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Conserved domains on  [gi|446210066|ref|WP_000287921|]
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MULTISPECIES: flavin reductase family protein [Staphylococcus]

Protein Classification

flavin reductase family protein( domain architecture ID 10004785)

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
Gene Ontology:  GO:0010181|GO:0016491
PubMed:  32951820
SCOP:  4002136

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 12-166 1.05e-37

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: 128.02  E-value: 1.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210066  12 RENYKLLIGSIIPRpIAFVTTLNQDASVNAAPFSFFNIVNNHPPMIAIAVqragGKRKDTALNIERTGDFVVHITDEDNV 91
Cdd:COG1853    2 PDAFRDALGRLAPG-VAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSV----AKSSDTLENIRETGEFVVNVLSEDQA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446210066  92 QDINETAAPLAYGDSELSRTKLSlLTSTTIKTPGIKDAKMRFECKLSQMILLGDvldgADLIIGEIVTYHIDDSI 166
Cdd:COG1853   77 ELANRFAGRSGRGVDKFAGAGLT-TASGEVGAPLLAEAPAWLECRVVDVIELGD----HTLFIGEVVAVHVDEDV 146
 
Name Accession Description Interval E-value
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 12-166 1.05e-37

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: 128.02  E-value: 1.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210066  12 RENYKLLIGSIIPRpIAFVTTLNQDASVNAAPFSFFNIVNNHPPMIAIAVqragGKRKDTALNIERTGDFVVHITDEDNV 91
Cdd:COG1853    2 PDAFRDALGRLAPG-VAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSV----AKSSDTLENIRETGEFVVNVLSEDQA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446210066  92 QDINETAAPLAYGDSELSRTKLSlLTSTTIKTPGIKDAKMRFECKLSQMILLGDvldgADLIIGEIVTYHIDDSI 166
Cdd:COG1853   77 ELANRFAGRSGRGVDKFAGAGLT-TASGEVGAPLLAEAPAWLECRVVDVIELGD----HTLFIGEVVAVHVDEDV 146
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 21-164 4.80e-24

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: 92.61  E-value: 4.80e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210066    21 SIIPRPIAFVTTLNQDAS-VNAAPFSFFNiVNNHPPMIAIAVQRAGGKRKDtalnIERTGDFVVHITDEDNVQDINETAA 99
Cdd:smart00903   2 GRFPTGVAVVTTRDGDGGrVGLTASSFVS-VSLDPPLVLVCVAKSSSTHPL----IRESGRFVVNVLAEDQADLARRFAG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446210066   100 PlaYGDSELSRTKLSLLTSTTIKTPGIKDAKMRFECKLSQMILLGDvldgADLIIGEIVTYHIDD 164
Cdd:smart00903  77 K--SGADRFEGVAWGLTEAGVTGAPILAGALAWLECRVVQVIEVGD----HTIFVGEVVAVHVRD 135
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 23-168 6.29e-20

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: 81.94  E-value: 6.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210066   23 IPRPIAFVTTlNQDASVNAAPFSFFNIVNNHPPMIAIAVQRaggkRKDTALNIERTGDFVVHITDEDNVQDINETAAPla 102
Cdd:pfam01613   4 FPTGVAVVTT-DDGGEPNGMTVSSFTSVSLDPPLVLVSINR----SSSTHDAIEASGEFVVNVLAEDQEELARRFAGR-- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446210066  103 YGDSELSRTKlslLTSTTIKTPGIKDAKMRFECKLSQMILLGDvldgADLIIGEIVTYHIDDSIYE 168
Cdd:pfam01613  77 SGRDKFAGIT---WVEGKVGAPLLKGALAALECRVVDTVDVGD----HTLFIGEVVDVRVDEDADG 135
 
Name Accession Description Interval E-value
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 12-166 1.05e-37

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: 128.02  E-value: 1.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210066  12 RENYKLLIGSIIPRpIAFVTTLNQDASVNAAPFSFFNIVNNHPPMIAIAVqragGKRKDTALNIERTGDFVVHITDEDNV 91
Cdd:COG1853    2 PDAFRDALGRLAPG-VAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSV----AKSSDTLENIRETGEFVVNVLSEDQA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446210066  92 QDINETAAPLAYGDSELSRTKLSlLTSTTIKTPGIKDAKMRFECKLSQMILLGDvldgADLIIGEIVTYHIDDSI 166
Cdd:COG1853   77 ELANRFAGRSGRGVDKFAGAGLT-TASGEVGAPLLAEAPAWLECRVVDVIELGD----HTLFIGEVVAVHVDEDV 146
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 21-164 4.80e-24

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: 92.61  E-value: 4.80e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210066    21 SIIPRPIAFVTTLNQDAS-VNAAPFSFFNiVNNHPPMIAIAVQRAGGKRKDtalnIERTGDFVVHITDEDNVQDINETAA 99
Cdd:smart00903   2 GRFPTGVAVVTTRDGDGGrVGLTASSFVS-VSLDPPLVLVCVAKSSSTHPL----IRESGRFVVNVLAEDQADLARRFAG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446210066   100 PlaYGDSELSRTKLSLLTSTTIKTPGIKDAKMRFECKLSQMILLGDvldgADLIIGEIVTYHIDD 164
Cdd:smart00903  77 K--SGADRFEGVAWGLTEAGVTGAPILAGALAWLECRVVQVIEVGD----HTIFVGEVVAVHVRD 135
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 23-168 6.29e-20

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: 81.94  E-value: 6.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446210066   23 IPRPIAFVTTlNQDASVNAAPFSFFNIVNNHPPMIAIAVQRaggkRKDTALNIERTGDFVVHITDEDNVQDINETAAPla 102
Cdd:pfam01613   4 FPTGVAVVTT-DDGGEPNGMTVSSFTSVSLDPPLVLVSINR----SSSTHDAIEASGEFVVNVLAEDQEELARRFAGR-- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446210066  103 YGDSELSRTKlslLTSTTIKTPGIKDAKMRFECKLSQMILLGDvldgADLIIGEIVTYHIDDSIYE 168
Cdd:pfam01613  77 SGRDKFAGIT---WVEGKVGAPLLKGALAALECRVVDTVDVGD----HTLFIGEVVDVRVDEDADG 135
 
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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