|
Name |
Accession |
Description |
Interval |
E-value |
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
3-537 |
0e+00 |
|
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441878 [Multi-domain] Cd Length: 531 Bit Score: 703.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 3 NSKTYDYIIIGGGSAGSVLAARLAEQADLKICLIEAGSRDETPRIQTPAGTITLYKSKKFSWNFYSTPQKSLGGRQIHVP 82
Cdd:COG2303 1 MLEEYDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRDDDPLIRMPAGYAKLLGNPRYDWRYETEPQPGLNGRRLYWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 83 RGKALGGSSSMNSMIYIRGLPSDYDRWEQQGCEGWGWNNVLPWFKRSEKNLLSQDpAYHGFNGELLVDKPRDPNPVSALF 162
Cdd:COG2303 81 RGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGAD-AYHGRSGPLPVSDPPLPNPLSDAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 163 VAAGKRVGLAENTDFNGKSLAGVGIYNVTQKDGKRLSSYRAFLHPHIGRSNLTVMTDCTVQTLIIEDKAVKGVRITEHGR 242
Cdd:COG2303 160 IEAAEELGIPRADDFNGGACEGCGFCQVTCRNGARWSAARAYLPPALKRPNLTVRTGALVTRILFDGGRATGVEYRDDGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 243 DQptSILCRHEVILSAGSIGSPHILLKSGIGPAAELEAAGIPLVHPLPGVGKNLQDHLDGLVTVRSRNPLTLGFSLAAWK 322
Cdd:COG2303 240 EH--TVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLPGVGRNLQDHLEVSVVFRFKEPVTLNKSLRKAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 323 PILtspfQYLFRRNGWLTTNYVEAGGFAATKLSSDEPDIQFHFVP-GYRSHRGRL-FEWGHGYAIHTCVLRPRSIGALQL 400
Cdd:COG2303 318 IGL----QYLLTRSGPLTSNVAEAGGFFRSDPGLERPDLQFHFLPlGLTPRWGKKaLHDGHGFTAHVEQLRPESRGRVTL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 401 K-RD--GQIAIDFNFLADPYDASVLVEGIKVARNILAQPEFNALHGEEMLPGKHIQTDEQLhQYVKEYCATVFHPVGTCK 477
Cdd:COG2303 394 DsADplGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPYRGEEILPGPDVQSDEEL-AFIRARAYTIYHPVGTCR 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 478 MGRDEMSVVAPDtLKVYGVENLRVADASIMPTLISGNTNAPSIMIGERAASMILQGTPVA 537
Cdd:COG2303 473 MGTDPDSVVDPR-LRVHGVENLRVVDASVMPTITSGNTNAPTIMLAEKAADMILGDYLKN 531
|
|
| PRK02106 |
PRK02106 |
choline dehydrogenase; Validated |
4-537 |
0e+00 |
|
choline dehydrogenase; Validated
Pssm-ID: 235000 [Multi-domain] Cd Length: 560 Bit Score: 572.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 4 SKTYDYIIIGGGSAGSVLAARLAEQADLKICLIEAGSRDE--TPRIQTPAGTITLYKSKKFSWNFYSTPQKSLGGRQIHV 81
Cdd:PRK02106 3 TMEYDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGPDYrwDFFIQMPAALAFPLQGKRYNWAYETEPEPHMNNRRMEC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 82 PRGKALGGSSSMNSMIYIRGLPSDYDRWEQQ-GCEGWGWNNVLPWFKRSEKNLLSQDPaYHGFNGELLVDKPRDP-NPVS 159
Cdd:PRK02106 83 PRGKVLGGSSSINGMVYIRGNAMDYDNWAELpGLEGWSYADCLPYFKKAETRDGGEDD-YRGGDGPLSVTRGKPGtNPLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 160 ALFVAAGKRVGLAENTDFNGKSLAGVGIYNVTQKDGKRLSSYRAFLHPHIGRSNLTVMTDCTVQTLIIEDKAVKGVRITE 239
Cdd:PRK02106 162 QAFVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPALKRPNLTIVTHALTDRILFEGKRAVGVEYER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 240 HGrdQPTSILCRHEVILSAGSIGSPHILLKSGIGPAAELEAAGIPLVHPLPGVGKNLQDHLDGLVTVRSRNPLTLGFSLA 319
Cdd:PRK02106 242 GG--GRETARARREVILSAGAINSPQLLQLSGIGPAEHLKELGIPVVHDLPGVGENLQDHLEVYIQYECKQPVSLYPALK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 320 AW-KPILTSpfQYLFRRNGWLTTNYVEAGGFAATKLSSDEPDIQFHFVPGYRSHRGRLFEWGHGYAIHTCVLRPRSIGAL 398
Cdd:PRK02106 320 WWnKPKIGA--EWLFTGTGLGASNHFEAGGFIRSRAGVDWPNIQYHFLPVAIRYDGSNAVKGHGFQAHVGPMRSPSRGSV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 399 QLK-RDGQIA--IDFNFLADPYDASVLVEGIKVARNILAQPEFNALHGEEMLPGKHIQTDEQLHQYVKEYCATVFHPVGT 475
Cdd:PRK02106 398 KLKsADPRAHpsILFNYMSTEQDWREFRDAIRLTREIMAQPALDPYRGREISPGADVQTDEEIDAFVREHAETAYHPSCT 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2276004607 476 CKMGRDEMSVVAPDTlKVYGVENLRVADASIMPTLISGNTNAPSIMIGERAASMILQGTPVA 537
Cdd:PRK02106 478 CKMGTDPMAVVDPEG-RVHGVEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIRGRTPLA 538
|
|
| betA |
TIGR01810 |
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied ... |
8-536 |
7.04e-158 |
|
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. This enzymatic system can be found in both gram-positive and gram-negative bacteria. As in Escherichia coli, Staphylococcus xylosus, and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 273814 [Multi-domain] Cd Length: 532 Bit Score: 461.27 E-value: 7.04e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 8 DYIIIGGGSAGSVLAARLAEQADLKICLIEAGSRD--ETPRIQTPAGTITLYKSKKFSWNFYSTPQKSLGGRQIHVPRGK 85
Cdd:TIGR01810 1 DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGSDypWDLLIQMPAALAYPAGNKRYNWIYETEPEPHMNNRRVGHARGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 86 ALGGSSSMNSMIYIRGLPSDYDRWEQQ-GCEGWGWNNVLPWFKRSEKNLLSQDPaYHGFNGELLVDKPRDPNPVSALFVA 164
Cdd:TIGR01810 81 VLGGSSSINGMIYQRGNPMDYEKWAKPeGMESWDYADCLPYYKRLETTFGGEKP-YRGHDGPIKVRRGPADNPLFQAFIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 165 AGKRVGLAENTDFNGKSLAGVGIYNVTQKDGKRLSSYRAFLHPHIGRSNLTVMTDCTVQTLIIEDKAVKGVRITEHGRdq 244
Cdd:TIGR01810 160 AGVEAGYNKTPDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAMKRPNLEVQTRAFVTKINFEGNRATGVEFKKGGR-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 245 PTSILCRHEVILSAGSIGSPHILLKSGIGPAAELEAAGIPLVHPLPGVGKNLQDHLDGLVTVRSRNPLtlgfSLAAWKPI 324
Cdd:TIGR01810 238 KEHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRIHLPGVGENLQDHLEVYVQHACKQPV----SLYPSLNW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 325 LTSPF---QYLFRRNGWLTTNYVEAGGFAATKLSSDEPDIQFHFVPGYRSHRGRLFEWGHGYAIHTCVLRPRSIGALQLK 401
Cdd:TIGR01810 314 LKQPFigaQWLFGRKGAGASNHFEGGGFVRSNDDVDYPNIQYHFLPVAIRYDGTKAPKAHGFQVHVGPMYSNSRGHVKIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 402 -RD--GQIAIDFNFLADPYDASVLVEGIKVARNILAQPEFNALHGEEMLPGKHIQTDEQLHQYVKEYCATVFHPVGTCKM 478
Cdd:TIGR01810 394 sKDpfEKPEIVFNYMSHEEDWREFREAIRVTREILKQKALDPYRGGEISPGPEVQTDEEIDEFVRRHGETALHPCGTCKM 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 479 G--RDEMSVVAPDTlKVYGVENLRVADASIMPTLISGNTNAPSIMIGERAASMILQGTPV 536
Cdd:TIGR01810 474 GpaSDEMSVVDPET-RVHGMEGLRVVDASIMPRITNGNLNAPVIMMGEKAADIIRGKKPL 532
|
|
| GMC_oxred_N |
pfam00732 |
GMC oxidoreductase; This family of proteins bind FAD as a cofactor. |
73-301 |
1.99e-49 |
|
GMC oxidoreductase; This family of proteins bind FAD as a cofactor.
Pssm-ID: 366272 [Multi-domain] Cd Length: 218 Bit Score: 169.77 E-value: 1.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 73 SLGGRQIHVPRGKALGGSSSMNSMIYIRGLPSDYDRWEQQ-GCEGWGWNNVLPWFKRSEknllsqdpayhgfnGELLV-D 150
Cdd:pfam00732 13 SVNGRRMILPAGSTVGGGSSVNWSACIRTPAAVLDEWASEfGLEGWGYDDYLPYMDKVE--------------GPLGVtT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 151 KPRDPNPVSALFVAAGKRVGLAENT---DFNGKSLAGVGIYNvtQKDGKRLSSYRAFLHPHIGRsNLTVMTDCTVQTLII 227
Cdd:pfam00732 79 KGIEESPLNQALLKAAEELGYPVEAvprNSNGCHYCGFCGLG--CPTGAKQSTARTWLRPALER-NLRILTGAKAEKIII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276004607 228 E---DKAVkGVRITEHGRDQPTSILCRHEVILSAGSIGSPHILLKSGIGPAAeleaagiplvHPlpgVGKNLQDHLD 301
Cdd:pfam00732 156 LgrgGRAV-GVEARDGGGGIKRLITAAKEVVVAAGALNTPPLLLRSGLGKNP----------HP---VGKNLQLHPV 218
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
3-537 |
0e+00 |
|
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441878 [Multi-domain] Cd Length: 531 Bit Score: 703.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 3 NSKTYDYIIIGGGSAGSVLAARLAEQADLKICLIEAGSRDETPRIQTPAGTITLYKSKKFSWNFYSTPQKSLGGRQIHVP 82
Cdd:COG2303 1 MLEEYDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRDDDPLIRMPAGYAKLLGNPRYDWRYETEPQPGLNGRRLYWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 83 RGKALGGSSSMNSMIYIRGLPSDYDRWEQQGCEGWGWNNVLPWFKRSEKNLLSQDpAYHGFNGELLVDKPRDPNPVSALF 162
Cdd:COG2303 81 RGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGAD-AYHGRSGPLPVSDPPLPNPLSDAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 163 VAAGKRVGLAENTDFNGKSLAGVGIYNVTQKDGKRLSSYRAFLHPHIGRSNLTVMTDCTVQTLIIEDKAVKGVRITEHGR 242
Cdd:COG2303 160 IEAAEELGIPRADDFNGGACEGCGFCQVTCRNGARWSAARAYLPPALKRPNLTVRTGALVTRILFDGGRATGVEYRDDGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 243 DQptSILCRHEVILSAGSIGSPHILLKSGIGPAAELEAAGIPLVHPLPGVGKNLQDHLDGLVTVRSRNPLTLGFSLAAWK 322
Cdd:COG2303 240 EH--TVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLPGVGRNLQDHLEVSVVFRFKEPVTLNKSLRKAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 323 PILtspfQYLFRRNGWLTTNYVEAGGFAATKLSSDEPDIQFHFVP-GYRSHRGRL-FEWGHGYAIHTCVLRPRSIGALQL 400
Cdd:COG2303 318 IGL----QYLLTRSGPLTSNVAEAGGFFRSDPGLERPDLQFHFLPlGLTPRWGKKaLHDGHGFTAHVEQLRPESRGRVTL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 401 K-RD--GQIAIDFNFLADPYDASVLVEGIKVARNILAQPEFNALHGEEMLPGKHIQTDEQLhQYVKEYCATVFHPVGTCK 477
Cdd:COG2303 394 DsADplGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPYRGEEILPGPDVQSDEEL-AFIRARAYTIYHPVGTCR 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 478 MGRDEMSVVAPDtLKVYGVENLRVADASIMPTLISGNTNAPSIMIGERAASMILQGTPVA 537
Cdd:COG2303 473 MGTDPDSVVDPR-LRVHGVENLRVVDASVMPTITSGNTNAPTIMLAEKAADMILGDYLKN 531
|
|
| PRK02106 |
PRK02106 |
choline dehydrogenase; Validated |
4-537 |
0e+00 |
|
choline dehydrogenase; Validated
Pssm-ID: 235000 [Multi-domain] Cd Length: 560 Bit Score: 572.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 4 SKTYDYIIIGGGSAGSVLAARLAEQADLKICLIEAGSRDE--TPRIQTPAGTITLYKSKKFSWNFYSTPQKSLGGRQIHV 81
Cdd:PRK02106 3 TMEYDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGPDYrwDFFIQMPAALAFPLQGKRYNWAYETEPEPHMNNRRMEC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 82 PRGKALGGSSSMNSMIYIRGLPSDYDRWEQQ-GCEGWGWNNVLPWFKRSEKNLLSQDPaYHGFNGELLVDKPRDP-NPVS 159
Cdd:PRK02106 83 PRGKVLGGSSSINGMVYIRGNAMDYDNWAELpGLEGWSYADCLPYFKKAETRDGGEDD-YRGGDGPLSVTRGKPGtNPLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 160 ALFVAAGKRVGLAENTDFNGKSLAGVGIYNVTQKDGKRLSSYRAFLHPHIGRSNLTVMTDCTVQTLIIEDKAVKGVRITE 239
Cdd:PRK02106 162 QAFVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPALKRPNLTIVTHALTDRILFEGKRAVGVEYER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 240 HGrdQPTSILCRHEVILSAGSIGSPHILLKSGIGPAAELEAAGIPLVHPLPGVGKNLQDHLDGLVTVRSRNPLTLGFSLA 319
Cdd:PRK02106 242 GG--GRETARARREVILSAGAINSPQLLQLSGIGPAEHLKELGIPVVHDLPGVGENLQDHLEVYIQYECKQPVSLYPALK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 320 AW-KPILTSpfQYLFRRNGWLTTNYVEAGGFAATKLSSDEPDIQFHFVPGYRSHRGRLFEWGHGYAIHTCVLRPRSIGAL 398
Cdd:PRK02106 320 WWnKPKIGA--EWLFTGTGLGASNHFEAGGFIRSRAGVDWPNIQYHFLPVAIRYDGSNAVKGHGFQAHVGPMRSPSRGSV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 399 QLK-RDGQIA--IDFNFLADPYDASVLVEGIKVARNILAQPEFNALHGEEMLPGKHIQTDEQLHQYVKEYCATVFHPVGT 475
Cdd:PRK02106 398 KLKsADPRAHpsILFNYMSTEQDWREFRDAIRLTREIMAQPALDPYRGREISPGADVQTDEEIDAFVREHAETAYHPSCT 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2276004607 476 CKMGRDEMSVVAPDTlKVYGVENLRVADASIMPTLISGNTNAPSIMIGERAASMILQGTPVA 537
Cdd:PRK02106 478 CKMGTDPMAVVDPEG-RVHGVEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIRGRTPLA 538
|
|
| betA |
TIGR01810 |
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied ... |
8-536 |
7.04e-158 |
|
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. This enzymatic system can be found in both gram-positive and gram-negative bacteria. As in Escherichia coli, Staphylococcus xylosus, and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 273814 [Multi-domain] Cd Length: 532 Bit Score: 461.27 E-value: 7.04e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 8 DYIIIGGGSAGSVLAARLAEQADLKICLIEAGSRD--ETPRIQTPAGTITLYKSKKFSWNFYSTPQKSLGGRQIHVPRGK 85
Cdd:TIGR01810 1 DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGSDypWDLLIQMPAALAYPAGNKRYNWIYETEPEPHMNNRRVGHARGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 86 ALGGSSSMNSMIYIRGLPSDYDRWEQQ-GCEGWGWNNVLPWFKRSEKNLLSQDPaYHGFNGELLVDKPRDPNPVSALFVA 164
Cdd:TIGR01810 81 VLGGSSSINGMIYQRGNPMDYEKWAKPeGMESWDYADCLPYYKRLETTFGGEKP-YRGHDGPIKVRRGPADNPLFQAFIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 165 AGKRVGLAENTDFNGKSLAGVGIYNVTQKDGKRLSSYRAFLHPHIGRSNLTVMTDCTVQTLIIEDKAVKGVRITEHGRdq 244
Cdd:TIGR01810 160 AGVEAGYNKTPDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAMKRPNLEVQTRAFVTKINFEGNRATGVEFKKGGR-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 245 PTSILCRHEVILSAGSIGSPHILLKSGIGPAAELEAAGIPLVHPLPGVGKNLQDHLDGLVTVRSRNPLtlgfSLAAWKPI 324
Cdd:TIGR01810 238 KEHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRIHLPGVGENLQDHLEVYVQHACKQPV----SLYPSLNW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 325 LTSPF---QYLFRRNGWLTTNYVEAGGFAATKLSSDEPDIQFHFVPGYRSHRGRLFEWGHGYAIHTCVLRPRSIGALQLK 401
Cdd:TIGR01810 314 LKQPFigaQWLFGRKGAGASNHFEGGGFVRSNDDVDYPNIQYHFLPVAIRYDGTKAPKAHGFQVHVGPMYSNSRGHVKIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 402 -RD--GQIAIDFNFLADPYDASVLVEGIKVARNILAQPEFNALHGEEMLPGKHIQTDEQLHQYVKEYCATVFHPVGTCKM 478
Cdd:TIGR01810 394 sKDpfEKPEIVFNYMSHEEDWREFREAIRVTREILKQKALDPYRGGEISPGPEVQTDEEIDEFVRRHGETALHPCGTCKM 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 479 G--RDEMSVVAPDTlKVYGVENLRVADASIMPTLISGNTNAPSIMIGERAASMILQGTPV 536
Cdd:TIGR01810 474 GpaSDEMSVVDPET-RVHGMEGLRVVDASIMPRITNGNLNAPVIMMGEKAADIIRGKKPL 532
|
|
| Rv0697 |
TIGR03970 |
dehydrogenase, Rv0697 family; This model describes a set of dehydrogenases belonging to the ... |
8-531 |
4.72e-76 |
|
dehydrogenase, Rv0697 family; This model describes a set of dehydrogenases belonging to the glucose-methanol-choline oxidoreductase (GMC oxidoreductase) family. Members of the present family are restricted to Actinobacterial genome contexts containing also members of families TIGR03962 and TIGR03969 (the mycofactocin system), and are proposed to be uniform in function.
Pssm-ID: 274888 [Multi-domain] Cd Length: 487 Bit Score: 248.58 E-value: 4.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 8 DYIIIGGGSAGSVLAARLAEQADLKICLIEAGS--RD--ETPRIQTPAGTITLYKSKKFSWNfYSTPQKSLGGRQIHVPR 83
Cdd:TIGR03970 2 DVLIVGAGSAGSVLAARLSEDPSCTVTVLEAGPgyRDpsRLPAQLTDGLRLPIGPASPVVWR-YGVELTDGPRRASQIVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 84 GKALGGSSSMNSMIYIRGLPSDYDRWeqqGCEGWGWNNVLPWFKRSEKNLLSQDPaYHGFNGELLVDKPRDPNPVSALFV 163
Cdd:TIGR03970 81 GRVLGGSGAVNGGYFCRALPADFDAW---PIPGWSWDDVLPHFRAIETDLDFDGP-LHGTAGPIPVRRTAELDGISAAFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 164 AAGKRVGLAENTDFNGKS---LAGVGIYNVTQKDGKRLSSYRAFLHPHIGRSNLTVMTDCTVQTLIIEDKAVKGVritEH 240
Cdd:TIGR03970 157 AAALGAGFGWIADLNGSGpglPGGVGAVPLNVDGGRRVSTAVAYLLPALKRPNLTVEADTRVVRILFSGTRAVGV---EV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 241 GRDQPTSILCRHEVILSAGSIGSPHILLKSGIGPAAELEAAGIPLVHPLPgVGKNLQDHLDGLVTVRSRNPLTLgfslaa 320
Cdd:TIGR03970 234 LGDGGPRTLRADRVVLCAGAVESAHLLLLSGIGPAEQLRAAGIAVVLDLP-VGSDFVDHPEWVLPYRWRPTHDR------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 321 wkPILTSPFQYLfrrngwLTTNYVE----AGGFAAtklssdepdiqfhFVPGyrSHRgrlfEWGHgyaIHTCVLRPRSIG 396
Cdd:TIGR03970 307 --PPTSPVLETV------LNTADIEirpyTAGFTA-------------LVPG--SPR----DDPH---LGVALMRPHSRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 397 ALQL---KRDGQIAIDFNFLADPYDASVLVEGIKVARNILAQPEFNALhgeeMLPGKHIQTDEqlhqYVKEYCATVFHPV 473
Cdd:TIGR03970 357 RIRLasaDPADPPRIEHRYDSSAADRAALRAGAALAHELLGSPELGPL----LEPAVREGEAS----WVLARLATSQHLC 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2276004607 474 GTCKMG-RDEMSVVAPDTLKVYGVENLRVADASIMPTLISGNTNAPSIMIGERAASMIL 531
Cdd:TIGR03970 429 GSCRMGgRDDPGAVVDARCRVRGVEGLWVVDGSILPVIPSRGPHATAVMVAERAAEFLG 487
|
|
| GMC_oxred_N |
pfam00732 |
GMC oxidoreductase; This family of proteins bind FAD as a cofactor. |
73-301 |
1.99e-49 |
|
GMC oxidoreductase; This family of proteins bind FAD as a cofactor.
Pssm-ID: 366272 [Multi-domain] Cd Length: 218 Bit Score: 169.77 E-value: 1.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 73 SLGGRQIHVPRGKALGGSSSMNSMIYIRGLPSDYDRWEQQ-GCEGWGWNNVLPWFKRSEknllsqdpayhgfnGELLV-D 150
Cdd:pfam00732 13 SVNGRRMILPAGSTVGGGSSVNWSACIRTPAAVLDEWASEfGLEGWGYDDYLPYMDKVE--------------GPLGVtT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 151 KPRDPNPVSALFVAAGKRVGLAENT---DFNGKSLAGVGIYNvtQKDGKRLSSYRAFLHPHIGRsNLTVMTDCTVQTLII 227
Cdd:pfam00732 79 KGIEESPLNQALLKAAEELGYPVEAvprNSNGCHYCGFCGLG--CPTGAKQSTARTWLRPALER-NLRILTGAKAEKIII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276004607 228 E---DKAVkGVRITEHGRDQPTSILCRHEVILSAGSIGSPHILLKSGIGPAAeleaagiplvHPlpgVGKNLQDHLD 301
Cdd:pfam00732 156 LgrgGRAV-GVEARDGGGGIKRLITAAKEVVVAAGALNTPPLLLRSGLGKNP----------HP---VGKNLQLHPV 218
|
|
| GMC_oxred_C |
pfam05199 |
GMC oxidoreductase; This domain found associated with pfam00732. |
392-526 |
7.50e-42 |
|
GMC oxidoreductase; This domain found associated with pfam00732.
Pssm-ID: 398739 [Multi-domain] Cd Length: 143 Bit Score: 147.16 E-value: 7.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 392 PRSIGALQLKR---DGQIAIDFNFLADPYDASVLVEGIKVARNILAQPEFNALHG-----EEMLPGKHIQTDEQLHQYVK 463
Cdd:pfam05199 1 PRSRGRVTLSSsdpTGLPVIDPNYLSDPADLAALRAALRLARRILAAAGLVLGVEltpgpVPEVSDAAVTSDDELLAYIR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2276004607 464 EYCATVFHPVGTCKMGRDEM-SVVAPDtLKVYGVENLRVADASIMPTLISGNTNAPSIMIGERA 526
Cdd:pfam05199 81 AAASTSYHPMGTCRMGADPDdAVVDPD-LRVHGVDNLRVVDASVFPSSPSGNPTLTIYALAERA 143
|
|
| PLN02785 |
PLN02785 |
Protein HOTHEAD |
6-533 |
6.43e-28 |
|
Protein HOTHEAD
Pssm-ID: 215420 [Multi-domain] Cd Length: 587 Bit Score: 117.98 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 6 TYDYIIIGGGSAGSVLAARLAEQadLKICLIEAGSrdetpriqTPAGTITLykskKFSWNFY---------STPQKSLGG 76
Cdd:PLN02785 55 AYDYIVVGGGTAGCPLAATLSQN--FSVLLLERGG--------VPFGNANV----SFLENFHigladtsptSASQAFIST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 77 RQIHVPRGKALGGSSSMNSMIYIRGLPSDYDRWeqqgcegwGW-----NNVLPWFKRSeknllsqdpayhgfngelLVDK 151
Cdd:PLN02785 121 DGVINARARVLGGGTCINAGFYSRASTRFIQKA--------GWdaklvNESYPWVERQ------------------IVHW 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 152 PRdpnpvSALFVAAgKRVGLAEN--TDFNGKS---LAG--VG--IYNVTqkdGKRLSSYR--AFLHPHigrsNLTVMTDC 220
Cdd:PLN02785 175 PK-----VAPWQAA-LRDSLLEVgvSPFNGFTydhVYGtkVGgtIFDEF---GRRHTAAEllAAGNPN----KLRVLLHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 221 TVQTLIIEDKAVK----GVRITEHGRDQPTSIL---CRHEVILSAGSIGSPHILLKSGIGPAAELEAAGIPLVHPLPGVG 293
Cdd:PLN02785 242 TVQKIVFDTSGKRpratGVIFKDENGNQHQAFLsnnKGSEIILSAGAIGSPQMLLLSGIGPKKELKKHKIPVVLHNEHVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 294 KNLQDHLDGLVTVRSRNPltlgfslaawkpiltsPFQYLFRRNGwLTTN--YVEAG-GFAATKLSsdepdIQFH------ 364
Cdd:PLN02785 322 KGMADNPMNSIFVPSKAP----------------VEQSLIQTVG-ITKMgvYIEASsGFGQSPDS-----IHCHhgimsa 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 365 -------FVPGYRS--------HRGR--LFEWGHGYAIHTCVLRPRSIGALQL---KRDGQIAIDFNFLADPYDASVLVE 424
Cdd:PLN02785 380 eigqlstIPPKQRTpeaiqayiHRKKnlPHEAFNGGFILEKIAGPISTGHLSLintNVDDNPSVTFNYFKHPQDLQRCVY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2276004607 425 GIKVARNILAQPEFNAL---HGEEM-------------LPGKHIQTDEQLHQYVKEYCATVFHPVGTCKMGRdemsVVAP 488
Cdd:PLN02785 460 GIRTIEKIVKTNHFTNFtqcDKQTMekvlnmsvkaninLIPKHTNDTKSLEQFCKDTVITIWHYHGGCHVGK----VVDQ 535
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2276004607 489 DTlKVYGVENLRVADASIMPTLISGNTNAPSIMIGERAASMILQG 533
Cdd:PLN02785 536 NY-KVLGVSRLRVIDGSTFDESPGTNPQATVMMMGRYMGVKILRE 579
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
4-39 |
3.08e-06 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 49.70 E-value: 3.08e-06
10 20 30
....*....|....*....|....*....|....*.
gi 2276004607 4 SKTYDYIIIGGGSAGSVLAARLAeQADLKICLIEAG 39
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAA-QLGLKVALVEKG 35
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
3-41 |
7.55e-06 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 48.22 E-value: 7.55e-06
10 20 30
....*....|....*....|....*....|....*....
gi 2276004607 3 NSKTYDYIIIGGGSAGSVLAARLAEQADLKICLIEAGSR 41
Cdd:COG0579 1 MMEMYDVVIIGAGIVGLALARELSRYEDLKVLVLEKEDD 39
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
4-37 |
9.98e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 44.81 E-value: 9.98e-05
10 20 30
....*....|....*....|....*....|....
gi 2276004607 4 SKTYDYIIIGGGSAGSVLAARLAEqADLKICLIE 37
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAG-LGMKVALIE 35
|
|
| Lycopene_cycl |
pfam05834 |
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. ... |
8-39 |
2.56e-04 |
|
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. Carotenoids with cyclic end groups are essential components of the photosynthetic membranes in all plants, algae, and cyanobacteria. These lipid-soluble compounds protect against photo-oxidation, harvest light for photosynthesis, and dissipate excess light energy absorbed by the antenna pigments. The cyclization of lycopene (psi, psi-carotene) is a key branch point in the pathway of carotenoid biosynthesis. Two types of cyclic end groups are found in higher plant carotenoids: the beta and epsilon rings. Carotenoids with two beta rings are ubiquitous, and those with one beta and one epsilon ring are common; however, carotenoids with two epsilon rings are rare.
Pssm-ID: 310433 [Multi-domain] Cd Length: 380 Bit Score: 43.56 E-value: 2.56e-04
10 20 30
....*....|....*....|....*....|...
gi 2276004607 8 DYIIIGGGSAGSVLAARLAEQA-DLKICLIEAG 39
Cdd:pfam05834 1 DVVIIGAGPAGLSLAARLAAAKpGLSVVLIEPG 33
|
|
| PRK07364 |
PRK07364 |
FAD-dependent hydroxylase; |
4-43 |
4.32e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236001 [Multi-domain] Cd Length: 415 Bit Score: 42.70 E-value: 4.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2276004607 4 SKTYDYIIIGGGSAGSVLAARLAEQAdLKICLIEAGSRDE 43
Cdd:PRK07364 16 SLTYDVAIVGGGIVGLTLAAALKDSG-LRIALIEAQPAEA 54
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
5-39 |
5.17e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 42.47 E-value: 5.17e-04
10 20 30
....*....|....*....|....*....|....*
gi 2276004607 5 KTYDYIIIGGGSAGSVlAARLAEQADLKICLIEAG 39
Cdd:PRK06292 2 EKYDVIVIGAGPAGYV-AARRAAKLGKKVALIEKG 35
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
5-39 |
5.71e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 42.20 E-value: 5.71e-04
10 20 30
....*....|....*....|....*....|....*
gi 2276004607 5 KTYDYIIIGGGSAGSVLAARLAEqADLKICLIEAG 39
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLAR-RGLDVTVLERG 34
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
7-85 |
4.06e-03 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 39.22 E-value: 4.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2276004607 7 YDYIIIGGGSAGSVLAARLAeQADLKICLIEagsRDETPRIQTPAGTITLYKSKKFSWNFYSTPQKSLGGRqIHVPRGK 85
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLA-DKGLRVLLLE---KKSFPRYKPCGGALSPRALEELDLPGELIVNLVRGAR-FFSPNGD 74
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
7-39 |
4.33e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 39.22 E-value: 4.33e-03
10 20 30
....*....|....*....|....*....|...
gi 2276004607 7 YDYIIIGGGSAGSVLAARLAeQADLKICLIEAG 39
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLA-QLGGKVTLIEDE 32
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
4-51 |
4.36e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 39.54 E-value: 4.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2276004607 4 SKTYDYIIIGGGSAGSVLAARLAeQADLKICLIEAGSRDetpRIQTPA 51
Cdd:PRK09126 1 MMHSDIVVVGAGPAGLSFARSLA-GSGLKVTLIERQPLA---ALADPA 44
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
3-57 |
5.70e-03 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 39.17 E-value: 5.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2276004607 3 NSKTYDYIIIGGGSAGSVLAARLAEQAD--LKICLIEA----------GSRDETPRIQTPAGTITLY 57
Cdd:COG4529 2 TGARKRIAIIGGGASGTALAIHLLRRAPepLRITLFEPrpelgrgvaySTDSPEHLLNVPAGRMSAF 68
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
11-41 |
6.94e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 35.20 E-value: 6.94e-03
10 20 30
....*....|....*....|....*....|.
gi 2276004607 11 IIGGGSAGSVLAARLAEQaDLKICLIEAGSR 41
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKR-GFRVLVLEKRDR 30
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
10-41 |
7.43e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 38.73 E-value: 7.43e-03
10 20 30
....*....|....*....|....*....|..
gi 2276004607 10 IIIGGGSAGsVLAARLAEQADLKICLIEAGSR 41
Cdd:TIGR00275 1 IIIGGGAAG-LMAAITAARAGLSVLLLEKNKK 31
|
|
| PRK07608 |
PRK07608 |
UbiH/UbiF family hydroxylase; |
2-39 |
7.44e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181057 [Multi-domain] Cd Length: 388 Bit Score: 38.78 E-value: 7.44e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2276004607 2 NNSKTYDYIIIGGGSAGSVLAARLAeQADLKICLIEAG 39
Cdd:PRK07608 1 AYHMKFDVVVVGGGLVGASLALALA-QSGLRVALLAPR 37
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
4-39 |
8.64e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 38.59 E-value: 8.64e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2276004607 4 SKTYDYIIIGGGSAGSVLAARLAeQADLKICLIEAG 39
Cdd:PRK06416 2 AFEYDVIVIGAGPGGYVAAIRAA-QLGLKVAIVEKE 36
|
|
|