DB code: S00385

CATH domain 3.40.109.10 : NADH Oxidase Catalytic domain
E.C. 1.6.99.-
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.109.10 : NADH Oxidase S00386 S00387 S00388

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P46072 Major NAD(P)H-flavin oxidoreductase
EC 1.6.99.-
FRASE I
PF00881 (Nitroreductase)
[Graphical View]
Q56691 NADPH-flavin oxidoreductase
EC 1.6.99.-
Flavin reductase P
NADPH-FMN oxidoreductase
PF00881 (Nitroreductase)
[Graphical View]

KEGG enzyme name
FMN 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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q56691 FRP_VIBHA Monomer. FMN.
P46072 FRA1_VIBFI Homodimer. FMN.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C01847 C00003 C00006 C00061 C00004 C00005 C00080
E.C.
Compound Reduced FMN NAD+ NADP+ FMN NADH NADPH H+
Type amide group,amine group,aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion amide group,amine group,nucleotide amide group,amine group,nucleotide amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion amide group,amine group,nucleotide amide group,amine group,nucleotide others
ChEBI 16048
15846
18009
17621
16908
16474
15378
PubChem 101960650
445395
711
5893
5886
643976
439153
5884
1038
1bkjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FMN Unbound Unbound
1bkjB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FMN Unbound Unbound
1cumA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FMN Unbound Unbound
1cumB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FMN Unbound Unbound
1vfrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FMN Unbound Unbound
1vfrB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FMN Unbound Unbound
2bkjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FMN Unbound Unbound
2bkjB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAD Unbound Bound:FMN Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [5]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bkjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLY 130;GLY 131
1bkjB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLY 130;GLY 131
1cumA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLY 130;GLY 131
1cumB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLY 130;GLY 131
1vfrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 165;GLY 166
1vfrB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 165;GLY 166
2bkjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLY 130;GLY 131
2bkjB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLY 130;GLY 131

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.13537
[5]
p.267
[6]
p.1729-1730

References
[1]
Resource
Comments CHARACTERIZATION
Medline ID 94307374
PubMed ID 8033996
Journal FEBS Lett
Year 1994
Volume 347
Pages 163-8
Authors Inouye S
Title NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein.
Related PDB
Related UniProtKB P46072
[2]
Resource
Comments
Medline ID
PubMed ID 8057370
Journal J Mol Biol
Year 1994
Volume 241
Pages 283-7
Authors Tanner J, Lei B, Liu M, Tu SC, Krause KL
Title Crystallization and preliminary crystallographic analysis of NADPH:FMN oxidoreductase from Vibrio harveyi.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID 97040519
PubMed ID 8885832
Journal Biochemistry
Year 1996
Volume 35
Pages 13531-9
Authors Tanner JJ, Lei B, Tu SC, Krause KL
Title Flavin reductase P: structure of a dimeric enzyme that reduces flavin.
Related PDB 1bkj 1cum
Related UniProtKB Q56691
[4]
Resource
Comments
Medline ID
PubMed ID 8776889
Journal J Struct Biol
Year 1996
Volume 117
Pages 70-2
Authors Koike H, Sasaki H, Tanokura M, Zenno S, Saigo K
Title Crystallization and preliminary crystallographic analysis of the major NAD(P)H: FMN oxidoreductase of Vibrio fischeri ATCC 7744.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID 98319858
PubMed ID 9654450
Journal J Mol Biol
Year 1998
Volume 280
Pages 259-73
Authors Koike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M
Title 1.8 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 PDB 1vfr
Related UniProtKB P46072
[6]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10493573
Journal Protein Sci
Year 1999
Volume 8
Pages 1725-32
Authors Tanner JJ, Tu SC, Barbour LJ, Barnes CL, Krause KL
Title Unusual folded conformation of nicotinamide adenine dinucleotide bound to flavin reductase P.
Related PDB 2bkj
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10869187
Journal Biochemistry
Year 2000
Volume 39
Pages 7813-9
Authors Wang H, Lei B, Tu SC
Title Vibrio harveyi NADPH-FMN oxidoreductase arg203 as a critical residue for NADPH recognition and binding.
Related PDB
Related UniProtKB

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.

Created Updated
2004-02-04 2012-10-03