EzCatDB: S00385
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DB codeS00385
CATH domainDomain 13.40.109.10 : NADH OxidaseCatalytic domain
E.C.1.6.99.-

CATH domainRelated DB codes (homologues)
3.40.109.10 : NADH OxidaseS00386,S00387,S00388

Enzyme Name
UniProtKBKEGG

P46072Q56691
Protein nameMajor NAD(P)H-flavin oxidoreductaseNADPH-flavin oxidoreductaseFMN reductase
NAD(P)H-FMN reductase
NAD(P)H-dependent FMN reductase
NAD(P)H:FMN oxidoreductase
NAD(P)H:flavin oxidoreductase
NAD(P)H2 dehydrogenase (FMN)
NAD(P)H2:FMN oxidoreductase
SsuE
riboflavin mononucleotide reductase
flavine mononucleotide reductase
riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide(phosphate)) reductase
flavin mononucleotide reductase
riboflavine mononucleotide reductase
SynonymsEC 1.6.99.-
FRASE I
EC 1.6.99.-
NADPH-FMN oxidoreductase
Flavin reductase P
PfamPF00881 (Nitroreductase)
[Graphical view]
PF00881 (Nitroreductase)
[Graphical view]


UniProtKB:Accession NumberP46072Q56691
Entry nameFRA1_VIBFIFRP_VIBHA
Activity

SubunitHomodimer.Monomer.
Subcellular location

CofactorFMN.FMN.

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01847C00003C00006C00061C00004C00005C00080
CompoundReduced FMNNAD+NADP+FMNNADHNADPHH+
Typeamide group,amine group,aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotideamide group,amine group,nucleotideamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotideamide group,amine group,nucleotideothers
ChEBI16048
15846
18009
17621
16908
16474
15378
PubChem711
445395
101960650
5893
5886
643976
439153
5884
1038
               
1bkjAUnboundUnboundUnboundBound:FMNUnboundUnbound 
1bkjBUnboundUnboundUnboundBound:FMNUnboundUnbound 
1cumAUnboundUnboundUnboundBound:FMNUnboundUnbound 
1cumBUnboundUnboundUnboundBound:FMNUnboundUnbound 
1vfrAUnboundUnboundUnboundBound:FMNUnboundUnbound 
1vfrBUnboundUnboundUnboundBound:FMNUnboundUnbound 
2bkjAUnboundUnboundUnboundBound:FMNUnboundUnbound 
2bkjBUnboundBound:NADUnboundBound:FMNUnboundUnbound 

Active-site residues
resource
literature [5]
pdbMain-chain involved in catalysis
         
1bkjAGLY 130;GLY 131
1bkjBGLY 130;GLY 131
1cumAGLY 130;GLY 131
1cumBGLY 130;GLY 131
1vfrAGLU 165;GLY 166
1vfrBGLU 165;GLY 166
2bkjAGLY 130;GLY 131
2bkjBGLY 130;GLY 131

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.13537
[5]p.267
[6]p.1729-1730

references
[1]
CommentsCHARACTERIZATION
Medline ID94307374
PubMed ID8033996
JournalFEBS Lett
Year1994
Volume347
Pages163-8
AuthorsInouye S
TitleNAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein.
Related UniProtKBP46072
[2]
PubMed ID8057370
JournalJ Mol Biol
Year1994
Volume241
Pages283-7
AuthorsTanner J, Lei B, Liu M, Tu SC, Krause KL
TitleCrystallization and preliminary crystallographic analysis of NADPH:FMN oxidoreductase from Vibrio harveyi.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID97040519
PubMed ID8885832
JournalBiochemistry
Year1996
Volume35
Pages13531-9
AuthorsTanner JJ, Lei B, Tu SC, Krause KL
TitleFlavin reductase P: structure of a dimeric enzyme that reduces flavin.
Related PDB1bkj,1cum
Related UniProtKBQ56691
[4]
PubMed ID8776889
JournalJ Struct Biol
Year1996
Volume117
Pages70-2
AuthorsKoike H, Sasaki H, Tanokura M, Zenno S, Saigo K
TitleCrystallization and preliminary crystallographic analysis of the major NAD(P)H: FMN oxidoreductase of Vibrio fischeri ATCC 7744.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID98319858
PubMed ID9654450
JournalJ Mol Biol
Year1998
Volume280
Pages259-73
AuthorsKoike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M
Title1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins.
Related PDB1vfr
Related UniProtKBP46072
[6]
CommentsX-ray crystallography
PubMed ID10493573
JournalProtein Sci
Year1999
Volume8
Pages1725-32
AuthorsTanner JJ, Tu SC, Barbour LJ, Barnes CL, Krause KL
TitleUnusual folded conformation of nicotinamide adenine dinucleotide bound to flavin reductase P.
Related PDB2bkj
[7]
PubMed ID10869187
JournalBiochemistry
Year2000
Volume39
Pages7813-9
AuthorsWang H, Lei B, Tu SC
TitleVibrio harveyi NADPH-FMN oxidoreductase arg203 as a critical residue for NADPH recognition and binding.

comments
This enzyme was transferred from E.C. 1.6.8.1 to E.C. 1.5.1.29, which is now obsolete. However, according to the Swiss-prot data, its E.C. number is E.C. 1.6.99.-. Considering the activity of this enzyme, it is adequate that this enzyme can be classified in E.C. 1.5.1.38, 1.5.1.39 and 1.5.1.41.

createdupdated
2004-02-042012-10-03


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