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Conserved domains on  [gi|2063608362|gb|QXI26169|]
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flavin reductase [Pseudomonas vanderleydeniana]

Protein Classification

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, ...
 6-155 9.09e-60

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: 188.11  E-value: 9.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362   6 DSRAFRRALGNFATGVTVVTAATADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSN 85
Cdd:COG1853     1 MPDAFRDALGRLAPGVAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2063608362  86 HFAR---SKDDRFA--DIEHEVGEGGAPLLADCSARFRCEKYQMVDGGDHWILIGKVVAF---DDFGRAPLLYHQGAY 155
Cdd:COG1853    81 RFAGrsgRGVDKFAgaGLTTASGEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVhvdEDVDGRPLLYLGGRY 158
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
175-308 3.04e-11

DNA-binding transcriptional regulator, MarR family [Transcription];


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 60.37  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362 175 SHFQGRLRDNLYYLMTQAVRCYQGTYQPRQLATGLRTSEARMLMVLENDAGLSQAELLREVAMPQREVEEAIANLCRKGL 254
Cdd:COG1846     2 SDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063608362 255 VTETEG-------RVRLSVAGIDQTEALWTIAREQQERVFSQFDEEQVANFKQVLQAIISA 308
Cdd:COG1846    82 VEREPDpedrravLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
 
Name Accession Description Interval E-value
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 6-155 9.09e-60

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: 188.11  E-value: 9.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362   6 DSRAFRRALGNFATGVTVVTAATADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSN 85
Cdd:COG1853     1 MPDAFRDALGRLAPGVAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2063608362  86 HFAR---SKDDRFA--DIEHEVGEGGAPLLADCSARFRCEKYQMVDGGDHWILIGKVVAF---DDFGRAPLLYHQGAY 155
Cdd:COG1853    81 RFAGrsgRGVDKFAgaGLTTASGEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVhvdEDVDGRPLLYLGGRY 158
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 14-155 1.26e-59

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: 187.37  E-value: 1.26e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362   14 LGNFATGVTVVTAATADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSNHFA-RSKD 92
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDGGRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAgKSGA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2063608362   93 DRFADIEH---EVGEGGAPLLADCSARFRCEKYQMVDGGDHWILIGKVVAFD-DFGRAPLLYHQGAY 155
Cdd:smart00903  81 DRFEGVAWgltEAGVTGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHvRDDGEPLVYHRGGY 147
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 14-155 1.08e-48

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: 159.37  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362  14 LGNFATGVTVVTAaTADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSNHFA-RSKD 92
Cdd:pfam01613   1 MRRFPTGVAVVTT-DDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLAEDQEELARRFAgRSGR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2063608362  93 DRFADIEHEVGEGGAPLLADCSARFRCEKYQMVDGGDHWILIGKVVAF---DDFGRAPLLYHQGAY 155
Cdd:pfam01613  80 DKFAGITWVEGKVGAPLLKGALAALECRVVDTVDVGDHTLFIGEVVDVrvdEDADGEPLLYYRRRY 145
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
175-308 3.04e-11

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 60.37  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362 175 SHFQGRLRDNLYYLMTQAVRCYQGTYQPRQLATGLRTSEARMLMVLENDAGLSQAELLREVAMPQREVEEAIANLCRKGL 254
Cdd:COG1846     2 SDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063608362 255 VTETEG-------RVRLSVAGIDQTEALWTIAREQQERVFSQFDEEQVANFKQVLQAIISA 308
Cdd:COG1846    82 VEREPDpedrravLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
hpaC PRK15486
4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
 10-134 5.94e-07

4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional


Pssm-ID: 185383  Cd Length: 170  Bit Score: 48.50  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362  10 FRRALGNFATGVTVVTAAtADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSNHFA- 88
Cdd:PRK15486   10 FRDAMASLSAAVNIVTTA-GDAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQELMARHFAg 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2063608362  89 ---RSKDDRFADIEHEVGEGGAPLLADCSARFRCEKYQMVDGGDHWILI 134
Cdd:PRK15486   89 mtgMAMEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYL 137
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 207-260 2.16e-04

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 38.72  E-value: 2.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2063608362 207 TGLRTSEARMLMVLENDAGLSQAELLREVAMPQREVEEAIANLCRKGLVTETEG 260
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPS 54
 
Name Accession Description Interval E-value
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 6-155 9.09e-60

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: 188.11  E-value: 9.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362   6 DSRAFRRALGNFATGVTVVTAATADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSN 85
Cdd:COG1853     1 MPDAFRDALGRLAPGVAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2063608362  86 HFAR---SKDDRFA--DIEHEVGEGGAPLLADCSARFRCEKYQMVDGGDHWILIGKVVAF---DDFGRAPLLYHQGAY 155
Cdd:COG1853    81 RFAGrsgRGVDKFAgaGLTTASGEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVhvdEDVDGRPLLYLGGRY 158
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 14-155 1.26e-59

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: 187.37  E-value: 1.26e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362   14 LGNFATGVTVVTAATADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSNHFA-RSKD 92
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDGGRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAgKSGA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2063608362   93 DRFADIEH---EVGEGGAPLLADCSARFRCEKYQMVDGGDHWILIGKVVAFD-DFGRAPLLYHQGAY 155
Cdd:smart00903  81 DRFEGVAWgltEAGVTGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHvRDDGEPLVYHRGGY 147
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 14-155 1.08e-48

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: 159.37  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362  14 LGNFATGVTVVTAaTADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSNHFA-RSKD 92
Cdd:pfam01613   1 MRRFPTGVAVVTT-DDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLAEDQEELARRFAgRSGR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2063608362  93 DRFADIEHEVGEGGAPLLADCSARFRCEKYQMVDGGDHWILIGKVVAF---DDFGRAPLLYHQGAY 155
Cdd:pfam01613  80 DKFAGITWVEGKVGAPLLKGALAALECRVVDTVDVGDHTLFIGEVVDVrvdEDADGEPLLYYRRRY 145
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
175-308 3.04e-11

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 60.37  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362 175 SHFQGRLRDNLYYLMTQAVRCYQGTYQPRQLATGLRTSEARMLMVLENDAGLSQAELLREVAMPQREVEEAIANLCRKGL 254
Cdd:COG1846     2 SDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063608362 255 VTETEG-------RVRLSVAGIDQTEALWTIAREQQERVFSQFDEEQVANFKQVLQAIISA 308
Cdd:COG1846    82 VEREPDpedrravLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
hpaC PRK15486
4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
 10-134 5.94e-07

4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional


Pssm-ID: 185383  Cd Length: 170  Bit Score: 48.50  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063608362  10 FRRALGNFATGVTVVTAAtADGRRVGVTANSFNSVSLEPALILWSLDKRSGSLEVFEQASHFAVNILAADQIDHSNHFA- 88
Cdd:PRK15486   10 FRDAMASLSAAVNIVTTA-GDAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQELMARHFAg 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2063608362  89 ---RSKDDRFADIEHEVGEGGAPLLADCSARFRCEKYQMVDGGDHWILI 134
Cdd:PRK15486   89 mtgMAMEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYL 137
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 207-260 2.16e-04

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 38.72  E-value: 2.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2063608362 207 TGLRTSEARMLMVLENDAGLSQAELLREVAMPQREVEEAIANLCRKGLVTETEG 260
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPS 54
 
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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