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Conserved domains on  [gi|2276004607|dbj|GKJ16073|]
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alcohol dehydrogenase [Klebsiella variicola]

Protein Classification

GMC family oxidoreductase( domain architecture ID 11455227)

GMC (glucose-methanol-choline) family oxidoreductase is a flavoprotein that catalyzes the oxidation of an alcohol moiety to the corresponding aldehyde with the concomitant reduction of flavin adenine dinucleotide (FAD)

EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050660
PubMed:  23578136|1542121
SCOP:  3000055

Graphical summary

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List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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