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Protein

FMN reductase [NAD(P)H]

Gene

nfrA2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reduces FMNH2 to FMN, with NADH or NADPH as reductant. It also reduces nitroaromatic compounds, quinones, chromates and azo dyes. It could supply the reduced form of FMN to luciferase-like protein and contribute to the degradation of aromatic compounds.1 Publication

Catalytic activityi

FMNH2 + NAD(P)+ = FMN + NAD(P)H.

Cofactori

FMN1 PublicationNote: Binds 1 FMN per subunit.1 Publication

Enzyme regulationi

FMN is a competitive inhibitor of NADH, and therefore leads to the preferential utilization of NADPH.1 Publication

Kineticsi

  1. KM=0.2 µM for 4-nitrophenol (NP)(at pH 8 and 25 degrees Celisus)1 Publication
  2. KM=0.7 µM for 5-nitro-2-furaldehyde semicarbazone (NF)(at pH 8 and 25 degrees Celisus)1 Publication
  3. KM=4.2 µM for FMN (at pH 8 and 25 degrees Celisus)1 Publication
  4. KM=4.4 µM for NADPH (at pH 8 and 25 degrees Celisus)1 Publication
  5. KM=5.0 µM for chromate (at pH 8 and 25 degrees Celisus)1 Publication
  6. KM=6.4 µM for NADH (at pH 8 and 25 degrees Celisus)1 Publication
  7. KM=96 µM for methyl-4-nitrobenzenesulfonate (NBS)(at pH 8 and 25 degrees Celisus)1 Publication
  1. Vmax=0.9 µmol/min/mg enzyme with chromate as substrate (at pH 8 and 25 degrees Celisus)1 Publication
  2. Vmax=4.0 µmol/min/mg enzyme with 5-nitro-2-furaldehyde semicarbazone (nitrofurazone, NF) as substrate (at pH 8 and 25 degrees Celisus)1 Publication
  3. Vmax=7.0 µmol/min/mg enzyme with 4-nitrophenol (NP) as substrate (at pH 8 and 25 degrees Celisus)1 Publication
  4. Vmax=73.6 µmol/min/mg enzyme with methyl-4-nitrobenzenesulfonate (NBS) as substrate (at pH 8 and 25 degrees Celisus)1 Publication
  5. Vmax=200 µmol/min/mg enzyme with FMN as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei67FMN1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Detoxification

Keywords - Ligandi

Flavoprotein, FMN, NAD

Enzyme and pathway databases

BioCyciBSUB:BSU03860-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
FMN reductase [NAD(P)H] (EC:1.5.1.39)
Alternative name(s):
NAD(P)H-dependent FMN reductase
NAD(P)H-dependent nitro/flavin reductase
NAD(P)H-dependent nitroreductase
NAD(P)H-dependent oxidoreductase
Gene namesi
Name:nfrA2
Synonyms:ycnD
Ordered Locus Names:BSU03860
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002055131 – 249FMN reductase [NAD(P)H]Add BLAST249

Proteomic databases

PaxDbiP94424.

Expressioni

Inductioni

Strongly induced by stress due to exposure to 6-brom-2-vinyl-chroman-4-on (chromanon) and less strongly induced after exposure to 2-methylhydroquinone (2-MHQ) or catechol stress.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002178.

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 9Combined sources7
Helixi24 – 36Combined sources13
Helixi40 – 42Combined sources3
Beta strandi46 – 51Combined sources6
Helixi54 – 63Combined sources10
Helixi68 – 72Combined sources5
Beta strandi73 – 82Combined sources10
Helixi84 – 94Combined sources11
Helixi100 – 102Combined sources3
Helixi104 – 127Combined sources24
Beta strandi131 – 135Combined sources5
Helixi136 – 139Combined sources4
Helixi142 – 148Combined sources7
Beta strandi155 – 164Combined sources10
Helixi178 – 181Combined sources4
Beta strandi184 – 186Combined sources3
Helixi190 – 212Combined sources23
Helixi220 – 228Combined sources9
Helixi236 – 242Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZCHX-ray1.85A1-249[»]
ProteinModelPortaliP94424.
SMRiP94424.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP94424.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 15FMN-binding5
Regioni134 – 136FMN-binding3
Regioni173 – 175FMN-binding3

Sequence similaritiesi

Belongs to the flavin oxidoreductase frp family.Curated

Phylogenomic databases

eggNOGiENOG4108DBC. Bacteria.
COG0778. LUCA.
HOGENOMiHOG000272869.
InParanoidiP94424.
KOiK19286.
OMAiPKYVFPV.
PhylomeDBiP94424.

Family and domain databases

CDDicd02146. NfsA_FRP. 1 hit.
Gene3Di3.40.109.10. 1 hit.
InterProiIPR016446. Flavin_OxRdtase_Frp.
IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
PIRSFiPIRSF005426. Frp. 1 hit.
SUPFAMiSSF55469. SSF55469. 1 hit.

Sequencei

Sequence statusi: Complete.

P94424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEVIKSLTD HRSIRSYTDE PVAQEQLDQI IEAVQSAPSS INGQQVTVIT
60 70 80 90 100
VQDKERKKKI SELAGGQPWI DQAPVFLLFC ADFNRAKIAL EDLHDFKMEI
110 120 130 140 150
TNGLESVLVG AVDAGIALGT ATAAAESLGL GTVPIGAVRG NPQELIELLE
160 170 180 190 200
LPKYVFPLSG LVIGHPADRS AKKPRLPQEA VNHQETYLNQ DELTSHIQAY
210 220 230 240
DEQMSEYMNK RTNGKETRNW SQSIASYYER LYYPHIREML EKQGFKVEK
Length:249
Mass (Da):27,868
Last modified:May 1, 1997 - v1
Checksum:i691BEAE44234FA59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50453 Genomic DNA. Translation: BAA09018.1.
AF417208 Genomic DNA. Translation: AAL09698.1.
AL009126 Genomic DNA. Translation: CAB12194.1.
PIRiH69763.
RefSeqiNP_388268.1. NC_000964.3.
WP_003234479.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12194; CAB12194; BSU03860.
GeneIDi938267.
KEGGibsu:BSU03860.
PATRICi18972346. VBIBacSub10457_0401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50453 Genomic DNA. Translation: BAA09018.1.
AF417208 Genomic DNA. Translation: AAL09698.1.
AL009126 Genomic DNA. Translation: CAB12194.1.
PIRiH69763.
RefSeqiNP_388268.1. NC_000964.3.
WP_003234479.1. NZ_JNCM01000031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZCHX-ray1.85A1-249[»]
ProteinModelPortaliP94424.
SMRiP94424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002178.

Proteomic databases

PaxDbiP94424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12194; CAB12194; BSU03860.
GeneIDi938267.
KEGGibsu:BSU03860.
PATRICi18972346. VBIBacSub10457_0401.

Phylogenomic databases

eggNOGiENOG4108DBC. Bacteria.
COG0778. LUCA.
HOGENOMiHOG000272869.
InParanoidiP94424.
KOiK19286.
OMAiPKYVFPV.
PhylomeDBiP94424.

Enzyme and pathway databases

BioCyciBSUB:BSU03860-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP94424.

Family and domain databases

CDDicd02146. NfsA_FRP. 1 hit.
Gene3Di3.40.109.10. 1 hit.
InterProiIPR016446. Flavin_OxRdtase_Frp.
IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
PIRSFiPIRSF005426. Frp. 1 hit.
SUPFAMiSSF55469. SSF55469. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNFRA2_BACSU
AccessioniPrimary (citable) accession number: P94424
Secondary accession number(s): Q548A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: November 2, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Catalyzis proceeds by a classical ping-pong bi-bi reaction mechanism. The reduction of nitro-organic compounds and inorganic chromate occur in the absence of external FMN and are therefore believed to require binding of these substrates in the active site. In contrast to these reduction processes, azo dyes are reduced only in the presence of external FMN, indicating that azo dye reduction occurs outside the active site of the enzyme.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.