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Conserved domains on  [gi|499211464|ref|WP_010909004|]
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FAD-binding oxidoreductase [Mycobacterium leprae]

Protein Classification

FAD-binding oxidoreductase( domain architecture ID 11416043)

FAD-binding oxidoreductase catalyzes the oxidation or reduction of a specific substrate using flavin adenine dinucleotide (FAD) as a cofactor

CATH:  3.30.465.50|3.40.462.20
EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
1-449 2.89e-122

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


:

Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 363.83  E-value: 2.89e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464   1 MLRSLAAVVGSsHVIADPDVLIAHSIDHTGRYRGQARALVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSLVAGTVPEHN 80
Cdd:COG0277    6 LLAALRAILAG-RVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  81 DVLLSTERLRSISEVDTVERRLRVGAGATLTAVQNAATAAGLVFGVDLCARATATVGGMASTNAGGLRTVRYGNMGEQVI 160
Cdd:COG0277   85 GVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 161 GLEVALPDGSLLCRHSLARFDNTGYNLPALFVGAEGTLGVITALDLRLHPAPAHRVTAVCGFSDLGALVDA-SRAFRDVY 239
Cdd:COG0277  165 GLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAvRALLAAGI 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 240 GIAALELIDGRASSLIREHLGVSSPVDGDWLLLVELAADHDQT--NRLAELSMAVQMCGVPAVGV--DAGAQQRLWRVRE 315
Cdd:COG0277  245 APAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDDAEEveAQLARLRAILEAGGATDVRVaaDGAERERLWKARK 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 316 SLAEVLGVYGPPLKF--DVSLPLSAISGFAKEAATLIDAqvsdvQEALPVLFGHVGEGNLHLNVLRCPPD-----REKTL 388
Cdd:COG0277  325 AALPALGRLDGGAKLleDVAVPPSRLPELLRELGALAAK-----YGLRATAFGHAGDGNLHVRILFDPADpeeveRARAA 399

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499211464 389 TAAMMELIAQAGGNVSSEHGVGSNKRAYLRMSRDPADIAAMRTIKAALDPTGYLNAAVLFD 449
Cdd:COG0277  400 AEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
1-449 2.89e-122

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 363.83  E-value: 2.89e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464   1 MLRSLAAVVGSsHVIADPDVLIAHSIDHTGRYRGQARALVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSLVAGTVPEHN 80
Cdd:COG0277    6 LLAALRAILAG-RVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  81 DVLLSTERLRSISEVDTVERRLRVGAGATLTAVQNAATAAGLVFGVDLCARATATVGGMASTNAGGLRTVRYGNMGEQVI 160
Cdd:COG0277   85 GVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 161 GLEVALPDGSLLCRHSLARFDNTGYNLPALFVGAEGTLGVITALDLRLHPAPAHRVTAVCGFSDLGALVDA-SRAFRDVY 239
Cdd:COG0277  165 GLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAvRALLAAGI 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 240 GIAALELIDGRASSLIREHLGVSSPVDGDWLLLVELAADHDQT--NRLAELSMAVQMCGVPAVGV--DAGAQQRLWRVRE 315
Cdd:COG0277  245 APAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDDAEEveAQLARLRAILEAGGATDVRVaaDGAERERLWKARK 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 316 SLAEVLGVYGPPLKF--DVSLPLSAISGFAKEAATLIDAqvsdvQEALPVLFGHVGEGNLHLNVLRCPPD-----REKTL 388
Cdd:COG0277  325 AALPALGRLDGGAKLleDVAVPPSRLPELLRELGALAAK-----YGLRATAFGHAGDGNLHVRILFDPADpeeveRARAA 399

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499211464 389 TAAMMELIAQAGGNVSSEHGVGSNKRAYLRMSRDPADIAAMRTIKAALDPTGYLNAAVLFD 449
Cdd:COG0277  400 AEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
 212-443 1.49e-58

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 192.53  E-value: 1.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  212 PAHRVTAVCGFSDLGALVDASRAFRDV-YGIAALELIDGRASSLIREHLGVSS--PVDGDWLLLVELAADHDQTNRlAEL 288
Cdd:pfam02913   2 PEVRAVALVGFPSFEAAVKAVREIARAgIIPAALELMDNDALDLVEATLGFPKglPRDAAALLLVEFEGDDEETAE-EEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  289 SMAVQMCGVPAVGV-----DAGAQQRLWRVRESLAE----VLGVYGPPLKFDVSLPLSAISGFAKEAATLIDAQVSDVqe 359
Cdd:pfam02913  81 EAVEAILEAGGAGDvvvatDEAEAERLWAARKYALPlrdaLGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVV-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  360 alpVLFGHVGEGNLHLNVL-----RCPPDREKTLTAAMMELIAQAGGNVSSEHGVGSNKRAYLRMSRDPADIAAMRTIKA 434
Cdd:pfam02913 159 ---CLFGHAGDGNLHLYILfdfrdPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKA 235


                  ....*....
gi 499211464  435 ALDPTGYLN 443
Cdd:pfam02913 236 AFDPKGILN 244
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
 39-447 3.10e-42

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 157.09  E-value: 3.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  39 LVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSLVAGTVPEHNDVLLSTERLRSISEVDTVERRLRVGAGATLTAVQNAAT 118
Cdd:PLN02805 137 VVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLE 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 119 AAGLVFGVDlcARATATVGGMASTNAGGLRTVRYGNMGEQVIGLEVALPDGSLLCRHSLARFDNTGYNLPALFVGAEGTL 198
Cdd:PLN02805 217 PYGLFFPLD--PGPGATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEGTL 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 199 GVITALDLRLHPAPAHRVTAVCGFSDLGALVDASRA------------FRDVYGIAALELIDGR----ASSLIREHLGVS 262
Cdd:PLN02805 295 GVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIAtmlsgiqvsrveLLDEVQIRAINMANGKnlpeAPTLMFEFIGTE 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 263 SPVDGDWLLLVELAADHDQTNRL-AElsmavqmcgvpavgvDAGAQQRLWRVRESLAEVLGVYGPPLKF---DVSLPLSA 338
Cdd:PLN02805 375 AYAREQTLIVQKIASKHNGSDFVfAE---------------EPEAKKELWKIRKEALWACFAMEPKYEAmitDVCVPLSH 439

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 339 ISGFAKEAATLIDAqvsdvQEALPVLFGHVGEGNLHLNVLRCPPDRE-----KTLTAAMMELIAQAGGNVSSEHGVGSNK 413
Cdd:PLN02805 440 LAELISRSKKELDA-----SPLVCTVIAHAGDGNFHTIILFDPSQEDqrreaERLNHFMVHTALSMEGTCTGEHGVGTGK 514

                        410       420       430
                 ....*....|....*....|....*....|....
gi 499211464 414 RAYLRMSRDPADIAAMRTIKAALDPTGYLNAAVL 447
Cdd:PLN02805 515 MKYLEKELGIEALQTMKRIKKALDPNNIMNPGKL 548
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 36-217 7.27e-05

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 45.24  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464   36 ARALVRPGTAEQVTEVLRVCRDVGAHVTVqggrTSLVAGTVPE-------HNDVLLSTERLRSISEVDTVERRLRVGAGA 108
Cdd:TIGR01677  32 AANVAYPKTEAELVSVVAAATAAGRKMKV----VTRYSHSIPKlacpdgsDGALLISTKRLNHVVAVDATAMTVTVESGM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  109 TLTAVQNAATAAGLVFGvdlcaraTA------TVGGMASTNA-GGLRTVRYGNMGEQVIGLEVALP----DGSLLCRhSL 177
Cdd:TIGR01677 108 SLRELIVEAEKAGLALP-------YApywwglTVGGMMGTGAhGSSLWGKGSAVHDYVVGIRLVVPasaaEGFAKVR-IL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 499211464  178 ARFDNtgynlPALFVGAE---GTLGVITALDLRLHPAPAHRVT 217
Cdd:TIGR01677 180 SEGDT-----PNEFNAAKvslGVLGVISQVTLALQPMFKRSVT 217
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
1-449 2.89e-122

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 363.83  E-value: 2.89e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464   1 MLRSLAAVVGSsHVIADPDVLIAHSIDHTGRYRGQARALVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSLVAGTVPEHN 80
Cdd:COG0277    6 LLAALRAILAG-RVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVPLDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  81 DVLLSTERLRSISEVDTVERRLRVGAGATLTAVQNAATAAGLVFGVDLCARATATVGGMASTNAGGLRTVRYGNMGEQVI 160
Cdd:COG0277   85 GVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRDNVL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 161 GLEVALPDGSLLCRHSLARFDNTGYNLPALFVGAEGTLGVITALDLRLHPAPAHRVTAVCGFSDLGALVDA-SRAFRDVY 239
Cdd:COG0277  165 GLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAvRALLAAGI 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 240 GIAALELIDGRASSLIREHLGVSSPVDGDWLLLVELAADHDQT--NRLAELSMAVQMCGVPAVGV--DAGAQQRLWRVRE 315
Cdd:COG0277  245 APAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDDAEEveAQLARLRAILEAGGATDVRVaaDGAERERLWKARK 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 316 SLAEVLGVYGPPLKF--DVSLPLSAISGFAKEAATLIDAqvsdvQEALPVLFGHVGEGNLHLNVLRCPPD-----REKTL 388
Cdd:COG0277  325 AALPALGRLDGGAKLleDVAVPPSRLPELLRELGALAAK-----YGLRATAFGHAGDGNLHVRILFDPADpeeveRARAA 399

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499211464 389 TAAMMELIAQAGGNVSSEHGVGSNKRAYLRMSRDPADIAAMRTIKAALDPTGYLNAAVLFD 449
Cdd:COG0277  400 AEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
 212-443 1.49e-58

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 192.53  E-value: 1.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  212 PAHRVTAVCGFSDLGALVDASRAFRDV-YGIAALELIDGRASSLIREHLGVSS--PVDGDWLLLVELAADHDQTNRlAEL 288
Cdd:pfam02913   2 PEVRAVALVGFPSFEAAVKAVREIARAgIIPAALELMDNDALDLVEATLGFPKglPRDAAALLLVEFEGDDEETAE-EEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  289 SMAVQMCGVPAVGV-----DAGAQQRLWRVRESLAE----VLGVYGPPLKFDVSLPLSAISGFAKEAATLIDAQVSDVqe 359
Cdd:pfam02913  81 EAVEAILEAGGAGDvvvatDEAEAERLWAARKYALPlrdaLGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVV-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  360 alpVLFGHVGEGNLHLNVL-----RCPPDREKTLTAAMMELIAQAGGNVSSEHGVGSNKRAYLRMSRDPADIAAMRTIKA 434
Cdd:pfam02913 159 ---CLFGHAGDGNLHLYILfdfrdPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKA 235


                  ....*....
gi 499211464  435 ALDPTGYLN 443
Cdd:pfam02913 236 AFDPKGILN 244
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
 39-447 3.10e-42

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 157.09  E-value: 3.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  39 LVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSLVAGTVPEHNDVLLSTERLRSISEVDTVERRLRVGAGATLTAVQNAAT 118
Cdd:PLN02805 137 VVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLE 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 119 AAGLVFGVDlcARATATVGGMASTNAGGLRTVRYGNMGEQVIGLEVALPDGSLLCRHSLARFDNTGYNLPALFVGAEGTL 198
Cdd:PLN02805 217 PYGLFFPLD--PGPGATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEGTL 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 199 GVITALDLRLHPAPAHRVTAVCGFSDLGALVDASRA------------FRDVYGIAALELIDGR----ASSLIREHLGVS 262
Cdd:PLN02805 295 GVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIAtmlsgiqvsrveLLDEVQIRAINMANGKnlpeAPTLMFEFIGTE 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 263 SPVDGDWLLLVELAADHDQTNRL-AElsmavqmcgvpavgvDAGAQQRLWRVRESLAEVLGVYGPPLKF---DVSLPLSA 338
Cdd:PLN02805 375 AYAREQTLIVQKIASKHNGSDFVfAE---------------EPEAKKELWKIRKEALWACFAMEPKYEAmitDVCVPLSH 439

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 339 ISGFAKEAATLIDAqvsdvQEALPVLFGHVGEGNLHLNVLRCPPDRE-----KTLTAAMMELIAQAGGNVSSEHGVGSNK 413
Cdd:PLN02805 440 LAELISRSKKELDA-----SPLVCTVIAHAGDGNFHTIILFDPSQEDqrreaERLNHFMVHTALSMEGTCTGEHGVGTGK 514

                        410       420       430
                 ....*....|....*....|....*....|....
gi 499211464 414 RAYLRMSRDPADIAAMRTIKAALDPTGYLNAAVL 447
Cdd:PLN02805 515 MKYLEKELGIEALQTMKRIKKALDPNNIMNPGKL 548
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
 21-443 3.79e-38

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 144.92  E-value: 3.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  21 LIAHSIDHTGRYRGQARALVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSLVAGTVPEHNDVLLSTERLRSISEVDTVER 100
Cdd:PRK11230  41 LIPYECDGLSAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKGVLLVMARFNRILDINPVGR 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 101 RLRVGAGATLTAVQNAATAAGLVFGVDLCARATATVGGMASTNAGGLRTVRYGNMGEQVIGLEVALPDGSLLCRHSLArF 180
Cdd:PRK11230 121 RARVQPGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEALTLGSDA-L 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 181 DNTGYNLPALFVGAEGTLGVITALDLRLHPAPAHRVTAVCGFSDLGalvDASRAFRDVygIAA------LELIDGRASSL 254
Cdd:PRK11230 200 DSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVE---KAGLAVGDI--IAAgiipggLEMMDNLSIRA 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 255 IREHLGVSSPVDGDWLLLVEL---AAD-HDQTNRLAELSMAVQMCGVpAVGVDAGAQQRLWRVRESLAEVLGVYGPPLK- 329
Cdd:PRK11230 275 AEDFIHAGYPVDAEAILLCELdgvESDvQEDCERVNDILLKAGATDV-RLAQDEAERVRFWAGRKNAFPAVGRISPDYYc 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 330 FDVSLPLSAISGFAKEAATLIDaqvsdvQEALPV--LFgHVGEGNLHLNVL---RCPP--DREKTLTAAMMELIAQAGGN 402
Cdd:PRK11230 354 MDGTIPRRELPGVLEGIARLSQ------QYGLRVanVF-HAGDGNMHPLILfdaNEPGelERAEALGGKILELCVEVGGS 426

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 499211464 403 VSSEHGVGSNKRAYLRMSRDPADIAAMRTIKAALDPTGYLN 443
Cdd:PRK11230 427 ITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLLN 467
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 36-172 2.45e-33

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 122.31  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464   36 ARALVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSLVAGTVPEhNDVLLSTERLRSISEVDTVERRLRVGAGATLTAVQN 115
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQT-GGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499211464  116 AATAAGLVFGVDLCARATATVGGMASTNAGGLRTVRYGNMGEQVIGLEVALPDGSLL 172
Cdd:pfam01565  80 ALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVV 136
PRK11183 PRK11183
D-lactate dehydrogenase; Provisional
 2-116 2.24e-09

D-lactate dehydrogenase; Provisional


Pssm-ID: 236872 [Multi-domain]  Cd Length: 564  Bit Score: 59.47  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464   2 LRSLAAVVGSSHVIADPDvliahsidHTGRYR-------GQARALVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSLVAG 74
Cdd:PRK11183   6 INELTRIVGSSHVLTDPA--------KTERYRkgfrsgqGDALAVVFPGTLLELWRVLQACVAADKIIIMQAANTGLTGG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499211464  75 TVPEHND-----VLLSTERLRSISEVDTVERRLRVgAGATLTAVQNA 116
Cdd:PRK11183  78 STPNGNDydrdiVIISTLRLDKIQLLNNGKQVLAL-PGTTLYQLEKA 123
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
31-210 5.77e-09

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 57.19  E-value: 5.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  31 RYRGQARALVRPGTAEQVTEVLRVCRDVGAHVTVQGGRtslvAGTVPEHNDVLLSTERL-RSISEVDTVERRLRVGAGAT 109
Cdd:PRK14652  31 RVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGG----ANTLVADAGVRGVVLRLpQDFPGESTDGGRLVLGAGAP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464 110 LTAVQNAATAAGLVfGVDLCARATATVGGMASTNAGglrtVRYGNMGEQVIGLEVALPDGSLLCRHSLARFDNTGYNLPA 189
Cdd:PRK14652 107 ISRLPARAHAHGLV-GMEFLAGIPGTLGGAVAMNAG----TKLGEMKDVVTAVELATADGAGFVPAAALGYAYRTCRLPP 181

                        170       180
                 ....*....|....*....|.
gi 499211464 190 lfvgaegtLGVITALDLRLHP 210
Cdd:PRK14652 182 --------GAVITRVEVRLRP 194
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 36-217 7.27e-05

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 45.24  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464   36 ARALVRPGTAEQVTEVLRVCRDVGAHVTVqggrTSLVAGTVPE-------HNDVLLSTERLRSISEVDTVERRLRVGAGA 108
Cdd:TIGR01677  32 AANVAYPKTEAELVSVVAAATAAGRKMKV----VTRYSHSIPKlacpdgsDGALLISTKRLNHVVAVDATAMTVTVESGM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  109 TLTAVQNAATAAGLVFGvdlcaraTA------TVGGMASTNA-GGLRTVRYGNMGEQVIGLEVALP----DGSLLCRhSL 177
Cdd:TIGR01677 108 SLRELIVEAEKAGLALP-------YApywwglTVGGMMGTGAhGSSLWGKGSAVHDYVVGIRLVVPasaaEGFAKVR-IL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 499211464  178 ARFDNtgynlPALFVGAE---GTLGVITALDLRLHPAPAHRVT 217
Cdd:TIGR01677 180 SEGDT-----PNEFNAAKvslGVLGVISQVTLALQPMFKRSVT 217
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
 30-211 1.11e-04

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 44.50  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464   30 GRYRGQARALVRPGTAEQVTEVLRVCRDVGAHVTVQGG--RTSLVAGTvpehNDVLLSTERLRSISEVDTVERRLRVGAG 107
Cdd:TIGR01678   9 KTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGghSPSDIACT----DGFLIHLDKMNKVLQFDKEKKQITVEAG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  108 ATLTAVQNAATAAGLVFGvDLCARATATVGGMASTNAGGlRTVRYGNMGEQVIGLEVALPDGSLL-CRHSlarfdntgyN 186
Cdd:TIGR01678  85 IRLYQLHEQLDEHGYSMS-NLGSISEVSVAGIISTGTHG-SSIKHGILATQVVALTIMTADGEVLeCSEE---------R 153

                         170       180
                  ....*....|....*....|....*...
gi 499211464  187 LPALFVGAE---GTLGVITALDLRLHPA 211
Cdd:TIGR01678 154 NADVFQAARvslGCLGIIVTVTIQVVPQ 181
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
34-172 1.06e-03

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 40.87  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499211464  34 GQARALVRPGTAEQVTEVLRVCRDVGAHVTVQGGRTSL------VAGTVpehndVLLSterlRSISEVDTVERRLRVGAG 107
Cdd:PRK13905  29 GPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLlvrdggIRGVV-----IRLG----KGLNEIEVEGNRITAGAG 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499211464 108 ATLTAVQNAATAAGLVfGVDLCARATATVGGMASTNAGGlrtvrYG-NMGEQVIGLEVALPDGSLL 172
Cdd:PRK13905 100 APLIKLARFAAEAGLS-GLEFAAGIPGTVGGAVFMNAGA-----YGgETADVLESVEVLDRDGEIK 159
 
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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