DB code: S00387

CATH domain 3.40.109.10 : NADH Oxidase Catalytic domain
E.C. 1.-.-.-
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.109.10 : NADH Oxidase S00385 S00386 S00388

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P17117 Oxygen-insensitive NADPH nitroreductase
EC 1.-.-.-
Modulator of drug activity A
NP_415372.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489124.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00881 (Nitroreductase)
[Graphical View]

KEGG enzyme name

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P17117 NFSA_ECOLI FMN.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00061 C00005 C06813 C00080 C00006 C02720 C00001
E.C.
Compound FMN NADPH Nitrobenzene H+ NADP+ N-Hydroxyarylamine H2O
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion amide group,amine group,nucleotide aromatic ring (only carbon atom),nitro group others amide group,amine group,nucleotide amine group,aromatic ring (only carbon atom) H2O
ChEBI 17621
16474
27798
15378
18009
28902
15377
PubChem 643976
5884
7416
1038
5886
7518
22247451
962
1f5vA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FMN Unbound Unbound Unbound Unbound
1f5vB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FMN Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1f5vA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f5vB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.267

References
[1]
Resource
Comments
Medline ID
PubMed ID 374406
Journal J Biol Chem
Year 1979
Volume 254
Pages 4009-14
Authors Peterson FJ, Mason RP, Hovsepian J, Holtzman JL
Title Oxygen-sensitive and -insensitive nitroreduction by Escherichia coli and rat hepatic microsomes.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8755878
Journal J Bacteriol
Year 1996
Volume 178
Pages 4508-14
Authors Zenno S, Koike H, Kumar AN, Jayaraman R, Tanokura M, Saigo K
Title Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase.
Related PDB
Related UniProtKB
[3]
Resource
Comments MUTAGENESIS
Medline ID 98101485
PubMed ID 9440535
Journal J Bacteriol
Year 1998
Volume 180
Pages 422-5
Authors Zenno S, Kobori T, Tanokura M, Saigo K
Title Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavin reductase in Vibrio harveyi, by a single amino acid substitution.
Related PDB
Related UniProtKB P17117
[4]
Resource
Comments Homologous enzyme
Medline ID
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
Related UniProtKB
[5]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11034992
Journal J Biol Chem
Year 2001
Volume 276
Pages 2816-23
Authors Kobori T, Sasaki H, Lee WC, Zenno S, Saigo K, Murphy ME, Tanokura M
Title Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution.
Related PDB 1f5v
Related UniProtKB

Comments
The substrates and products are annotated based on literature [1].
Although this enzyme is homologous to other NADPH nitrogenase (S00388 in EzCatDB), the catalytic residues are not conserved in this enzyme.

Created Updated
2004-07-12 2009-02-26