EzCatDB: S00387
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DB codeS00387
CATH domainDomain 13.40.109.10 : NADH OxidaseCatalytic domain
E.C.1.-.-.-

CATH domainRelated DB codes (homologues)
3.40.109.10 : NADH OxidaseS00385,S00386,S00388

Enzyme Name
UniProtKB

P17117
Protein nameOxygen-insensitive NADPH nitroreductase
SynonymsEC 1.-.-.-
Modulator of drug activity A
RefSeqNP_415372.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489124.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF00881 (Nitroreductase)
[Graphical view]


UniProtKB:Accession NumberP17117
Entry nameNFSA_ECOLI
Activity
Subunit
Subcellular location
CofactorFMN.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00061C00005C06813C00080C00006C02720C00001
CompoundFMNNADPHNitrobenzeneH+NADP+N-HydroxyarylamineH2O
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotidearomatic ring (only carbon atom),nitro groupothersamide group,amine group,nucleotideamine group,aromatic ring (only carbon atom)H2O
ChEBI17621
16474
27798
15378
18009
28902
15377
PubChem643976
5884
7416
1038
5886
7518
962
22247451
               
1f5vABound:FMNUnboundUnbound UnboundUnbound 
1f5vBBound:FMNUnboundUnbound UnboundUnbound 

Active-site residues
pdb
        
1f5vA
1f5vB

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.267

references
[1]
PubMed ID374406
JournalJ Biol Chem
Year1979
Volume254
Pages4009-14
AuthorsPeterson FJ, Mason RP, Hovsepian J, Holtzman JL
TitleOxygen-sensitive and -insensitive nitroreduction by Escherichia coli and rat hepatic microsomes.
[2]
PubMed ID8755878
JournalJ Bacteriol
Year1996
Volume178
Pages4508-14
AuthorsZenno S, Koike H, Kumar AN, Jayaraman R, Tanokura M, Saigo K
TitleBiochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase.
[3]
CommentsMUTAGENESIS
Medline ID98101485
PubMed ID9440535
JournalJ Bacteriol
Year1998
Volume180
Pages422-5
AuthorsZenno S, Kobori T, Tanokura M, Saigo K
TitleConversion 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 UniProtKBP17117
[4]
CommentsHomologous enzyme
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.
[5]
CommentsX-ray crystallography
PubMed ID11034992
JournalJ Biol Chem
Year2001
Volume276
Pages2816-23
AuthorsKobori T, Sasaki H, Lee WC, Zenno S, Saigo K, Murphy ME, Tanokura M
TitleStructure 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 PDB1f5v

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.

createdupdated
2004-07-122009-02-26


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