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Conserved domains on  [gi|740730740|ref|WP_038516026|]
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MULTISPECIES: 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase reductase subunit [Amycolatopsis]

Protein Classification

flavin reductase family protein( domain architecture ID 10658186)

flavin reductase family protein such as flavin reductase that catalyzes the reduction of FMN, and to a lesser extent, FAD, using NADH as an electron donor

CATH:  2.30.110.10
EC:  1.-.-.-
Gene Ontology:  GO:0010181|GO:0016491
SCOP:  4002136

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 20-161 8.38e-57

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


:

Pssm-ID: 214900  Cd Length: 147  Bit Score: 175.42  E-value: 8.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740    20 LGHFCTGVAVVTGHDGE-APVGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSAVFGAR-GA 97
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDgGRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAGKsGA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740730740    98 DKFASVDWTPAPS---GSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTALGEPSDDRPLLFHRGRY 161
Cdd:smart00903  81 DRFEGVAWGLTEAgvtGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHVRDDGEPLVYHRGGY 147
 
Name Accession Description Interval E-value
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 20-161 8.38e-57

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


Pssm-ID: 214900  Cd Length: 147  Bit Score: 175.42  E-value: 8.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740    20 LGHFCTGVAVVTGHDGE-APVGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSAVFGAR-GA 97
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDgGRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAGKsGA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740730740    98 DKFASVDWTPAPS---GSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTALGEPSDDRPLLFHRGRY 161
Cdd:smart00903  81 DRFEGVAWGLTEAgvtGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHVRDDGEPLVYHRGGY 147
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 12-163 2.18e-55

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441458  Cd Length: 160  Bit Score: 172.32  E-value: 2.18e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740  12 DPARFRTVLGHFCTGVAVVT-GHDGEAPVGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSA 90
Cdd:COG1853    1 MPDAFRDALGRLAPGVAVVTtRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740  91 VFGA---RGADKFASVDWTPA--PSGSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTAL--GEPSDDRPLLFHRGRYTV 163
Cdd:COG1853   81 RFAGrsgRGVDKFAGAGLTTAsgEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVhvDEDVDGRPLLYLGGRYRR 160
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 20-162 1.05e-50

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


Pssm-ID: 460266  Cd Length: 149  Bit Score: 160.14  E-value: 1.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740   20 LGHFCTGVAVVTGHDGEAPVGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSAVFGAR-GAD 98
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLAEDQEELARRFAGRsGRD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740730740   99 KFASVDWTPAPSGSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTALGEPSDD--RPLLFHRGRYT 162
Cdd:pfam01613  81 KFAGITWVEGKVGAPLLKGALAALECRVVDTVDVGDHTLFIGEVVDVRVDEDAdgEPLLYYRRRYR 146
hpaC PRK15486
4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
 15-161 1.72e-10

4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional


Pssm-ID: 185383  Cd Length: 170  Bit Score: 56.97  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740  15 RFRTVLGHFCTGVAVVT--GHDGEApvGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSAVF 92
Cdd:PRK15486   9 RFRDAMASLSAAVNIVTtaGDAGRC--GITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQELMARHF 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740730740  93 ----GARGADKFASVDWTPAPSGSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTALGEPSDDRPLLFHRGRY 161
Cdd:PRK15486  87 agmtGMAMEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYLVEIKNIILSAEGHGLIYFKRRF 159
 
Name Accession Description Interval E-value
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 20-161 8.38e-57

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


Pssm-ID: 214900  Cd Length: 147  Bit Score: 175.42  E-value: 8.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740    20 LGHFCTGVAVVTGHDGE-APVGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSAVFGAR-GA 97
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDgGRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAGKsGA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740730740    98 DKFASVDWTPAPS---GSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTALGEPSDDRPLLFHRGRY 161
Cdd:smart00903  81 DRFEGVAWGLTEAgvtGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHVRDDGEPLVYHRGGY 147
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 12-163 2.18e-55

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441458  Cd Length: 160  Bit Score: 172.32  E-value: 2.18e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740  12 DPARFRTVLGHFCTGVAVVT-GHDGEAPVGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSA 90
Cdd:COG1853    1 MPDAFRDALGRLAPGVAVVTtRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740  91 VFGA---RGADKFASVDWTPA--PSGSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTAL--GEPSDDRPLLFHRGRYTV 163
Cdd:COG1853   81 RFAGrsgRGVDKFAGAGLTTAsgEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVhvDEDVDGRPLLYLGGRYRR 160
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 20-162 1.05e-50

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


Pssm-ID: 460266  Cd Length: 149  Bit Score: 160.14  E-value: 1.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740   20 LGHFCTGVAVVTGHDGEAPVGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSAVFGAR-GAD 98
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLAEDQEELARRFAGRsGRD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740730740   99 KFASVDWTPAPSGSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTALGEPSDD--RPLLFHRGRYT 162
Cdd:pfam01613  81 KFAGITWVEGKVGAPLLKGALAALECRVVDTVDVGDHTLFIGEVVDVRVDEDAdgEPLLYYRRRYR 146
hpaC PRK15486
4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
 15-161 1.72e-10

4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional


Pssm-ID: 185383  Cd Length: 170  Bit Score: 56.97  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740  15 RFRTVLGHFCTGVAVVT--GHDGEApvGFACQSFAALSLDPPLVLFCPAKTSRTWAVLAESGRFAVNVLAEDQQDVSAVF 92
Cdd:PRK15486   9 RFRDAMASLSAAVNIVTtaGDAGRC--GITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQELMARHF 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740730740  93 ----GARGADKFASVDWTPAPSGSPLLTGALTWIDCTLEAVHEAGDHYVVVGRVTALGEPSDDRPLLFHRGRY 161
Cdd:PRK15486  87 agmtGMAMEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYLVEIKNIILSAEGHGLIYFKRRF 159
COG2457 COG2457
Uncharacterized conserved protein, DUF447 domain [Function unknown];
37-165 9.22e-05

Uncharacterized conserved protein, DUF447 domain [Function unknown];


Pssm-ID: 441992  Cd Length: 183  Bit Score: 40.99  E-value: 9.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740730740  37 APVGFACqsfaalslDPPLVLFCPAKTSRTWAVLAESGRFAVNVLaedqQDVS----AVFGARGADKFASVDWTPAPsgS 112
Cdd:COG2457   19 APMGIIV--------KGDELVLRPFKGSTTYENLLATGEAVVNVT----DDPRvfagSLFGRLDPEDFPLVPAERVD--G 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 740730740 113 PLLTGALTWIDCTLEAVHEAGDHYVVVGRVTALGEpSDDRPLLFHRGRYTVTE 165
Cdd:COG2457   85 PRLKDALAHIELEVTSIEDDSERPVLELRVVHIGI-HRPPFRGFNRAQAAVIE 136
 
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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