--ERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASP 357
Cdd:PLN02467 324 SDPLEEGCRLGPVvSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFiEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 358 FRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYL 480
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
43-420 |
2.31e-38 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 149.66 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAeaidkvygevATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE------------- 253
Cdd:PRK09847 183 AAGNSVI--LKPSEKSPLSairLAGLAKEAGLPDGVLNVVTGFGHEAgQALSRHNDIDAIAFTGSTRtgkqllkdagdsn 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 290
Cdd:PRK09847 261 mkrvwleaggksanivfadcpdlqqaasataagifynqgqvciAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 291 MGAR-GAAACDLVQRFVREAQSQGaQVFQAGDVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 369
Cdd:PRK09847 341 MGTLiDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAN 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 223972653 370 GTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:PRK09847 420 DSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSG 470
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
89-427 |
3.67e-38 |
|
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: 147.68 E-value: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLwtLESLV--TGrAVREVRDGDVQLAQQLLHYHA---------IQASTQE 157
Cdd:cd07104 12 AQKAWAATPPQERAAILRKAAEILEERRDEI--ADWLIreSG-STRPKAAFEVGAAIAILREAAglprrpegeILPSDVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 158 --EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP----LLLAQLAGELGPFPGILNVLSGPA 231
Cdd:cd07104 89 gkESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVV--LKPDSRTPvtggLLIAEIFEEAGLPKGVLNVVPGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 232 SLV-PILASQPGIRKVAFCGAPE--------------------GG------L---------------------------- 256
Cdd:cd07104 167 SEIgDALVEHPRVRMISFTGSTAvgrhigelagrhlkkvalelGGnnplivLddadldlavsaaafgaflhqgqicmaag 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPTLVS 335
Cdd:cd07104 247 RILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGpLINERQVDRVHAIVEDAVAAGARLLTGGTY--EGLFYQPTVLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 336 NLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTG 414
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDePHVPFG 404
|
410
....*....|...
gi 223972653 415 GCKESGCSWHGGP 427
Cdd:cd07104 405 GVKASGGGRFGGP 417
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
42-434 |
4.76e-38 |
|
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: 148.26 E-value: 4.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 42 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQA-QAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLEEVVGTFPLsTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST-----------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:cd07131 81 RLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCG--------------- 250
Cdd:cd07131 160 LVCGNTVV--FKPAEDTPACalkLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGstevgerigetcarp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ------------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDM 291
Cdd:cd07131 238 nkrvalemggknpiivmddadldlALEGALwsafgttgqrctatsRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 292 G-ARGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEAL 365
Cdd:cd07131 318 GpLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGyekgyFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 366 LVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAhglrdPSV------PTGGCKESGcswHGGPDGLYEYL 434
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNA-----PTIgaevhlPFGGVKKSG---NGHREAGTTAL 464
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
42-441 |
3.35e-36 |
|
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: 142.70 E-value: 3.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 42 HYVNGKWLKPEhRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:cd07086 1 GVIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGRAVREVRdGDVQ-----------LAQQLlhYHAIQASTQEE--ALAGWEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:cd07086 80 LVSLEMGKILPEGL-GEVQemidicdyavgLSRML--YGLTIPSERPGhrLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPL-------LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCG----------- 250
Cdd:cd07086 157 ALVCGNTVV--WKPSETTPLtaiavtkILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGstevgrrvget 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ----------------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 287
Cdd:cd07086 235 varrfgrvllelggnnaiivmddadldlAVRAVLfaavgtagqrctttrRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 288 AVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKE 363
Cdd:cd07086 315 GTLVGpLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEpgnYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 364 ALLVANGTPRGGSASVWSERLGQALE-LG-YGLQVGTVWINA-------HGlrdpsvPTGGCKESGcswhGGpdglyeyl 434
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRwLGpKGSDCGIVNVNIptsgaeiGG------AFGGEKETG----GG-------- 456
|
....*..
gi 223972653 435 RPSGTPA 441
Cdd:cd07086 457 RESGSDA 463
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
43-435 |
1.55e-35 |
|
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: 141.09 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST---------QEEALAGWEPMGVIGLILPPTFSFLEMMWRI 186
Cdd:cd07140 89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcdkIQGKTipinqarpnRNLTLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 187 CPALAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL------ 256
Cdd:cd07140 169 AACLAAGNTVV--LKPAQVTPLTalkFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKhimksc 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 287
Cdd:cd07140 247 avsnlkkvslelggkspliifadcdmdkavrmgmssvffnkgenciaagRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 288 AVDMGARGAAA-CDLVQRFVREAQSQGAQVFQAG-DVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAK-EA 364
Cdd:cd07140 327 STDHGPQNHKAhLDKLVEYCERGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 365 LLV-ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07140 407 VLQrANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLK 478
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
61-436 |
2.24e-35 |
|
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: 140.05 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQAstqEEALA-----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPA 203
Cdd:cd07099 81 LALEAIDWAARNA---PRVLAprkvptgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVV--LKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 204 SPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQpGIRKVAFCGAPEGGL------------------------ 256
Cdd:cd07099 156 EVTPLvgeLLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRkvmaaaaerlipvvlelggkdpmi 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDLVQRF 305
Cdd:cd07099 235 vladadleraaaaavwgamvnagqtcisveRVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARqLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 306 VREAQSQGAQVFQAGDVPSER-PFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERL 384
Cdd:cd07099 315 VDDAVAKGAKALTGGARSNGGgPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 223972653 385 GQALELGYGLQVGTVWINAHGLRD--PSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDVLLTAgiPALPFGGVKDSGGGRRHGAEGLREFCRP 448
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-420 |
2.88e-35 |
|
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: 139.79 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 57 VPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRd 136
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 137 GDVQLAQQLLHYHAIQASTQEE---------------ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVP 201
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGetipvdayeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVV--VK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 202 PASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL--------------------- 256
Cdd:cd07145 158 PSSNTPLtaiELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLliaskaggtgkkvalelggsd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ---------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLV 302
Cdd:cd07145 238 pmivlkdadleravsiavrgrfenagqvcnavkRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLiSPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 303 QRFVREAQSQGAQVFQAGDVPsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSE 382
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRD-EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430
....*....|....*....|....*....|....*....
gi 223972653 383 RLGQALELGYGLQVGTVWINAHG-LRDPSVPTGGCKESG 420
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTrFRWDNLPFGGFKKSG 435
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
42-420 |
3.61e-35 |
|
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: 139.69 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 42 HYVNGKWLKP----EHRNsvPCQdpiTGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQR 117
Cdd:cd07097 3 NYIDGEWVAGgdgeENRN--PSD---TSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 118 LLWTLESLVTGRAVREVRdGDVQLAQQLLHYHA---------IQASTQE--EALAGWEPMGVIGLILPPTFSFLEMMWRI 186
Cdd:cd07097 78 ELARLLTREEGKTLPEAR-GEVTRAGQIFRYYAgealrlsgeTLPSTRPgvEVETTREPLGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 187 CPALAVGCTVValVPPASPAPLLLAQLA---GELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL------ 256
Cdd:cd07097 157 APALAYGNTVV--FKPAELTPASAWALVeilEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRriaaaa 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGA 288
Cdd:cd07097 235 aargarvqlemggknplvvlddadldlavecavqgaffstgqrctassRLIVTEGIHDRFVEALVERTKALKVGDALDEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 289 VDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGD-VPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEA 364
Cdd:cd07097 315 VDIGpVVSERQLEKDLRYIEIARSEGAKLVYGGErLKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 365 LLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINA--HGLrDPSVPTGGCKESG 420
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptAGV-DYHVPFGGRKGSS 451
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
43-435 |
1.55e-34 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 138.42 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST--QEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAgaadkIHGETlkMSRQLQGYtlkEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE------------- 253
Cdd:PLN02766 184 AAGCTMV--VKPAEQTPlsaLFYAHLAKLAGVPDGVINVVTGFGPTAgAAIASHMDVDKVSFTGSTEvgrkimqaaatsn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDM 291
Cdd:PLN02766 262 lkqvslelggkspllifddadvdmavdlallgifynkgeicvASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 292 GAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 369
Cdd:PLN02766 342 GPQvDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYiEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKAN 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223972653 370 GTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:PLN02766 422 NTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
89-432 |
3.71e-34 |
|
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: 135.67 E-value: 3.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAstqEEALAG------ 162
Cdd:cd07100 11 AFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEAR-AEVEKCAWICRYYAENA---EAFLADepietd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 163 -------WEPMGVIGLILPPTFSFLEMMwRIC-PALAVGCTVvaLVPPASPAP---LLLAQLAGELGPFPGILNVLSGPA 231
Cdd:cd07100 87 agkayvrYEPLGVVLGIMPWNFPFWQVF-RFAaPNLMAGNTV--LLKHASNVPgcaLAIEELFREAGFPEGVFQNLLIDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 232 SLVPILASQPGIRKVAFCGAPEGG-----------------L-------------------------------------R 257
Cdd:cd07100 164 DQVEAIIADPRVRGVTLTGSERAGravaaeagknlkksvleLggsdpfivlddadldkavktavkgrlqnagqsciaakR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 258 LLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARgAAACDLVQRFVREAQSQGAQVFQAGDVPsERP--FYPPTL 333
Cdd:cd07100 244 FIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGplAR-KDLRDELHEQVEEAVAAGATLLLGGKRP-DGPgaFYPPTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 334 VSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPT 413
Cdd:cd07100 322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPF 401
|
410 420
....*....|....*....|..
gi 223972653 414 GGCKESGcswHG---GPDGLYE 432
Cdd:cd07100 402 GGVKRSG---YGrelGRFGIRE 420
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
42-435 |
2.49e-33 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 135.32 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 42 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAgwadkihgltVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPE-------------- 253
Cdd:PLN02466 220 LACGNTIVLKTAEQTPlSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDtgkivlelaaksnl 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -----------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 292
Cdd:PLN02466 300 kpvtlelggkspfivcedadvdkavelahfalffnqgqcccAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 293 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:PLN02466 380 PQiDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYiQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANN 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:PLN02466 460 TRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
61-420 |
5.74e-33 |
|
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: 132.72 E-value: 5.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR-KEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHA------------IQASTQEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASP 205
Cdd:cd07149 84 RAIETLRLSAeeakrlagetipFDASPGGEGRIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV--LKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 206 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL------------------------- 256
Cdd:cd07149 162 TPLsalKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEaiarkaglkkvtlelgsnaavivda 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ---------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVRE 308
Cdd:cd07149 242 dadlekavercvsgafanagqvcisvqRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMiSEAEAERIEEWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 309 AQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQAL 388
Cdd:cd07149 322 AVEGGARLLTGGKR--DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKAL 399
|
410 420 430
....*....|....*....|....*....|...
gi 223972653 389 ELGYGLQVGTVWIN-AHGLRDPSVPTGGCKESG 420
Cdd:cd07149 400 KAARELEVGGVMINdSSTFRVDHMPYGGVKESG 432
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
61-433 |
1.21e-32 |
|
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: 131.68 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQ 140
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-WFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHY-----HAIQASTQEEALAGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP-- 207
Cdd:cd07150 84 FTPELLRAaagecRRVRGETLPSDSPGTvsmsvrRPLGVVAGITPFNYPLILATKKVAFALAAGNTVV--LKPSEETPvi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 208 -LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL----------------------------- 256
Cdd:cd07150 162 gLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGReiaekagrhlkkitlelggknplivlada 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQ 310
Cdd:cd07150 242 dldyavraaafgafmhqgqicmsasRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGpLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 311 SQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALEL 390
Cdd:cd07150 322 AKGAKLLTGGKY--DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 223972653 391 GYGLQVGTVWINAHGLRD-PSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07150 400 AERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEF 443
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
43-434 |
5.87e-32 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 130.41 E-value: 5.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:PRK11241 94 MTLEQGKPLAEAK-GEISYAASFIEWFAEEGkriygdtipghQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCG----------------- 250
Cdd:PRK11241 173 AGCTMV--LKPASQTPfsaLALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGsteigrqlmeqcakdik 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ----------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:PRK11241 251 kvslelggnapfivfddadldkAVEGALaskfrnagqtcvcanRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPS-ERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGT 371
Cdd:PRK11241 331 LiDEKAVAKVEEHIADALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 372 PRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:PRK11241 411 EFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYL 473
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
474-716 |
7.07e-32 |
|
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: 129.86 E-value: 7.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 474 APPYGLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK 552
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINpATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPP-------------AERAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 --STLASRLER------------QGAELKAAEAEVELSARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVC 617
Cdd:COG1012 70 ilLRAADLLEErreelaalltleTGKPLAEARGEVDRAADFLRyYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 618 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS 696
Cdd:COG1012 150 PWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGS 229
|
250 260
....*....|....*....|.
gi 223972653 697 AQ-GSQFVEWAsAGNLKPVWA 716
Cdd:COG1012 230 TAvGRRIAAAA-AENLKRVTL 249
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
101-435 |
8.43e-32 |
|
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: 129.40 E-value: 8.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 101 RAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDgDVQLAQQLLHYHAIQA-STQEEALAG--------------WEP 165
Cdd:cd07146 42 RSAILNKAAALLEARREEFARLITLESGLCLKDTRY-EVGRAADVLRFAAAEAlRDDGESFSCdltangkarkiftlREP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 166 MGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSG-PASLVPILASQP 241
Cdd:cd07146 121 LGVVLAITPFNHPLNQVAHKIAPAIAANNRIV--LKPSEKTPLsaiYLADLLYEAGLPPDMLSVVTGePGEIGDELITHP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 242 GIRKVAFCGA-----------------------------PEGGL-----------------------RLLIQESVWDEAM 269
Cdd:cd07146 199 DVDLVTFTGGvavgkaiaatagykrqllelggndplivmDDADLeraatlavagsyansgqrctavkRILVHESVADEFV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 270 RRLQERMGRLRSGRGLDGAVDMGA---RGAAacDLVQRFVREAQSQGAQVFQAGdvpsER--PFYPPTLVSNLPPASPCA 344
Cdd:cd07146 279 DLLVEKSAALVVGDPMDPATDMGTvidEEAA--IQIENRVEEAIAQGARVLLGN----QRqgALYAPTVLDHVPPDAELV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 345 QVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN-AHGLRDPSVPTGGCKESGCsw 423
Cdd:cd07146 353 TEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNeVPGFRSELSPFGGVKDSGL-- 430
|
410
....*....|..
gi 223972653 424 hGGPDGLYEYLR 435
Cdd:cd07146 431 -GGKEGVREAMK 441
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
46-420 |
7.32e-30 |
|
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: 123.57 E-value: 7.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 46 GKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHqrllwtlESL 125
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEER-------RDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 126 VTGRAVREvrDGDVQLAQQLlHYHAIQASTQEEA--------------LAGWE------PMGVIGLILPPTFSFLEMMWR 185
Cdd:cd07151 74 IVEWLIRE--SGSTRIKANI-EWGAAMAITREAAtfplrmegrilpsdVPGKEnrvyrePLGVVGVISPWNFPLHLSMRS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 186 ICPALAVGCTVValVPPASPAP----LLLAQLAGELGPFPGILNVLSGPAS---------LVPILASQPGIRKV-----A 247
Cdd:cd07151 151 VAPALALGNAVV--LKPASDTPitggLLLAKIFEEAGLPKGVLNVVVGAGSeigdafvehPVPRLISFTGSTPVgrhigE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 248 FCG--------------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLD 286
Cdd:cd07151 229 LAGrhlkkvalelggnnpfvvledadidaAVNAAVfgkflhqgqicmainRIIVHEDVYDEFVEKFVERVKALPYGDPSD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 287 GAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEAL 365
Cdd:cd07151 309 PDTVVGPLiNESQVDGLLDKIEQAVEEGATLLVGGEA--EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 223972653 366 LVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTGGCKESG 420
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSG 442
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
61-436 |
1.96e-29 |
|
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: 122.16 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRD---- 136
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVevdr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 137 --GDVQLAQQLLHYH--------AIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPA 206
Cdd:cd07094 85 aiDTLRLAAEEAERIrgeeipldATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVV--LKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 207 PL---LLAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPE------------------GGL-------- 256
Cdd:cd07094 163 PLsalELAKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAvgealranaggkrialelGGNapvivdrd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 --------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREA 309
Cdd:cd07094 243 adldaaiealakggfyhagqvcisvqRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLiSEEAAERVERWVEEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 310 QSQGAQVFQAGDvpSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALE 389
Cdd:cd07094 323 VEAGARLLCGGE--RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 223972653 390 LGYGLQVGTVWINAHG-LRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07094 401 AAEKLEVGGVMVNDSSaFRTDWMPFGGVKESGVGREGVPYAMEEMTEE 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
61-433 |
4.54e-29 |
|
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: 121.26 E-value: 4.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYhaiqASTQEEALA----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPAS 204
Cdd:cd07101 82 VAIVARYY----ARRAERLLKprrrrgaipvltrttvNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 205 P-APLLLAQLAGELGPFPGILNVLSGPASLV--------------------PILASQPGIRKVAFC-------------- 249
Cdd:cd07101 158 AlTALWAVELLIEAGLPRDLWQVVTGPGSEVggaivdnadyvmftgstatgRVVAERAGRRLIGCSlelggknpmivled 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 250 --------GAPEGGL-----------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREA 309
Cdd:cd07101 238 adldkaaaGAVRACFsnagqlcvsieRIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSlISQAQLDRVTAHVDDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 310 QSQGAQVFQAGdvpSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERL 384
Cdd:cd07101 318 VAKGATVLAGG---RARPdlgpyFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 223972653 385 GQALELGYGLQVGTVWIN-----AHGLRDpsVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07101 395 ARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKY 446
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
42-420 |
5.88e-28 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 118.44 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 42 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQE---EALAG-------WEPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:PRK13252 89 LETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEgeqIPLRGgsfvytrREPLGVCAGIGAWNYPIQIACWKSAPALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCG-APEG------------- 254
Cdd:PRK13252 169 AGNAMI--FKPSEVTPLTalkLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGgVPTGkkvmaaaaaslke 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 255 ----------------------------------------GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR 294
Cdd:PRK13252 247 vtmelggksplivfddadldraadiamlanfyssgqvctnGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 295 -GAAACDLVQRFVREAQSQGAQVFQAGDVPSER-----PFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVA 368
Cdd:PRK13252 327 vSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfangAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 223972653 369 NGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:PRK13252 407 NDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSG 458
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
89-435 |
1.97e-27 |
|
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: 115.75 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGrAVREVRDGDVQLAQQLLHYHAIQASTQEE---------- 158
Cdd:cd07105 12 AFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-ATAAWAGFNVDLAAGMLREAASLITQIIGgsipsdkpgt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 159 -ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP-LLLAQLAGELGPFPGILNVLS-GP---AS 232
Cdd:cd07105 91 lAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRThWLIGRVFHEAGLPKGVLNVVThSPedaPE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 233 LVPILASQPGIRKVAFCG---------------------------------------APEGGL---------------RL 258
Cdd:cd07105 171 VVEALIAHPAVRKVNFTGstrvgriiaetaakhlkpvllelggkapaivledadldaAANAALfgaflnsgqicmsteRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 259 LIQESVWDEAMRRLQERMGRLRSGrgldGAVDMGARGAAACDLVQRFVREAQSQGAQVFqAGDVPSERP---FYPPTLVS 335
Cdd:cd07105 251 IVHESIADEFVEKLKAAAEKLFAG----PVVLGSLVSAAAADRVKELVDDALSKGAKLV-VGGLADESPsgtSMPPTILD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 336 NLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTG 414
Cdd:cd07105 326 NVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDePTLPHG 405
|
410 420
....*....|....*....|.
gi 223972653 415 GCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07105 406 GVKSSGYGRFNGKWGIDEFTE 426
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
89-433 |
5.05e-27 |
|
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: 114.70 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGrAVREVRDGDVQLAQQLLHyHAIQASTQEE---------- 158
Cdd:cd07152 25 AQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-SIRPKAGFEVGAAIGELH-EAAGLPTQPQgeilpsapgr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 159 -ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP--LLLAQLAGELGPFPGILNVLSGPASLVP 235
Cdd:cd07152 103 lSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggVVIARLFEEAGLPAGVLHVLPGGADAGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 236 ILASQPGIRKVAFCGAPEGGL------------------------------------------------------RLLIQ 261
Cdd:cd07152 183 ALVEDPNVAMISFTGSTAVGRkvgeaagrhlkkvslelggknalivlddadldlaasngawgaflhqgqicmaagRHLVH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 262 ESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDvpSERPFYPPTLVSNLPPA 340
Cdd:cd07152 263 ESVADAYTAKLAAKAKHLPVGDPATGQVALGPLiNARQLDRVHAIVDDSVAAGARLEAGGT--YDGLFYRPTVLSGVKPG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 341 SPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTGGCKES 419
Cdd:cd07152 341 MPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDePHNPFGGMGAS 420
|
410
....*....|....*
gi 223972653 420 GC-SWHGGPDGLYEY 433
Cdd:cd07152 421 GNgSRFGGPANWEEF 435
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
22-436 |
2.89e-26 |
|
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: 113.47 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 22 VPESHACALAWLDTQDRCLG-HY---VNGKWLKPEHR-NSV-PCQdpiTGENLASCLQAQAEDVAAAVEAARMAFKGWSA 95
Cdd:cd07124 11 DEENRAAFRAALARVREELGrEYplvIGGKEVRTEEKiESRnPAD---PSEVLGTVQKATKEEAEAAVQAARAAFPTWRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 96 HPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQAstqeEALAG------------- 162
Cdd:cd07124 88 TPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREM----LRLRGfpvemvpgednry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 163 -WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PIL 237
Cdd:cd07124 163 vYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVV--LKPAEDTPViaaKLVEILEEAGLPPGVVNFLPGPGEEVgDYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 238 ASQPGIRKVAFCGAPEGGL------------------------------------------------------------R 257
Cdd:cd07124 241 VEHPDVRFIAFTGSREVGLriyeraakvqpgqkwlkrviaemggknaiivdedadldeaaegivrsafgfqgqkcsacsR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 258 LLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGaQVFQAGDVPSERP---FYPPTL 333
Cdd:cd07124 321 VIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPViDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAegyFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 334 VSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS---ERLGQALElgyGLQVGTVWINahglRD-- 408
Cdd:cd07124 400 FADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSrspEHLERARR---EFEVGNLYAN----RKit 472
|
490 500 510
....*....|....*....|....*....|...
gi 223972653 409 ---PSV-PTGGCKESGC-SWHGGPDGLYEYLRP 436
Cdd:cd07124 473 galVGRqPFGGFKMSGTgSKAGGPDYLLQFMQP 505
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
51-433 |
2.97e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 110.35 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 51 PEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRA 130
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 131 VREVRDGDVQLAQQLLHYhaiqASTQEEALA----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGC 194
Cdd:PRK09407 108 RRHAFEEVLDVALTARYY----ARRAPKLLAprrragalpvltktteLRQPKGVVGVISPWNYPLTLAVSDAIPALLAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 195 TVVAlvPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV--------------------PILASQPGIRKVAFC-- 249
Cdd:PRK09407 184 AVVL--KPDSQTPltaLAAVELLYEAGLPRDLWQVVTGPGPVVgtalvdnadylmftgstatgRVLAEQAGRRLIGFSle 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 250 --------------------GAPEGGL-----------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAA 297
Cdd:PRK09407 262 lggknpmivlddadldkaaaGAVRACFsnagqlcisieRIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSlISEA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 298 ACDLVQRFVREAQSQGAQVFqAGDVPseRP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTP 372
Cdd:PRK09407 342 QLETVSAHVDDAVAKGATVL-AGGKA--RPdlgplFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTP 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223972653 373 RGGSASVWSERLGQALELGYGLQVGTVWIN-----AHGLRDpsVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:PRK09407 419 YGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKY 482
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
476-714 |
6.44e-25 |
|
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: 108.84 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSpgaraallwalAAALERRK-- 552
Cdd:cd07091 3 PTGLFINNEFvDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRK-----------MDPRERGRll 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLASRLERQGAELKAAEA-------------EVELSARRLR---AWGARVQaqGHTLQVAGlRGPVLRLREPLGVLAVV 616
Cdd:cd07091 72 NKLADLIERDRDELAALESldngkpleesakgDVALSIKCLRyyaGWADKIQ--GKTIPIDG-NFLAYTRREPIGVCGQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 617 CPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 695
Cdd:cd07091 149 IPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTG 228
|
250 260
....*....|....*....|
gi 223972653 696 S-AQGSQFVEWASAGNLKPV 714
Cdd:cd07091 229 StAVGRTIMEAAAKSNLKKV 248
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
43-420 |
1.29e-24 |
|
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: 108.04 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHrNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSA-HPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:cd07082 5 LINGEWKESSG-KTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGR----AVREV-RDGD--VQLAQQLLHYHA------IQASTQE-EALAGWEPMGVIgLILPP-------TFSfl 180
Cdd:cd07082 84 LLMWEIGKtlkdALKEVdRTIDyiRDTIEELKRLDGdslpgdWFPGTKGkIAQVRREPLGVV-LAIGPfnyplnlTVS-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 181 emmwRICPALAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV--PILASqPGIRKVAFCGAPEGG 255
Cdd:cd07082 161 ----KLIPALIMGNTVV--FKPATQGVLLgipLAEAFHDAGFPKGVVNVVTGRGREIgdPLVTH-GRIDVISFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 LRL----------------------------------------------------LIQESVWDEAMRRLQERMGRLRSGR 283
Cdd:cd07082 234 NRLkkqhpmkrlvlelggkdpaivlpdadlelaakeivkgalsysgqrctaikrvLVHESVADELVELLKEEVAKLKVGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 284 GLDGAVDMGA---RGAAacDLVQRFVREAQSQGAQVFQAGDVPSERPFYPpTLVSNLPPASPCAQVEVPWPVVVASPFRT 360
Cdd:cd07082 314 PWDNGVDITPlidPKSA--DFVEGLIDDAVAKGATVLNGGGREGGNLIYP-TLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 361 AKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSV-PTGGCKESG 420
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSG 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
477-714 |
2.71e-24 |
|
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: 107.04 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGRFQAP-GARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--S 553
Cdd:cd07559 1 YDNFINGEWVAPsKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSV-------------AERANilN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDE 620
Cdd:cd07559 68 KIADRIEENLELLAVAEtldngkpiretlaADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 621 WPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGS 700
Cdd:cd07559 148 FPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVG 227
|
250
....*....|....
gi 223972653 701 QFVEWASAGNLKPV 714
Cdd:cd07559 228 RLIMQYAAENLIPV 241
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
165-421 |
2.95e-24 |
|
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: 106.56 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 165 PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLVPILASQP 241
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV--LKPASRTPlsaLILGEVLAETGLPKGAFSVLPCSRDDADLLVTDE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 242 GIRKVAFCGAPEGGL----------------------------------------------------RLLIQESVWDEAM 269
Cdd:cd07147 201 RIKLLSFTGSPAVGWdlkaragkkkvvlelggnaavivdsdadldfaaqriifgafyqagqscisvqRVLVHRSVYDEFK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 270 RRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEV 348
Cdd:cd07147 281 SRLVARVKALKTGDPKDDATDVGPMiSESEAERVEGWVNEAVDAGAKLLTGGKR--DGALLEPTILEDVPPDMEVNCEEV 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 349 PWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN-AHGLRDPSVPTGGCKESGC 421
Cdd:cd07147 359 FGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVPTFRVDHMPYGGVKDSGI 432
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
499-714 |
2.97e-24 |
|
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: 106.64 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKS--TLASRLERQGAELKAAEA----- 571
Cdd:cd07092 5 ATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPA-------------ERSKAllKLADAIEENAEELAALESrntgk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 572 --------EVELSARRLR--AWGARVQ--------AQGHTLQVaglrgpvlrLREPLGVLAVVCPDEWPLLAFVSLLAPA 633
Cdd:cd07092 72 plhlvrddELPGAVDNFRffAGAARTLegpaageyLPGHTSMI---------RREPIGVVAQIAPWNYPLMMAAWKIAPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 634 LAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 713
Cdd:cd07092 143 LAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR 222
|
.
gi 223972653 714 V 714
Cdd:cd07092 223 V 223
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
165-434 |
3.97e-24 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 105.59 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 165 PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV-PILASQ 240
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIV--IKPSEFTPnnaIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 241 PGIRKVAFCGAPEGGL------------------------------------------------------RLLIQESVWD 266
Cdd:PRK10090 149 PKVAMVSMTGSVSAGEkimaaaaknitkvclelggkapaivmddadldlavkaivdsrvinsgqvcncaeRVYVQKGIYD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 267 EAMRRLQERMGRLRSGRGLDG-AVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPC 343
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPAERnDIAMGPLiNAAALERVEQKVARAVEEGARVALGGKAVEGKGyYYPPTLLLDVRQEMSI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 344 AQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSW 423
Cdd:PRK10090 309 MHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGG 388
|
330
....*....|.
gi 223972653 424 HGGPDGLYEYL 434
Cdd:PRK10090 389 ADGKHGLHEYL 399
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
254-430 |
5.99e-24 |
|
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: 105.84 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFqAGDVPSERP----- 327
Cdd:cd07098 268 GIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMiSPARFDRLEELVADAVEKGARLL-AGGKRYPHPeypqg 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 328 -FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL 406
Cdd:cd07098 347 hYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGV 426
|
170 180
....*....|....*....|....*.
gi 223972653 407 R--DPSVPTGGCKESGCSWHGGPDGL 430
Cdd:cd07098 427 NyyVQQLPFGGVKGSGFGRFAGEEGL 452
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
505-714 |
8.12e-24 |
|
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: 105.31 E-value: 8.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLER--QGAELKAAEAEVELSARRLRA 582
Cdd:pfam00171 21 ATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELA-ELETleNGKPLAEARGEVDRAIDVLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 583 W-GARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMAT 661
Cdd:pfam00171 100 YaGLARRLDGETLPSDPGRLAYTR-REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 662 V-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEwASAGNLKPV 714
Cdd:pfam00171 179 AgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvGRHIAE-AAAQNLKRV 232
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
480-714 |
3.24e-23 |
|
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: 103.93 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAF--PGWAGQSPGARAALLWALAAALERRKSTLA 556
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINpANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 sRLE--RQGAELKAAEAEVELSARRLRAW--------GARVQAQGHTLQVAglrgpvlrLREPLGVLAVVCPDEWPLLAF 626
Cdd:cd07119 81 -RLEtlNTGKTLRESEIDIDDVANCFRYYaglatketGEVYDVPPHVISRT--------VREPVGVCGLITPWNYPLLQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 627 VSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEW 705
Cdd:cd07119 152 AWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMR 231
|
....*....
gi 223972653 706 ASAGNLKPV 714
Cdd:cd07119 232 AAAGNVKKV 240
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
479-714 |
4.80e-23 |
|
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: 103.34 E-value: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFP--GWAGQSPgaraallwalaaaLERRK--S 553
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDpRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTG-------------YERSRilL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAE-------------AEVELSARRLRAW-GARVQAQGHTLQVAGLRGpVLRLREPLGVLAVVCPD 619
Cdd:cd07142 73 RFADLLEKHADELAALEtwdngkpyeqaryAEVPLAARLFRYYaGWADKIHGMTLPADGPHH-VYTLHEPIGVVGQIIPW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 620 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 698
Cdd:cd07142 152 NFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTE 231
|
250
....*....|....*..
gi 223972653 699 -GSQFVEWASAGNLKPV 714
Cdd:cd07142 232 vGKIIMQLAAKSNLKPV 248
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
480-698 |
6.19e-23 |
|
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: 102.71 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGARssRPIRDSS--GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS 557
Cdd:cd07097 4 YIDGEWVAGGDG--EENRNPSdtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 558 RLER-QGAELKAAEAEVELSARRLRAWGARVQAQ-GHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 635
Cdd:cd07097 82 LLTReEGKTLPEARGEVTRAGQIFRYYAGEALRLsGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 636 YGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 698
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTA 225
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
518-714 |
6.28e-23 |
|
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: 102.29 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 518 AVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLR---AWGARVQAQGHT 593
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLeTGKPIEEALGEVARAADTFRyyaGLARRLHGEVIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 594 LQVAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVT 672
Cdd:cd07078 83 SPDPGELA--IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVVT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 223972653 673 GDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRV 202
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
499-714 |
8.04e-23 |
|
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: 102.13 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLERQ--GAELKAAE-AEVEL 575
Cdd:cd07115 5 ATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELA-RLESLdtGKPIRAARrLDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 576 SARRLRAWGARVQAQGHtlQVAGLRGPVLR--LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 653
Cdd:cd07115 84 AADTFRYYAGWADKIEG--EVIPVRGPFLNytVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 654 EVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07115 162 RIAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRV 223
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
476-712 |
1.16e-22 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 101.91 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRFQAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKS-- 553
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPK-------------ERAEAll 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAEA-------------EVELSARRLR--AWGARVQ--------AQGHTLQVaglrgpvlRlREPL 610
Cdd:PRK13473 69 KLADAIEENADEFARLESlncgkplhlalndEIPAIVDVFRffAGAARCLegkaageyLEGHTSMI--------R-RDPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 611 GVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQA 690
Cdd:PRK13473 140 GVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRM 219
|
250 260
....*....|....*....|...
gi 223972653 691 MWYFGS-AQGSQFVEwASAGNLK 712
Cdd:PRK13473 220 VSLTGSiATGKHVLS-AAADSVK 241
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
500-714 |
2.23e-22 |
|
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: 100.87 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 500 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSAR 578
Cdd:cd07150 8 DGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEgGSTYGKAWFETTFTPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 579 RLRAWGARVQA-QGHTLQ--VAGLRGPVlrLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 655
Cdd:cd07150 88 LLRAAAGECRRvRGETLPsdSPGTVSMS--VRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 656 CQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07150 166 AEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKI 225
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
507-714 |
7.12e-22 |
|
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: 99.14 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLRAwga 585
Cdd:cd07106 13 APVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLeQGKPLAEAQFEVGGAVAWLRY--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 586 rvqaqghtlqVAGLRGPVLRLRE-----------PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALE 654
Cdd:cd07106 90 ----------TASLDLPDEVIEDddtrrvelrrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 655 VCQDMATVFPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07106 160 LGELAQEVLPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRV 218
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
505-741 |
9.18e-22 |
|
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: 98.97 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELK-AAEAEVELSARRLRA 582
Cdd:cd07108 11 GEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALEtGNALRtQARPEAAVLADLFRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 583 WGarvqaqghtlQVAG-LRGPVLRL---------REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:cd07108 91 FG----------GLAGeLKGETLPFgpdvltytvREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 653 LEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPVWASRG-------CPRAwD 725
Cdd:cd07108 161 LLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGgkspmivFPDA-D 239
|
250
....*....|....*.
gi 223972653 726 QEAEGAGPELGLRVAR 741
Cdd:cd07108 240 LDDAVDGAIAGMRFTR 255
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
507-715 |
1.01e-21 |
|
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: 98.83 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAFPG--WAGQSPgaraallwalaaalERRKSTL---ASRLERQGAEL-------------KA 568
Cdd:cd07112 18 VAACDAADVDRAVAAARRAFESgvWSRLSP--------------AERKAVLlrlADLIEAHRDELalletldmgkpisDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 569 AEAEVELSARRLRaWGARVQAQghtlqVAGLRGPV------LRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVM 642
Cdd:cd07112 84 LAVDVPSAANTFR-WYAEAIDK-----VYGEVAPTgpdalaLITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 643 VPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWASAGNLKPVW 715
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGStEVGRRFLEYSGQSNLKRVW 232
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
499-714 |
1.45e-21 |
|
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: 98.46 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--GAELKAAEAEVELS 576
Cdd:cd07109 5 STGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLdtGKPLTQARADVEAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 577 ARRLRAWGARVQA-QGHTLQVaglrGP---VLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:cd07109 85 ARYFEYYGGAADKlHGETIPL----GPgyfVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 653 LEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07109 161 LRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPV 223
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
476-714 |
1.65e-21 |
|
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: 98.37 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRFqAPGARSSRP--IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-WAGQSPGARA-ALLWALAAALERR 551
Cdd:cd07143 6 PTGLFINGEF-VDSVHGGTVkvYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGLKVSGSKRgRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 552 KSTLAS--RLERQGAELKAAEAEVELSARRLRAWGARV-QAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVS 628
Cdd:cd07143 85 LDYLASieALDNGKTFGTAKRVDVQASADTFRYYGGWAdKIHGQVIETDIKKLTYTR-HEPIGVCGQIIPWNFPLLMCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 629 LLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWA 706
Cdd:cd07143 164 KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGStLVGRKVMEAA 243
|
....*...
gi 223972653 707 SAGNLKPV 714
Cdd:cd07143 244 AKSNLKKV 251
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
40-402 |
2.45e-21 |
|
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: 97.97 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRdGDVQLAQQLLHY-----HAIQASTQEEALAG------WEPMGVIGLILPptFSFLEM--MWRI 186
Cdd:cd07085 81 ARLITLEHGKTLADAR-GDVLRGLEVVEFacsipHLLKGEYLENVARGidtysyRQPLGVVAGITP--FNFPAMipLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 187 CPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCG-----------AP 252
Cdd:cd07085 158 PMAIACGNTFV--LKPSERVPGaamRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGstpvgeyiyerAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 253 EGGLR-------------------------------------------LLIQESVWDEAMRRLQERMGRLRSGRGLDGAV 289
Cdd:cd07085 236 ANGKRvqalggaknhavvmpdadleqtanalvgaafgaagqrcmalsvAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 290 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAG-DVPSerPFYP------PTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07085 316 DMGPViSPAAKERIEGLIESGVEEGAKLVLDGrGVKV--PGYEngnfvgPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN 402
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN 434
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
499-714 |
4.34e-21 |
|
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: 97.06 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAEA----- 571
Cdd:cd07107 5 ATGQVLARVPAASAADVDRAVAAARAAFPEWRATTP-------------LERARmlRELATRLREHAEELALIDAldcgn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 572 -------EVELSARRLRAWGARV-QAQGHTLQVAGlRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMV 643
Cdd:cd07107 72 pvsamlgDVMVAAALLDYFAGLVtELKGETIPVGG-RNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 644 PSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07107 151 PPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHV 221
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
480-714 |
1.05e-20 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 95.80 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASR 558
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNpATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 559 L-ERQGAELKAAEAEVELSARRLR--AWGARvQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 635
Cdd:cd07088 81 IvEEQGKTLSLARVEVEFTADYIDymAEWAR-RIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 636 YGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
43-436 |
3.10e-20 |
|
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: 94.95 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKP-EHRNSVPCQDPitGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:cd07083 22 VIGGEWVDTkERMVSVSPFAP--SEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGRAVREVRDgDVQLAQQLLHYHAIQA---STQEEALAG---------WEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:cd07083 100 TLTYEVGKNWVEAID-DVAEAIDFIRYYARAAlrlRYPAVEVVPypgednesfYVGLGAGVVISPWNFPVAIFTGMIVAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVVAlvPPASPAPLLLA---QLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL--------- 256
Cdd:cd07083 179 VAVGNTVIA--KPAEDAVVVGYkvfEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKkiyeaaarl 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ---------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGL 285
Cdd:cd07083 257 apgqtwfkrlyvetggknaiivdetadfelvvegvvvsafgfqgqkcsaasRLILTQGAYEPVLERLLKRAERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 286 DGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFYPPTLVSNLPPASPCAQVEVPWPV--VVASPFRTAK 362
Cdd:cd07083 337 ENGTDLGPViDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVlsVIRYKDDDFA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 363 EALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAH--GLRDPSVPTGGCKESGCSWH-GGPDGLYEYLRP 436
Cdd:cd07083 417 EALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKitGALVGVQPFGGFKLSGTNAKtGGPHYLRRFLEM 493
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
499-698 |
1.58e-19 |
|
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: 92.03 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSA 577
Cdd:cd07145 7 ANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEvGKPIKQSRVEVERTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 578 R--RLRAWGARVqAQGHTLQVAGL----RGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLL 651
Cdd:cd07145 87 RlfKLAAEEAKV-LRGETIPVDAYeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 223972653 652 ALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 698
Cdd:cd07145 166 AIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTA 213
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
477-731 |
1.67e-19 |
|
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: 92.13 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07117 1 YGLFINGEWvKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASrLER--QGAELKAAEA-EVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAP 632
Cdd:cd07117 81 AM-VETldNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 633 ALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLK 712
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
|
250 260
....*....|....*....|....*..
gi 223972653 713 PVWASRGCPRA--------WDQEAEGA 731
Cdd:cd07117 240 PATLELGGKSAniifddanWDKALEGA 266
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
477-714 |
2.28e-19 |
|
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: 91.74 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGRFQAP-GARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--S 553
Cdd:cd07116 1 YDNFIGGEWVAPvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSV-------------AERANilN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDE 620
Cdd:cd07116 68 KIADRMEANLEMLAVAEtwdngkpvretlaADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 621 WPLLAFVSLLAPALAYGNTVVMVPSAACP---LLALEVCQDMatvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS- 696
Cdd:cd07116 148 FPLLMATWKLAPALAAGNCVVLKPAEQTPasiLVLMELIGDL---LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGEt 224
|
250
....*....|....*...
gi 223972653 697 AQGSQFVEWASAgNLKPV 714
Cdd:cd07116 225 TTGRLIMQYASE-NIIPV 241
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
477-712 |
2.40e-19 |
|
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: 91.69 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAgQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07111 22 FGHFINGKWVKPENRKSFPTINpATGEVLASVLQAEEEDVDAAVAAARTAFESWS-ALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLER--QGAELKAA-EAEVELSARRLRAWGarVQAQghtLQVAGLRGPvlrlrEPLGVLAVVCPDEWPLLAFVSLLAP 632
Cdd:cd07111 101 FAVLESldNGKPIRESrDCDIPLVARHFYHHA--GWAQ---LLDTELAGW-----KPVGVVGQIVPWNFPLLMLAWKICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 633 ALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDrDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAG 709
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALlfaEICAEAG--LPPGVLNIVTGN-GSFGSALANHPGVDKVAFTGSTEVGRALRRATAG 247
|
...
gi 223972653 710 NLK 712
Cdd:cd07111 248 TGK 250
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
520-714 |
2.53e-19 |
|
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: 90.37 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 520 EAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLR---AWGARVQAQGHTLQ 595
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLeTGKPIEEALGEVARAIDTFRyaaGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 596 VAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGD 674
Cdd:cd06534 81 DPGGEA--YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 223972653 675 RDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPV 198
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
479-719 |
4.61e-19 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 91.11 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRDSSGNLH-GYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGaraallwalaaaleRRKSTL 555
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPlAKIARGKSVDIDRAVSAARGVFERgdWSLSSPA--------------KRKAVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ---ASRLERQGAELKAAEA-------------EVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPD 619
Cdd:PRK09847 88 nklADLMEAHAEELALLETldtgkpirhslrdDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 620 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 698
Cdd:PRK09847 168 NFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTR 247
|
250 260
....*....|....*....|..
gi 223972653 699 -GSQFVEWASAGNLKPVWASRG 719
Cdd:PRK09847 248 tGKQLLKDAGDSNMKRVWLEAG 269
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
478-714 |
4.63e-19 |
|
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: 90.96 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 478 GLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-WAGQSPGARaallwalaaalERRKSTL 555
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNpATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAER-----------GRILLRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQGAELKAAEA-------------EVELSARRLR---AWGARVQaqGHTLQV-----AGLRGPVLRLREPLGVLA 614
Cdd:cd07113 70 ADLIEQHGEELAQLETlcsgksihlsrafEVGQSANFLRyfaGWATKIN--GETLAPsipsmQGERYTAFTRREPVGVVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 615 VVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQdMATV--FPAGLANVVTGDRDhLTRCLALHQDVQAMW 692
Cdd:cd07113 148 GIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAE-LAKEagIPDGVLNVVNGKGA-VGAQLISHPDVAKVS 225
|
250 260
....*....|....*....|..
gi 223972653 693 YFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07113 226 FTGSVATGKKIGRQAASDLTRV 247
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
476-714 |
5.83e-19 |
|
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: 90.63 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGARAALLWALAAALERRK 552
Cdd:cd07140 5 PHQLFINGEFvDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLAS--RLERQGAELKAAEAEVELSARRLR---AWGARVQaqGHTLQVAGLRgP----VLRLREPLGVLAVVCPDEWPL 623
Cdd:cd07140 85 EELATieSLDSGAVYTLALKTHVGMSIQTFRyfaGWCDKIQ--GKTIPINQAR-PnrnlTLTKREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 624 LAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQ 701
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPiGKH 241
|
250
....*....|...
gi 223972653 702 FVEWASAGNLKPV 714
Cdd:cd07140 242 IMKSCAVSNLKKV 254
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
479-714 |
7.33e-19 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 90.64 E-value: 7.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAF---PgWAGQSPgaraallwalaaaLERRKST 554
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDpRTGEVIAHVAEGDAEDVNRAVAAARKAFdegP-WPKMTA-------------YERSRIL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 555 L--ASRLERQGAEL-------------KAAEAEVELSARRLR---AW-----GARVQAQG-HTLQVaglrgpvlrLREPL 610
Cdd:PLN02466 126 LrfADLLEKHNDELaaletwdngkpyeQSAKAELPMFARLFRyyaGWadkihGLTVPADGpHHVQT---------LHEPI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 611 GVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQ 689
Cdd:PLN02466 197 GVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVD 276
|
250 260
....*....|....*....|....*.
gi 223972653 690 AMWYFGSAQGSQFV-EWASAGNLKPV 714
Cdd:PLN02466 277 KLAFTGSTDTGKIVlELAAKSNLKPV 302
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
499-712 |
8.56e-19 |
|
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: 90.10 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAF--PGWAgQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVEL 575
Cdd:cd07120 5 ATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALeNGKILGEARFEISG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 576 SARRLRAWG--ARVQAqGHTLQVAGLRGPVLrLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 653
Cdd:cd07120 84 AISELRYYAglARTEA-GRMIEPEPGSFSLV-LREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 654 EV--CQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLK 712
Cdd:cd07120 162 AIirILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLK 222
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
479-714 |
1.29e-18 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 89.88 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAF-----PGWAGQSPGaraallwalaaaleRRK 552
Cdd:PLN02766 23 LFINGEFvDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFdhgpwPRMSGFERG--------------RIM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLASRLERQGAELKAAEA-------------EVELSARRLRAW-GARVQAQGHTLQVAG-LRGpvLRLREPLGVLAVVC 617
Cdd:PLN02766 89 MKFADLIEEHIEELAALDTidagklfalgkavDIPAAAGLLRYYaGAADKIHGETLKMSRqLQG--YTLKEPIGVVGHII 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 618 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ--DMATVfPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 695
Cdd:PLN02766 167 PWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHlaKLAGV-PDGVINVVTGFGPTAGAAIASHMDVDKVSFTG 245
|
250 260
....*....|....*....|
gi 223972653 696 SAQ-GSQFVEWASAGNLKPV 714
Cdd:PLN02766 246 STEvGRKIMQAAATSNLKQV 265
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
476-714 |
1.64e-18 |
|
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: 89.39 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAraallwalaaalERRK-- 552
Cdd:cd07144 7 PTGLFINNEFVKSSDGETIKtVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGE------------ERGEll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLASRLERQGAELKAAEA----------------EVELSARRLRAWGARVQAQGHTLQVAGLRgpvLRLREPLGVLAVV 616
Cdd:cd07144 75 DKLADLVEKNRDLLAAIEAldsgkpyhsnalgdldEIIAVIRYYAGWADKIQGKTIPTSPNKLA---YTLHEPYGVCGQI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 617 CPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 695
Cdd:cd07144 152 IPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTG 231
|
250
....*....|....*....
gi 223972653 696 SAQGSQFVEWASAGNLKPV 714
Cdd:cd07144 232 STATGRLVMKAAAQNLKAV 250
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
471-714 |
4.71e-18 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 87.87 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 471 PSPAPPYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-----WAGQSPGARAALLWAL 544
Cdd:PLN02467 2 AIPVPRRQLFIGGEWREPVLGKRIPvVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 545 AAALERRKSTLAsRLERQ--GAELKAAEAEV-------ELSARRLRAWGARvQAQGHTLQVAGLRGPVlrLREPLGVLAV 615
Cdd:PLN02467 82 AAKITERKSELA-KLETLdcGKPLDEAAWDMddvagcfEYYADLAEALDAK-QKAPVSLPMETFKGYV--LKEPLGVVGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 616 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALE---VCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMW 692
Cdd:PLN02467 158 ITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLEladICREVG--LPPGVLNVVTGLGTEAGAPLASHPGVDKIA 235
|
250 260
....*....|....*....|..
gi 223972653 693 YFGSAQGSQFVEWASAGNLKPV 714
Cdd:PLN02467 236 FTGSTATGRKIMTAAAQMVKPV 257
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
479-696 |
6.14e-18 |
|
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: 87.17 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STL 555
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINpATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSV-------------EERAAllERI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQGAELKAAEAEvELSARRlrAWGARVQAQG------HTLQVAGL------RGPVLRLREPLGVLAVVCPDEWPL 623
Cdd:cd07138 68 AEAYEARADELAQAITL-EMGAPI--TLARAAQVGLgighlrAAADALKDfefeerRGNSLVVREPIGVCGLITPWNWPL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223972653 624 LAFVSLLAPALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS 696
Cdd:cd07138 145 NQIVLKVAPALAAGCTVVLKPSEVAPLSAIilaEILDEAG--LPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGS 218
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
507-714 |
6.78e-18 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 87.22 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAF--PGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAE--------AEVE 574
Cdd:cd07114 13 VPEASAADVDRAVAAARAAFegGAWRKLTP-------------TERGKllRRLADLIEANAEELAELEtrdngkliRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 575 LSARRLRAW-----GARVQAQGHTLQVAglRGPVLR--LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAA 647
Cdd:cd07114 80 AQVRYLAEWyryyaGLADKIEGAVIPVD--KGDYLNftRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 648 CPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07114 158 TPASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPV 225
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
479-716 |
7.92e-18 |
|
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: 87.19 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS 557
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNpATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 558 RLER-QGAELKAAEAEVelsARRLR----AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAP 632
Cdd:cd07085 83 LITLeHGKTLADARGDV---LRGLEvvefACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 633 ALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLAlHQDVQAMWYFGSAQGSQFVEWASAG 709
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMrlaELLQEAG--LPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAA 236
|
....*..
gi 223972653 710 NLKPVWA 716
Cdd:cd07085 237 NGKRVQA 243
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
499-714 |
9.99e-18 |
|
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: 86.47 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAE------ 570
Cdd:cd07093 5 ATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSP-------------AERARilHKVADLIEARADELALLEsldtgk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 571 -------AEVELSARRLRAWGARVQAQGHTL--QVAGLRGPVlrLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNT 639
Cdd:cd07093 72 pitlartRDIPRAAANFRFFADYILQLDGESypQDGGALNYV--LRQPVGVAGLITP--WnlPLMLLTWKIAPALAFGNT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 640 VVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 714
Cdd:cd07093 148 VVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGEtATGRTIMR-AAAPNLKPV 223
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
479-714 |
1.11e-17 |
|
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: 86.47 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSpATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQ-GAELKAAE-AEVELSARRLRAWGArvQAQGHTL---QVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLL 630
Cdd:cd07139 81 ARLWTAEnGMPISWSRrAQGPGPAALLRYYAA--LARDFPFeerRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 631 APALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRD---HLTRclalHQDVQAMWYFGSAQGSQFVE 704
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYllaEAAEEAG--LPPGVVNVVPADREvgeYLVR----HPGVDKVSFTGSTAAGRRIA 232
|
250
....*....|
gi 223972653 705 WASAGNLKPV 714
Cdd:cd07139 233 AVCGERLARV 242
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
89-434 |
1.22e-17 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 86.91 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQA-----STQEEALAG- 162
Cdd:PRK03137 85 AFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMlkladGKPVESRPGe 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 163 -----WEPMGViGLILPP-TFSFLEMMWRICPALAVGCTVVAlvPPASPAPLLLAQLAG---ELGPFPGILNVLSG-PAS 232
Cdd:PRK03137 164 hnryfYIPLGV-GVVISPwNFPFAIMAGMTLAAIVAGNTVLL--KPASDTPVIAAKFVEvleEAGLPAGVVNFVPGsGSE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 233 LVPILASQPGIRKVAFCGAPEGGL-------------------------------------------------------- 256
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLriyeraakvqpgqiwlkrviaemggkdaivvdedadldlaaesivasafgfsgqkc 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ----RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAvDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFYPP 331
Cdd:PRK03137 321 sacsRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPViNQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQP 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 332 TLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS---ERLGQALELgygLQVGTVWIN------ 402
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISnnrEHLEKARRE---FHVGNLYFNrgctga 476
|
410 420 430
....*....|....*....|....*....|....*.
gi 223972653 403 ---AHglrdpsvPTGGCKESGC-SWHGGPDGLYEYL 434
Cdd:PRK03137 477 ivgYH-------PFGGFNMSGTdSKAGGPDYLLLFL 505
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
499-714 |
2.05e-17 |
|
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: 85.48 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLERQGAELKAAEAEVELS-- 576
Cdd:cd07110 5 ATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELA-ELEARDNGKPLDEAAWDVDdv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 577 ----------ARRLRAWGARvqaqghTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSA 646
Cdd:cd07110 84 agcfeyyadlAEQLDAKAER------AVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 647 ACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07110 158 LTSLTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPV 226
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
257-420 |
2.91e-17 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 85.17 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGA-AACDLVQRFVREAQSQGAQVFQAGDVPsERP--FYPPTL 333
Cdd:PRK09406 270 RFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATeQGRDEVEKQVDDAVAAGATILCGGKRP-DGPgwFYPPTV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 334 VSNLPPASPCAQVEVPWPVvvASPFRTAK--EALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSV 411
Cdd:PRK09406 349 ITDITPDMRLYTEEVFGPV--ASLYRVADidEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPEL 426
|
....*....
gi 223972653 412 PTGGCKESG 420
Cdd:PRK09406 427 PFGGVKRSG 435
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
505-714 |
4.30e-17 |
|
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: 84.41 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLER-------------RKSTLAS--RLErQGAELKAA 569
Cdd:cd07103 11 GEVPDAGAADADAAIDAAAAAFKTWRKTTA-------------RERaailrrwadlireRAEDLARllTLE-QGKPLAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 570 EAEVELSARRLRaW----GARVQAQGHTLQVAGLRgpVLRLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNTVVMV 643
Cdd:cd07103 77 RGEVDYAASFLE-WfaeeARRIYGRTIPSPAPGKR--ILVIKQPVGVVAAITP--WnfPAAMITRKIAPALAAGCTVVLK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 644 PSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 714
Cdd:cd07103 152 PAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGStAVGKLLMA-QAADTVKRV 223
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
43-387 |
9.58e-17 |
|
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: 83.80 E-value: 9.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 43 YVNGKWLKPEHrnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:cd07130 2 VYDGEWGGGGG--VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRdGDVQ-----------LAQQLlhYHAIQAStqEEA----LAGWEPMGVIGLIlpPTFSFLEMMWRIC 187
Cdd:cd07130 80 VSLEMGKILPEGL-GEVQemidicdfavgLSRQL--YGLTIPS--ERPghrmMEQWNPLGVVGVI--TAFNFPVAVWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 188 PALAVGCTVVALVPPASPAPL-------LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPE------- 253
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLtaiavtkIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAvgrqvgq 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -------------GG----------------------------------LRLLIQESVWDEAMRRLQERMGRLRSGRGLD 286
Cdd:cd07130 233 avaarfgrsllelGGnnaiivmedadldlavravlfaavgtagqrctttRRLIVHESIYDEVLERLKKAYKQVRIGDPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 287 GAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGDVpSERP--FYPPTLVSNLPPAsPCAQVEVPWPVVVASPFRTAKE 363
Cdd:cd07130 313 DGTLVGPlHTKAAVDNYLAAIEEAKSQGGTVLFGGKV-IDGPgnYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDTLEE 390
|
410 420
....*....|....*....|....
gi 223972653 364 ALLVANGTPRGGSASVWSERLGQA 387
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNA 414
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
62-436 |
1.61e-16 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 82.68 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 62 PITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVR----EVRDG 137
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAqaggEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 138 D------VQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVvaLVPPASPAPLL-- 209
Cdd:cd07102 83 LerarymISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAV--ILKHSPQTPLCge 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 210 -LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGL-------------------------------- 256
Cdd:cd07102 161 rFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRaiqraaagrfikvglelggkdpayvrpdadld 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ----------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAAcDLVQRFVREAQSQ 312
Cdd:cd07102 241 aaaeslvdgaffnsgqsccsieRIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGpvVSARAA-DFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 313 GA------QVFQAGDVPSerPFYPPTLVSNLPPASPCAQVEVPWPVV----VASPfrtaKEALLVANGTPRGGSASVWSE 382
Cdd:cd07102 320 GAralidgALFPEDKAGG--AYLAPTVLTNVDHSMRVMREETFGPVVgimkVKSD----AEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 223972653 383 RLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRP 447
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
514-714 |
3.62e-16 |
|
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: 81.42 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 514 DIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLR-AWGARVQAQG 591
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIREsGSTRPKAAFEVGAAIAILReAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 592 HTLQvAGLRGPVLRL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACP-----LLAlEVCQDMAtvFPA 665
Cdd:cd07104 81 EILP-SDVPGKESMVrRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA-EIFEEAG--LPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 223972653 666 GLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKV 205
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
504-714 |
5.09e-16 |
|
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: 81.23 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 504 HGYV----AEGGAKDIRGAVEAAHQAFP-GWAGQSPGARAALLWALAAALERRKSTLASRLE--RQGAELKAAEAEVELS 576
Cdd:cd07118 6 HGVVvaryAEGTVEDVDAAVAAARKAFDkGPWPRMSGAERAAVLLKVADLIRARRERLALIEtlESGKPISQARGEIEGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 577 ARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 655
Cdd:cd07118 86 ADLWRyAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLML 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 656 CQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEwASAGNLKPV 714
Cdd:cd07118 166 AELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRvGKAIAA-AAARNLKKV 225
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
480-714 |
7.09e-16 |
|
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: 80.85 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRF--QAPGAR--SSRPIRDSsgNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07131 2 YIGGEWvdSASGETfdSRNPADLE--EVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQ-GAELKAAEAEVElsarrlRAWGARVQAQGHTLQVAGLRGP-------VLRLREPLGVLAVVCPDEWPLLAFV 627
Cdd:cd07131 80 ARLVTREmGKPLAEGRGDVQ------EAIDMAQYAAGEGRRLFGETVPselpnkdAMTRRQPIGVVALITPWNFPVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 628 SLLAPALAYGNTVVMVPSAACPLLALEVCQD-MATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWA 706
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVELfAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGET 233
|
....*...
gi 223972653 707 SAGNLKPV 714
Cdd:cd07131 234 CARPNKRV 241
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
477-688 |
4.15e-15 |
|
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: 78.80 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGR-FQAPGARSSRPIRDSSGNLhGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07124 33 YPLVIGGKeVRTEEKIESRNPADPSEVL-GTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQ-GAELKAAEAEV-------ELSARRLRAWGARVqaqghtlqVAGLRGPVLRLR-EPLGVLAVVCPDEWPLLAF 626
Cdd:cd07124 112 AAWMVLEvGKNWAEADADVaeaidflEYYAREMLRLRGFP--------VEMVPGEDNRYVyRPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 627 VSLLAPALAYGNTVVMVPSAACPLLA---LEVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDV 688
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAaklVEILEEAG--LPPGVVNFLPGPGEEVGDYLVEHPDV 246
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
61-433 |
1.72e-14 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 76.44 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQAST----------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCT-VVALVPPASPAPLL 209
Cdd:PRK13968 92 KSANLCDWYAEHGPAmlkaeptlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGyLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 210 LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGL--------------------------------- 256
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAaigaqagaalkkcvlelggsdpfivlndadlel 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ---------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAACDLVQRfVREAQSQG 313
Cdd:PRK13968 252 avkaavagryqntgqvcaaakRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGpmARFDLRDELHHQ-VEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 314 AQVFQAGD-VPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGY 392
Cdd:PRK13968 331 ARLLLGGEkIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 223972653 393 GLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:PRK13968 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
499-674 |
6.45e-14 |
|
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: 74.92 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKSTL---ASRLERQGAE---------- 565
Cdd:cd07082 24 IDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPL-------------EERIDCLhkfADLLKENKEEvanllmweig 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 566 --LKAAEAEVELSARRLRawgarvqaqgHTLQVAG-LRGPVLRL--------------REPLGVLAVVCPDEWPLLAFVS 628
Cdd:cd07082 91 ktLKDALKEVDRTIDYIR----------DTIEELKrLDGDSLPGdwfpgtkgkiaqvrREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 223972653 629 LLAPALAYGNTVVMVPSAACPLLA---LEVCQDMAtvFPAGLANVVTGD 674
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGiplAEAFHDAG--FPKGVVNVVTGR 207
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
507-714 |
1.31e-13 |
|
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: 73.92 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAF-PGwagqSPgaraallWALAAALERRK--STLASRLERQGAELKAAEA------------ 571
Cdd:cd07141 38 VQEGDKADVDKAVKAARAAFkLG----SP-------WRTMDASERGRllNKLADLIERDRAYLASLETldngkpfsksyl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 572 -EVELSARRLR---AWGARVQaqGHTLQVaglRGPVLRL--REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPS 645
Cdd:cd07141 107 vDLPGAIKVLRyyaGWADKIH--GKTIPM---DGDFFTYtrHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 646 AACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEWASAGNLKPV 714
Cdd:cd07141 182 EQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEvGKLIQQAAGKSNLKRV 252
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
505-714 |
1.75e-13 |
|
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: 73.43 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAraallwalaaalERRK--STLASRLERQGAELKA---AEA-------- 571
Cdd:cd07089 11 GTAPDAGAADVDAAIAAARRAFDTGDWSTDAE------------ERARclRQLHEALEARKEELRAllvAEVgapvmtar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 572 --EVELSARRLRAWG------ARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMV 643
Cdd:cd07089 79 amQVDGPIGHLRYFAdladsfPWEFDLPVPALRGGPGRRVVR-REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 644 PSAACPLLALEVCQDMA-TVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 714
Cdd:cd07089 158 PAPDTPLSALLLGEIIAeTDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGStAVGRRIMA-QAAATLKRV 229
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
500-698 |
1.81e-13 |
|
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: 73.40 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 500 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQGAE-LKAAEAEVELSAR 578
Cdd:cd07149 8 DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKpIKDARKEVDRAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 579 --RLRAWGARvQAQGHTLQVAGLRGPVLR----LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:cd07149 88 tlRLSAEEAK-RLAGETIPFDASPGGEGRigftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 223972653 653 LEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVqAMWYF-GSAQ 698
Cdd:cd07149 167 LKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRV-RMISFtGSPA 213
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
496-714 |
2.56e-13 |
|
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: 72.72 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 496 IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRKSTL-ASRLERQ------------ 562
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSG-------------MERGRILRkAADLLRErndeiarletid 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 563 -GAELKAAEAEVELSARRLRAWGARVQA-QGHTLQVAGLRGPVLRlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGN 638
Cdd:cd07090 69 nGKPIEEARVDIDSSADCLEYYAGLAPTlSGEHVPLPGGSFAYTR-REPLGV--CAGIGAWnyPIQIASWKSAPALACGN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 639 TVVMVPSAACPLLALEvcqdMATVF-----PAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 713
Cdd:cd07090 146 AMVYKPSPFTPLTALL----LAEILteaglPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH 220
|
.
gi 223972653 714 V 714
Cdd:cd07090 221 V 221
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
500-697 |
1.07e-12 |
|
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: 70.92 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 500 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSAR 578
Cdd:cd07094 8 DGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEgGKPIKDARVEVDRAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 579 RLRAWGARVQA-QGHTLQVAGLRGPVLRL----REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 653
Cdd:cd07094 88 TLRLAAEEAERiRGEEIPLDATQGSDNRLawtiREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 223972653 654 EVCQdmaTVFPAGLA----NVVTGDRDHLTRCLALHQDVQAMWYFGSA 697
Cdd:cd07094 168 ELAK---ILVEAGVPegvlQVVTGEREVLGDAFAADERVAMLSFTGSA 212
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
514-714 |
4.59e-12 |
|
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: 68.76 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 514 DIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRK--STLASRLERQGAELKAAEAE------------VELSARR 579
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPS-------------ERRDilLKAADLLESRRDEFIEAMMEetgataawagfnVDLAAGM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 580 LRAWGARV-QAQGHTLQVAGLRGPVLRLREPLGVLAVVCPdeW--PL-LAFVSLLAPaLAYGNTVVMVPSAACPLLALEV 655
Cdd:cd07105 68 LREAASLItQIIGGSIPSDKPGTLAMVVKEPVGVVLGIAP--WnaPViLGTRAIAYP-LAAGNTVVLKASELSPRTHWLI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 656 CQDM-ATVFPAGLANVVTGDRDH---LTRCLALHQDVQAMWYFGSAQ-GSQFVEWAsAGNLKPV 714
Cdd:cd07105 145 GRVFhEAGLPKGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRvGRIIAETA-AKHLKPV 207
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
44-402 |
4.47e-11 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 66.31 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 44 VNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLE 123
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 124 SLVTGRAVREvRDGDVQLAQQLLHYHAIQASTQE-----------EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAV 192
Cdd:PLN02419 198 TTEQGKTLKD-SHGDIFRGLEVVEHACGMATLQMgeylpnvsngvDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 193 GCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGLRLLIQESVwdeAMRR 271
Cdd:PLN02419 277 GNTFILKPSEKDPgASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAA---KGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 272 LQERMGRLRSGRGL-DGAVD----------MGARG--------------------------------------------- 295
Cdd:PLN02419 354 IQSNMGAKNHGLVLpDANIDatlnallaagFGAAGqrcmalstvvfvgdakswedklverakalkvtcgsepdadlgpvi 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 296 -AAACDLVQRFVREAQSQGAQVFQAGD---VPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 369
Cdd:PLN02419 434 sKQAKERICRLIQSGVDDGAKLLLDGRdivVPGYEKgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIIN 513
|
410 420 430
....*....|....*....|....*....|...
gi 223972653 370 GTPRGGSASVWSERLGQALELGYGLQVGTVWIN 402
Cdd:PLN02419 514 KNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
507-674 |
4.56e-11 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 65.87 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS--RLErQGAELKAAEAEVELSARRLRaWG 584
Cdd:PLN02278 56 VPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQlmTLE-QGKPLKEAIGEVAYGASFLE-YF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 585 AR--VQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPL--LALEVCQDMA 660
Cdd:PLN02278 134 AEeaKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLtaLAAAELALQA 213
|
170
....*....|....
gi 223972653 661 TVfPAGLANVVTGD 674
Cdd:PLN02278 214 GI-PPGVLNVVMGD 226
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
515-714 |
6.80e-11 |
|
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: 65.34 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 515 IRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLR---AWGARVQAQ 590
Cdd:cd07102 20 VRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQmGRPIAQAGGEIRGMLERARymiSIAEEALAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 591 GHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ--DMATVfPAGLA 668
Cdd:cd07102 100 IRVPEKDGFERYIRR--EPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAafAEAGL-PEGVF 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 223972653 669 NVVTGDRDHLTRCLALHqDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07102 177 QVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAGRFIKV 221
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
30-437 |
1.39e-10 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 64.47 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 30 LAWLDTQDRCLGHYVNGKWlkPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLA 109
Cdd:PLN02315 11 LSEIGLSSRNLGCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 110 EVIQKHQRLLWTLESLVTGR----AVREVR------DGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFSF 179
Cdd:PLN02315 89 DALRAKLDYLGRLVSLEMGKilaeGIGEVQeiidmcDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 180 LEMMWRICPALAVGCTVVALVPPASP-----APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEG 254
Cdd:PLN02315 169 AVLGWNACIALVCGNCVVWKGAPTTPlitiaMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 255 GL------------------------------------------------------RLLIQESVWDEAMRRLQERMGRLR 280
Cdd:PLN02315 249 GLmvqqtvnarfgkcllelsgnnaiivmddadiqlavrsvlfaavgtagqrcttcrRLLLHESIYDDVLEQLLTVYKQVK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 281 SGRGLDGAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGD-VPSERPFYPPTLVSnLPPASPCAQVEVPWPVVVASPF 358
Cdd:PLN02315 329 IGDPLEKGTLLGPlHTPESKKNFEKGIEIIKSQGGKILTGGSaIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKF 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 359 RTAKEALLVANGTPRGGSASVWSERLGQALElgyglqvgtvWINAH----GLRDPSVPT---------GGCKESGCSWHG 425
Cdd:PLN02315 408 KTLEEAIEINNSVPQGLSSSIFTRNPETIFK----------WIGPLgsdcGIVNVNIPTngaeiggafGGEKATGGGREA 477
|
490
....*....|..
gi 223972653 426 GPDGLYEYLRPS 437
Cdd:PLN02315 478 GSDSWKQYMRRS 489
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
501-676 |
1.65e-10 |
|
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: 63.78 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 501 GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARR 579
Cdd:cd07099 6 GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAeTGKPRADAGLEVLLALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 580 LRAW---GARVQAQGHTLQVAGLRGPVLRL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 655
Cdd:cd07099 86 IDWAarnAPRVLAPRKVPTGLLMPNKKATVeYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELL 165
|
170 180
....*....|....*....|..
gi 223972653 656 CQDMATV-FPAGLANVVTGDRD 676
Cdd:cd07099 166 AEAWAAAgPPQGVLQVVTGDGA 187
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
501-714 |
1.69e-10 |
|
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: 63.85 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 501 GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARR 579
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVREsGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 580 LR-AWGARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPllaleVCQD 658
Cdd:cd07152 81 LHeAAGLPTQPQGEILPSAPGRLSLAR-RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP-----VSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 659 M--ATVF-----PAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07152 155 VviARLFeeaglPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKV 216
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
42-420 |
5.54e-10 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 62.47 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 42 HYVNGKWLKPEHRNSVPCQDPITGE---NLASCLQAQAEDVAAAVeaaRMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRL 118
Cdd:PLN00412 18 YYADGEWRTSSSGKSVAITNPSTRKtqyKVQACTQEEVNKAMESA---KAAQKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 119 LwtLESLV------TGRAVREV-RDGDV----------QLAQ-QLLHYHAIQASTQEE-ALAGWEPMGVIGLILPPTFSF 179
Cdd:PLN00412 95 I--AECLVkeiakpAKDAVTEVvRSGDLisytaeegvrILGEgKFLVSDSFPGNERNKyCLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 180 LEMMWRICPALAVGCTVVaLVPP--ASPAPLLLAQ---LAGelgpFP-GILNVLSGPASLV-PILASQPGIRKVAFCGAP 252
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVV-LKPPtqGAVAALHMVHcfhLAG----FPkGLISCVTGKGSEIgDFLTMHPGVNCISFTGGD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 253 EG---------------------------------------------GLR------LLIQESVWDEAMRRLQERMGRLRS 281
Cdd:PLN00412 248 TGiaiskkagmvplqmelggkdacivledadldlaaaniikggfsysGQRctavkvVLVMESVADALVEKVNAKVAKLTV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 282 GRGLDGAVDMGARGAAACDLVQRFVREAQSQGAQVFQagDVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:PLN00412 328 GPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQ--EWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPS-VPTGGCKESG 420
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSG 465
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
257-432 |
1.03e-09 |
|
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: 61.28 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFqAGDVPSERPFYPPTLVS 335
Cdd:cd07148 270 RVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLiRPREVDRVEEWVNEAVAAGARLL-CGGKRLSDTTYAPTVLL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 336 NLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAH-GLRDPSVPTG 414
Cdd:cd07148 349 DPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHtAFRVDWMPFA 428
|
170
....*....|....*...
gi 223972653 415 GCKESGCSWHGGPDGLYE 432
Cdd:cd07148 429 GRRQSGYGTGGIPYTMHD 446
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
513-674 |
1.87e-09 |
|
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: 60.78 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 513 KDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--GAELKAAeAEVELSARRLRawgarvQAQ 590
Cdd:cd07151 32 EDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIREsgSTRIKAN-IEWGAAMAITR------EAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 591 GHTLQVAGLRGPVL------RL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACP----LLalevcqdM 659
Cdd:cd07151 105 TFPLRMEGRILPSDvpgkenRVyREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitggLL-------L 177
|
170 180
....*....|....*....|
gi 223972653 660 ATVF-----PAGLANVVTGD 674
Cdd:cd07151 178 AKIFeeaglPKGVLNVVVGA 197
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
514-698 |
1.87e-09 |
|
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: 60.36 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 514 DIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--------GAELKAAEAEVELS--ARRLRAW 583
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISREtgkplweaQTEVAAMAGKIDISikAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 584 GARVQAQGHTLqvaglrgpVLRLRePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV- 662
Cdd:cd07095 81 ERATPMAQGRA--------VLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAg 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 223972653 663 FPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQ 698
Cdd:cd07095 152 LPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAA 186
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
480-676 |
2.36e-09 |
|
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: 60.29 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGARssRPIRDSSGN--LHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL-- 555
Cdd:cd07125 36 IINGEETETGEG--APVIDPADHerTIGEVSLADAEDVDAALAIAAAAFAGWSATPV--------------EERAEILek 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 -ASRLERQGAELKA----------AEAEVELS---------ARRLRAWGARVQAQGHTLQVAGLRgpvlrlREPLGVLAV 615
Cdd:cd07125 100 aADLLEANRGELIAlaaaeagktlADADAEVReaidfcryyAAQARELFSDPELPGPTGELNGLE------LHGRGVFVC 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 616 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM--ATVfPAGLANVVTGDRD 676
Cdd:cd07125 174 ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheAGV-PRDVLQLVPGDGE 235
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
480-704 |
4.65e-09 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 59.54 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASR 558
Cdd:PRK11241 14 LINGEWlDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 559 LE-RQGAELKAAEAEVELSARRLRaWGARVQAQ--GHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 635
Cdd:PRK11241 94 MTlEQGKPLAEAKGEISYAASFIE-WFAEEGKRiyGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 636 YGNTVVMVPSAACPL--LALEVCQDMATVfPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVE 704
Cdd:PRK11241 173 AGCTMVLKPASQTPFsaLALAELAIRAGI-PAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEiGRQLME 243
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
505-713 |
1.02e-08 |
|
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: 58.38 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 583
Cdd:TIGR01238 66 GQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREaGKTIHNAIAEVREAVDFCRYY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 584 GARVQaqgHTLQVAGLRgpvlrlrePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV- 662
Cdd:TIGR01238 146 AKQVR---DVLGEFSVE--------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAg 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 223972653 663 FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 713
Cdd:TIGR01238 215 FPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDA 265
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
512-698 |
1.54e-08 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 57.66 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 512 AKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--------GAELKAAEAEVELSarrLRAW 583
Cdd:PRK09457 36 AAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAREtgkplweaATEVTAMINKIAIS---IQAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 584 GARVqaqGHTLQVAGLRGPVLRLRePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV--CQDMAT 661
Cdd:PRK09457 113 HERT---GEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTvkLWQQAG 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 223972653 662 VfPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQ 698
Cdd:PRK09457 189 L-PAGVLNLVQGGRE-TGKALAAHPDIDGLLFTGSAN 223
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
461-719 |
1.68e-08 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 57.83 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 461 STLPAGPEIGPSPAPPYGL--FVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAR 537
Cdd:PLN02419 96 SWLSTSPEQSTQPQMPPRVpnLIGGSFvESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 538 AALLWALAAALERRKSTLASRLE-RQGAELKAAEAEVELSARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAV 615
Cdd:PLN02419 176 QRVMLKFQELIRKNMDKLAMNITtEQGKTLKDSHGDIFRGLEVVEhACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 616 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ-DMATVFPAGLANVVTGDRDHLTrCLALHQDVQAMWYF 694
Cdd:PLN02419 256 ICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAElAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFV 334
|
250 260
....*....|....*....|....*
gi 223972653 695 GSAQGSQFVEWASAGNLKPVWASRG 719
Cdd:PLN02419 335 GSNTAGMHIYARAAAKGKRIQSNMG 359
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
560-708 |
2.20e-08 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 57.05 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 560 ERQGAELKAAEAEVELSARRLR---AWGARVQaqGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAY 636
Cdd:PRK10090 21 EEGGKIQQLAEVEVAFTADYIDymaEWARRYE--GEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 637 GNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWASA 708
Cdd:PRK10090 99 GNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSvSAGEKIMAAAAK 172
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
549-697 |
4.30e-08 |
|
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: 56.21 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 549 ERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAWGA---RVQAQGHTLQVAGLRGP--VLRLREPLGVLAVVCPDEWP 622
Cdd:cd07146 54 EARREEFARLITLEsGLCLKDTRYEVGRAADVLRFAAAealRDDGESFSCDLTANGKArkIFTLREPLGVVLAITPFNHP 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 623 LLAFVSLLAPALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSA 697
Cdd:cd07146 134 LNQVAHKIAPAIAANNRIVLKPSEKTPLSAIylaDLLYEAG--LPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGV 209
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
505-674 |
5.49e-08 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 56.10 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEV-------ELS 576
Cdd:PRK03137 65 GRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEaGKPWAEADADTaeaidflEYY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 577 ARRLRAWgarvqAQGHTlqVAGLRGPVLRLR-EPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 655
Cdd:PRK03137 145 ARQMLKL-----ADGKP--VESRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKF 217
|
170 180
....*....|....*....|
gi 223972653 656 CQDMATV-FPAGLANVVTGD 674
Cdd:PRK03137 218 VEVLEEAgLPAGVVNFVPGS 237
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
58-420 |
8.13e-08 |
|
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: 55.66 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 58 PCQDPITGE-NLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrD 136
Cdd:cd07125 49 PVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA-D 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 137 GDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASP 205
Cdd:cd07125 128 AEVREAIDFCRYYAAQArelfsdpelpgPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIA--KPAEQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 206 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE-----------------------GG--- 255
Cdd:cd07125 206 TPLiaaRAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTEtaklinralaerdgpilpliaetGGkna 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 ------------------------------LRLLI-QESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAAcDLV 302
Cdd:cd07125 286 mivdstalpeqavkdvvqsafgsagqrcsaLRLLYlQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGplIDKPAG-KLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 303 QRFVREAQSQGAQVFQAgDVPSERP-FYPPTLVSNlpPASPCAQVEVPWPV--VVASPFRTAKEALLVANGTPRGGSASV 379
Cdd:cd07125 365 RAHTELMRGEAWLIAPA-PLDDGNGyFVAPGIIEI--VGIFDLTTEVFGPIlhVIRFKAEDLDEAIEDINATGYGLTLGI 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 223972653 380 WSERLGQALELGYGLQVGTVWINahglRD------PSVPTGGCKESG 420
Cdd:cd07125 442 HSRDEREIEYWRERVEAGNLYIN----RNitgaivGRQPFGGWGLSG 484
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
515-714 |
9.64e-08 |
|
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: 55.16 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 515 IRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAEL------------KAAEAEVELSARRL 580
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSF-------------AERAAllRKLADLLRERKDELarlitlemgkpiAEARAEVEKCAWIC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 581 R--AWGARVQAQGHTLQVAGLRGPVlrLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNTVVMVPSAACPLLAL--- 653
Cdd:cd07100 68 RyyAENAEAFLADEPIETDAGKAYV--RYEPLGVVLGIMP--WnfPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALaie 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 654 EVCQDMAtvFPAGLANVVTGDRDHLTRCLAlHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07100 144 ELFREAG--FPEGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKS 201
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
505-654 |
1.32e-07 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 55.26 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL---ASRLERQGAELKA------------A 569
Cdd:PRK11905 582 GTVTEASAEDVERALAAAQAAFPEWSATPA--------------AERAAILeraADLMEAHMPELFAlavreagktlanA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 570 EAEVELSARRLRAWGARVQaqgHTLQVAGlrgpvlrlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVMVPSAA 647
Cdd:PRK11905 648 IAEVREAVDFLRYYAAQAR---RLLNGPG--------HKPLGP--VVCISPWnfPLAIFTGQIAAALVAGNTVLAKPAEQ 714
|
....*..
gi 223972653 648 CPLLALE 654
Cdd:PRK11905 715 TPLIAAR 721
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
557-714 |
2.19e-07 |
|
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: 54.07 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 SRLERQGAELKAAEAEVELSARRLRAWGARVQAQgHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPLLAFVSLLAPALAY 636
Cdd:cd07087 51 PPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRVS-VPLLLQPAKAYVIP--EPLGVVLIIGPWNYPLQLALAPLIGAIAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 637 GNTVVMVPSAACP----LLALEVcqdmATVFPAGLANVVTGDRDHLTRCLALHQDVqaMWYFGSAQGSQFVEWASAGNLK 712
Cdd:cd07087 128 GNTVVLKPSELAPatsaLLAKLI----PKYFDPEAVAVVEGGVEVATALLAEPFDH--IFFTGSPAVGKIVMEAAAKHLT 201
|
..
gi 223972653 713 PV 714
Cdd:cd07087 202 PV 203
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
475-714 |
3.46e-07 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 53.35 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 475 PPYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLER--- 550
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEvINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTA-------------MERsri 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 551 -RKStlASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQA-QGHTLQvagLRGP--VLRLREPLGVL 613
Cdd:PRK13252 72 lRRA--VDILRERNDELAALEtldtgkpiqetsvVDIVTGADVLEYYAGLAPAlEGEQIP---LRGGsfVYTRREPLGVC 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 614 AVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVcqdmATVF-----PAGLANVVTGDRDhLTRCLALHQDV 688
Cdd:PRK13252 147 AGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKL----AEIYteaglPDGVFNVVQGDGR-VGAWLTEHPDI 221
|
250 260
....*....|....*....|....*.
gi 223972653 689 QAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:PRK13252 222 AKVSFTGGVPTGKKVMAAAAASLKEV 247
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
500-676 |
5.74e-07 |
|
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: 52.63 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 500 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEV----- 573
Cdd:cd07147 8 TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEaGKPIKDARGEVaraid 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 574 --ELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLrePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLL 651
Cdd:cd07147 88 tfRIAAEEATRIYGEVLPLDISARGEGRQGLVRRF--PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLS 165
|
170 180
....*....|....*....|....*.
gi 223972653 652 ALEVCQDMA-TVFPAGLANVVTGDRD 676
Cdd:cd07147 166 ALILGEVLAeTGLPKGAFSVLPCSRD 191
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
549-684 |
7.66e-07 |
|
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: 52.23 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 549 ERRKSTLASRLER----------QGAELKAA--------EAEVELS------------ARRLRAWgARVQAQGHTLQVAG 598
Cdd:cd07134 13 ALRASTAAERIAKlkrlkkailaRREEIIAAlaadfrkpAAEVDLTeilpvlseinhaIKHLKKW-MKPKRVRTPLLLFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 599 LRGPVLRlrEPLGVLAVVCPDEWPL-LAFvSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDH 677
Cdd:cd07134 92 TKSKIRY--EPKGVCLIISPWNYPFnLAF-GPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEV 168
|
....*..
gi 223972653 678 LTRCLAL 684
Cdd:cd07134 169 AQALLEL 175
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
557-714 |
1.18e-06 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 51.95 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 SRLERQGAELKAAEAEVELSARRLRAWGARVQAQGHTLQvagLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAY 636
Cdd:PTZ00381 60 HPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVF---GPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 637 GNTVVMVPSAacplLALEVCQDMATVFPAGLAN----VVTGDRDHLTRCLALHQDVqaMWYFGSAQGSQFVEWASAGNLK 712
Cdd:PTZ00381 137 GNTVVLKPSE----LSPHTSKLMAKLLTKYLDPsyvrVIEGGVEVTTELLKEPFDH--IFFTGSPRVGKLVMQAAAENLT 210
|
..
gi 223972653 713 PV 714
Cdd:PTZ00381 211 PC 212
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
480-698 |
1.34e-06 |
|
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: 51.41 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGAR---SSRPIRDSSgnlHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLA 556
Cdd:cd07086 2 VIGGEWVGSGGEtftSRNPANGEP---IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 SRLERQ-GAELKAAEAEVE-----------LSaRRLrawgarvqaQGHTlqVAGLRgPVLRLRE---PLGVLAVVCPDEW 621
Cdd:cd07086 79 RLVSLEmGKILPEGLGEVQemidicdyavgLS-RML---------YGLT--IPSER-PGHRLMEqwnPLGVVGVITAFNF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 622 PLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-----FPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGS 696
Cdd:cd07086 146 PVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVlekngLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGS 224
|
..
gi 223972653 697 AQ 698
Cdd:cd07086 225 TE 226
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
609-699 |
4.69e-06 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 49.75 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 609 PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVP---SAACPLLALEvCQDMATvFPAGLANVVTGDRDHLTRCLALH 685
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPptqGAVAALHMVH-CFHLAG-FPKGLISCVTGKGSEIGDFLTMH 235
|
90
....*....|....
gi 223972653 686 QDVQAMWYFGSAQG 699
Cdd:PLN00412 236 PGVNCISFTGGDTG 249
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-258 |
1.05e-05 |
|
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: 48.42 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 87 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ-----LAQQLLHYHAiQASTQEEALA 161
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAamagkIDISIKAYHE-RTGERATPMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 162 GWE------PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPAS 232
Cdd:cd07095 88 QGRavlrhrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVV--FKPSELTPAvaeLMVELWEEAGLPPGVLNLVQGGRE 165
|
170 180
....*....|....*....|....*.
gi 223972653 233 LVPILASQPGIRKVAFCGAPEGGLRL 258
Cdd:cd07095 166 TGEALAAHEGIDGLLFTGSAATGLLL 191
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
490-657 |
1.27e-05 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 48.66 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 490 ARSSRPIRDSSGNLH------------GYVAEGGAKDIRGAVEAAHQAFPGWAgQSPGaraallwalaaalERRKSTL-- 555
Cdd:PRK11904 550 QWQAGPIINGEGEARpvvspadrrrvvGEVAFADAEQVEQALAAARAAFPAWS-RTPV-------------EERAAILer 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 -ASRLERQGAELKA------------AEAEVELSARRLRAWGArvQAQGHTLQVAGLRGPV-----LRLrEPLGVLAVVC 617
Cdd:PRK11904 616 aADLLEANRAELIAlcvreagktlqdAIAEVREAVDFCRYYAA--QARRLFGAPEKLPGPTgesneLRL-HGRGVFVCIS 692
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 223972653 618 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ 657
Cdd:PRK11904 693 PWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVK 732
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
605-701 |
2.15e-05 |
|
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: 47.62 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 605 RLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM--ATVFPAGLANVVTGDRdHLTRCL 682
Cdd:cd07084 96 GYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLhyAGLLPPEDVTLINGDG-KTMQAL 174
|
90
....*....|....*....
gi 223972653 683 ALHQDVQAMWYFGSAQGSQ 701
Cdd:cd07084 175 LLHPNPKMVLFTGSSRVAE 193
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
487-674 |
5.14e-05 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 46.41 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 487 APGARSSRPIRDS-SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKSTLASR---LERQ 562
Cdd:PRK09407 27 DGAAGPTREVTAPfTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVR-------------ERAAVLLRFHdlvLENR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 563 GAELKAAEAEvelsarrlrAWGARVQAQGHTLQVAGL-----------------RG--PVL----RLREPLGVLAVVCPD 619
Cdd:PRK09407 94 EELLDLVQLE---------TGKARRHAFEEVLDVALTaryyarrapkllaprrrAGalPVLtkttELRQPKGVVGVISPW 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 620 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALeVCQDMATV--FPAGLANVVTGD 674
Cdd:PRK09407 165 NYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTAL-AAVELLYEagLPRDLWQVVTGP 220
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
249-425 |
5.54e-05 |
|
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: 46.45 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 249 CGAPEgglRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR--GAAACDLVQRFVREAQSQGAQVFQAGDVPSER 326
Cdd:cd07134 240 CIAPD---YVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARivNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQ 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 327 PFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN---A 403
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNdvvL 396
|
170 180
....*....|....*....|...
gi 223972653 404 HGLrDPSVPTGGCKESGC-SWHG 425
Cdd:cd07134 397 HFL-NPNLPFGGVNNSGIgSYHG 418
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
41-258 |
9.32e-05 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 45.72 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 41 GHYVNGKWL--KPEHRNSVpcqDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRL 118
Cdd:PRK09457 2 TLWINGDWIagQGEAFESR---NPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 119 LWTLESLVTGRAVREVRD------GDVQLAQQllHYHAIQASTQEEALAG-----WEPMGVIGLILPPTFSFLEMMWRIC 187
Cdd:PRK09457 79 LAEVIARETGKPLWEAATevtamiNKIAISIQ--AYHERTGEKRSEMADGaavlrHRPHGVVAVFGPYNFPGHLPNGHIV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 188 PALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGLRL 258
Cdd:PRK09457 157 PALLAGNTVV--FKPSELTPWvaeLTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLL 228
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
607-714 |
1.70e-04 |
|
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: 44.80 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 607 REPLGVLAVVCPDEWPL-LAFVSLLApALAYGNTVVMVPSAACPLLAlEVCQDM-ATVFPAGLANVVTGDRD---HLtrc 681
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFqLALAPLIG-AIAAGNTAVLKPSELTPNTS-KVIAKIiEETFDEEYVAVVEGGVEenqEL--- 172
|
90 100 110
....*....|....*....|....*....|...
gi 223972653 682 laLHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07136 173 --LDQKFDYIFFTGSVRVGKIVMEAAAKHLTPV 203
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
557-676 |
2.26e-04 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 44.40 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 SRLERQGAELKAAEAEVELSARRLRAWgARVQAQGHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPL-LAFVSLLApALA 635
Cdd:cd07133 52 SRHETLLAEILPSIAGIKHARKHLKKW-MKPSRRHVGLLFLPAKAEVEY--QPLGVVGIIVPWNYPLyLALGPLIA-ALA 127
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 223972653 636 YGNTVVMVPSAACPLLAlEVCQDM-ATVFPAGLANVVTGDRD 676
Cdd:cd07133 128 AGNRVMIKPSEFTPRTS-ALLAELlAEYFDEDEVAVVTGGAD 168
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
93-253 |
2.58e-04 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 44.58 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 93 WSAHPGVVRAQHLTRLAEVIQKH-QRLLWTL--ESLVT-GRAVREVRDgdvqlAQQLLHYHAIQAStQEEALAGWEPMGV 168
Cdd:PRK11809 698 WFATPPAERAAILERAADLMEAQmQTLMGLLvrEAGKTfSNAIAEVRE-----AVDFLRYYAGQVR-DDFDNDTHRPLGP 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 169 IGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASPAPLLLAQ---LAGELGPFPGILNVLSGPASLV-PILASQPGIR 244
Cdd:PRK11809 772 VVCISPWNFPLAIFTGQVAAALAAGNSVLA--KPAEQTPLIAAQavrILLEAGVPAGVVQLLPGRGETVgAALVADARVR 849
|
....*....
gi 223972653 245 KVAFCGAPE 253
Cdd:PRK11809 850 GVMFTGSTE 858
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
505-652 |
2.85e-04 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 44.54 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL---ASRLERQGAELKA------------A 569
Cdd:COG4230 585 GTVVEATAADVEAALAAAQAAFPAWSATPV--------------EERAAILeraADLLEAHRAELMAllvreagktlpdA 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 570 EAEVelsarR-----LRAWGARVQAQGHTLQVaglrgpvlrlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVM 642
Cdd:COG4230 651 IAEV-----ReavdfCRYYAAQARRLFAAPTV----------LRGRGV--FVCISPWnfPLAIFTGQVAAALAAGNTVLA 713
|
170
....*....|
gi 223972653 643 VPSAACPLLA 652
Cdd:COG4230 714 KPAEQTPLIA 723
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
89-250 |
2.99e-04 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 44.42 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQAS---TQEEALA 161
Cdd:PRK11904 597 AFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKtlqdAIAEVRE-----AVDFCRYYAAQARrlfGAPEKLP 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 162 G---------WEPMGVIGLILPPTFS---FLEmmwRICPALAVGCTVVAlvPPASPAPL---LLAQLAGELGPFPGILNV 226
Cdd:PRK11904 672 GptgesnelrLHGRGVFVCISPWNFPlaiFLG---QVAAALAAGNTVIA--KPAEQTPLiaaEAVKLLHEAGIPKDVLQL 746
|
170 180
....*....|....*....|....*
gi 223972653 227 LSGP-ASLVPILASQPGIRKVAFCG 250
Cdd:PRK11904 747 LPGDgATVGAALTADPRIAGVAFTG 771
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
607-714 |
3.60e-04 |
|
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: 43.75 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 607 REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQ 686
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQGGVPETTALLEQKF 185
|
90 100
....*....|....*....|....*...
gi 223972653 687 DvqAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07135 186 D--KIFYTGSGRVGRIIAEAAAKHLTPV 211
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
505-713 |
3.91e-04 |
|
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: 43.72 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 583
Cdd:cd07083 47 GTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEvGKNWVEAIDDVAEAIDFIRYY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 584 GarVQAQGHTLQVAGLRGPVLRLRE----PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM 659
Cdd:cd07083 127 A--RAALRLRYPAVEVVPYPGEDNEsfyvGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIF 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 660 ATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVeWASAGNLKP 713
Cdd:cd07083 205 HEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKI-YEAAARLAP 258
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
606-674 |
7.73e-04 |
|
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: 42.68 E-value: 7.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 606 LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM-ATVFPAGLANVVTGD 674
Cdd:cd07101 115 NRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLiEAGLPRDLWQVVTGP 184
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
505-652 |
7.80e-04 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 43.04 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 583
Cdd:PRK11809 674 GYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREaGKTFSNAIAEVREAVDFLRYY 753
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 584 GARVQAQ----GHtlqvaglrgpvlrlrEPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:PRK11809 754 AGQVRDDfdndTH---------------RPLGP--VVCISPWnfPLAIFTGQVAAALAAGNSVLAKPAEQTPLIA 811
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
608-721 |
8.33e-04 |
|
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: 42.40 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 608 EPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAlevcQDMATVFPAGLAN----VVTGDRDHLTrcLA 683
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATS----ALLAKLIPEYLDTkaikVIEGGVPETT--AL 173
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 223972653 684 LHQDVQAMWYFGSAQGSQFVEWASAGNLKPVWASRG--CP 721
Cdd:cd07137 174 LEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGgkCP 213
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
607-714 |
8.84e-04 |
|
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: 42.59 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 607 REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAlevcQDMATVFPAGLAN----VVTGDRDHLTRCL 682
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA----KLLAELIPKYLDKecypVVLGGVEETTELL 173
|
90 100 110
....*....|....*....|....*....|..
gi 223972653 683 ALHQDVqaMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07132 174 KQRFDY--IFYTGSTSVGKIVMQAAAKHLTPV 203
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
87-258 |
3.03e-03 |
|
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: 40.68 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 87 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQqLLHYHAIQASTQEEALAGWE-- 164
Cdd:cd07084 9 DISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQ-LRARAFVIYSYRIPHEPGNHlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 165 ------------PMGVIGLILPPTFSFLEMMWRICPALAVGCTVvaLVPPASPAPLLLAQ---LAGELGPFP-GILNVLS 228
Cdd:cd07084 88 qglkqqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPV--IVKPHTAVSIVMQImvrLLHYAGLLPpEDVTLIN 165
|
170 180 190
....*....|....*....|....*....|
gi 223972653 229 GPASLVPILASQPGIRKVAFCGAPEGGLRL 258
Cdd:cd07084 166 GDGKTMQALLLHPNPKMVLFTGSSRVAEKL 195
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
515-699 |
3.60e-03 |
|
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: 40.60 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 515 IRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKS---TLASRLERQGAELKA-AEAEVELSARRL-----RAWG- 584
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSP--------------ARRAAfleAIADEIEALGDELVArAHAETGLPEARLqgelgRTTGq 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 585 ----ARVQAQGHTLQV---------AGLRGPVLRLRE-PLGVLAVVCPDEWPlLAFvSLL----APALAYGNTVVMVPSA 646
Cdd:cd07129 67 lrlfADLVREGSWLDAridpadpdrQPLPRPDLRRMLvPLGPVAVFGASNFP-LAF-SVAggdtASALAAGCPVVVKAHP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 647 ACP----LLALEVCQDM-ATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQG 699
Cdd:cd07129 145 AHPgtseLVARAIRAALrATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRG 202
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
573-667 |
3.64e-03 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 40.48 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 573 VELSARRLRAWGARVQAQGHTLQVAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:cd07148 90 VELAADELGQLGGREIPMGLTPASAGRIA--FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSC 167
|
90
....*....|....*
gi 223972653 653 LEVcqdMATVFPAGL 667
Cdd:cd07148 168 LAF---VDLLHEAGL 179
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
82-278 |
4.03e-03 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 40.62 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 82 AVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQAsTQE 157
Cdd:PRK11905 595 ALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKtlanAIAEVRE-----AVDFLRYYAAQA-RRL 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 158 EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASPAPlLLAQLAGEL----GPFPGILNVLSGPASL 233
Cdd:PRK11905 669 LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA--KPAEQTP-LIAARAVRLlheaGVPKDALQLLPGDGRT 745
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 223972653 234 V-PILASQPGIRKVAFCGAPEGGlrLLIQesvwdeamRRLQERMGR 278
Cdd:PRK11905 746 VgAALVADPRIAGVMFTGSTEVA--RLIQ--------RTLAKRSGP 781
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
82-250 |
5.35e-03 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 40.31 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 82 AVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQASTQE 157
Cdd:COG4230 598 ALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKtlpdAIAEVRE-----AVDFCRYYAAQARRLF 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 158 EALAGWEPMGVIGLILPptfsflemmW---------RICPALAVGCTVVAlvPPASPAPlLLAQLAGEL----GPFPGIL 224
Cdd:COG4230 673 AAPTVLRGRGVFVCISP---------WnfplaiftgQVAAALAAGNTVLA--KPAEQTP-LIAARAVRLlheaGVPADVL 740
|
170 180
....*....|....*....|....*..
gi 223972653 225 NVLSGPASLV-PILASQPGIRKVAFCG 250
Cdd:COG4230 741 QLLPGDGETVgAALVADPRIAGVAFTG 767
|
|
| |
