EzCatDB: S00388
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DB codeS00388
CATH domainDomain 13.40.109.10 : NADH OxidaseCatalytic domain
E.C.1.5.1.34,1.-.-.-
MACiEM0211

CATH domainRelated DB codes (homologues)
3.40.109.10 : NADH OxidaseS00385,S00386,S00387

Enzyme Name
UniProtKBKEGG

P38489Q01234
Protein nameOxygen-insensitive NAD(P)H nitroreductaseOxygen-insensitive NAD(P)H nitroreductase6,7-dihydropteridine reductase
   (EC 1.5.1.34)

6,7-dihydropteridine:NAD(P)H oxidoreductase
   (EC 1.5.1.34)

DHPR
   (EC 1.5.1.34)

NAD(P)H:6,7-dihydropteridine oxidoreductase
   (EC 1.5.1.34)

NADH-dihydropteridine reductase
   (EC 1.5.1.34)

NADPH-dihydropteridine reductase
   (EC 1.5.1.34)

NADPH-specific dihydropteridine reductase
   (EC 1.5.1.34)

dihydropteridine (reduced nicotinamide adenine dinucleotide)reductase
   (EC 1.5.1.34)

dihydropteridine reductase
   (EC 1.5.1.34)

dihydropteridine reductase (NADH)
   (EC 1.5.1.34)

5,6,7,8-tetrahydropteridine:NAD(P)H+ oxidoreductase
   (EC 1.5.1.34)

SynonymsEC 1.-.-.-
FMN-dependent nitroreductase
Dihydropteridine reductase
EC 1.5.1.34
NR
EC 1.-.-.-
RefSeqNP_415110.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488865.1 (Protein)
NC_007779.1 (DNA/RNA sequence)

PfamPF00881 (Nitroreductase)
[Graphical view]
PF00881 (Nitroreductase)
[Graphical view]

KEGG pathways
MAP codePathwaysE.C.
MAP00633Trinitrotoluene degradation1.5.1.34
MAP00790Folate biosynthesis1.5.1.34

UniProtKB:Accession NumberP38489Q01234
Entry nameNFNB_ECOLINFNB_ENTCL
ActivityA 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H.
SubunitHomodimer.Homodimer.
Subcellular location

CofactorFMN.FMN.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00061C00272C00003C00006C00268C00004C00005C00080
CompoundFMN5,6,7,8-TetrahydrobiopterinNAD+NADP+6,7-DihydrobiopterinNADHNADPHH+
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamide group,amine group,aromatic ring (with nitrogen atoms),carbohydrateamide group,amine group,nucleotideamide group,amine group,nucleotideamide group,amine group,aromatic ring (with nitrogen atoms),carbohydrateamide group,amine group,nucleotideamide group,amine group,nucleotideothers
ChEBI17621
59560
15846
18009

16908
16474
15378
PubChem643976
44257
5893
5886
133246
439153
5884
1038
                
1ds7ABound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1ds7BBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1icrABound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icrBBound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icuABound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icuBBound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icuCBound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icuDBound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icvABound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icvBBound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icvCBound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1icvDBound:FMNUnboundAnalogue:NIOUnboundUnboundUnboundUnbound 
1idtABound:FMNAnalogue:CB1UnboundUnboundUnboundUnboundUnbound 
1idtBBound:FMNAnalogue:CB1UnboundUnboundUnboundUnboundUnbound 
1oo5ABound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1oo5BBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1oo6ABound:FMNAnalogue:SN2UnboundUnboundUnboundUnboundUnbound 
1oo6BBound:FMNAnalogue:SN2UnboundUnboundUnboundUnboundUnbound 
1oonABound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1oonBBound:FMNAnalogue:BELUnboundUnboundUnboundUnboundUnbound 
1ooqABound:FMNAnalogue:DTCUnboundUnboundUnboundUnboundUnbound 
1ooqBBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqbABound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqbBBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqbCBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqbDBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqcABound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqcBBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqcCBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqcDBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqdABound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqdBBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqdCBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1kqdDBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1necABound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1necBBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1necCBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 
1necDBound:FMNUnboundUnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
literature [7]
pdbCatalytic residuesMain-chain involved in catalysis
          
1ds7ALYS 14
GLU 165
1ds7BLYS 14
GLU 165
1icrALYS 14
GLU 165
1icrBLYS 14
GLU 165
1icuALYS 14
GLU 165
1icuBLYS 14
GLU 165
1icuCLYS 14
GLU 165
1icuDLYS 14
GLU 165
1icvALYS 14
GLU 165
1icvBLYS 14
GLU 165
1icvCLYS 14
GLU 165
1icvDLYS 14
GLU 165
1idtALYS 14
GLU 165
1idtBLYS 14
GLU 165
1oo5ALYS 14
GLU 165
1oo5BLYS 14
GLU 165
1oo6ALYS 14
GLU 165
1oo6BLYS 14
GLU 165
1oonALYS 14
GLU 165
1oonBLYS 14
GLU 165
1ooqALYS 14
GLU 165
1ooqBLYS 14
GLU 165
1kqbALYS 14
GLU 165
1kqbBLYS 14
GLU 165
1kqbCLYS 14
GLU 165
1kqbDLYS 14
GLU 165
1kqcALYS 14
GLU 165
1kqcBLYS 14
GLU 165
1kqcCLYS 14
GLU 165
1kqcDLYS 14
GLU 165
1kqdALYS 14
GLU 165
1kqdBLYS 14
GLU 165
1kqdCLYS 14
GLU 165
1kqdDLYS 14
GLU 165
1necALYS 13
GLU 164
1necBLYS 13
GLU 164
1necCLYS 13
GLU 164
1necDLYS 13
GLU 164

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.3627
[7]p.208-210
[11]p.4017

references
[1]
PubMed ID1999405
JournalJ Biol Chem
Year1991
Volume266
Pages4119-25
AuthorsBryant C, DeLuca M
TitlePurification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae.
[2]
PubMed ID8182754
JournalJ Mol Biol
Year1994
Volume238
Pages852-3
AuthorsSkelly JV, Collins PJ, Knox RJ, Anlezark GM, Melton RG
TitleCrystallization and preliminary crystallographic data for an FMN-dependent nitroreductase from Escherichia coli B.
[3]
PubMed ID8755909
JournalJ Bacteriol
Year1996
Volume178
Pages4731-3
AuthorsZenno S, Koike H, Tanokura M, Saigo K
TitleConversion of NfsB, a minor Escherichia coli nitroreductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, by a single amino acid substitution.
[4]
PubMed ID8947835
JournalJ Biochem (Tokyo)
Year1996
Volume120
Pages736-44
AuthorsZenno S, Koike H, Tanokura M, Saigo K
TitleGene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS)
PubMed ID11020276
JournalJ Med Chem
Year2000
Volume43
Pages3624-31
AuthorsParkinson GN, Skelly JV, Neidle S
TitleCrystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme.
Related PDB1ds7
Related UniProtKBP38489
[6]
PubMed ID11361014
JournalArch Biochem Biophys
Year2001
Volume385
Pages170-8
AuthorsNivinskas H, Koder RL, Anusevicius Z, Sarlauskas J, Miller AF, Cenas N
TitleQuantitative structure-activity relationships in two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H:nitroreductase.
[7]
PubMed ID11491290
JournalJ Mol Biol
Year2001
Volume309
Pages203-13
AuthorsLovering AL, Hyde EI, Searle PF, White SA
TitleThe structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution.
Related PDB1icr,1icu,1icv
[8]
PubMed ID12139974
JournalArch Biochem Biophys
Year2002
Volume403
Pages249-58
AuthorsNivinskas H, Staskeviciene S, Sarlauskas J, Koder RL, Miller AF, Cenas N
TitleTwo-electron reduction of quinones by Enterobacter cloacae NAD(P)H:nitroreductase: quantitative structure-activity relationships.
[9]
PubMed ID12450383
JournalBiochemistry
Year2002
Volume41
Pages14197-205
AuthorsKoder RL, Haynes CA, Rodgers ME, Rodgers DW, Miller AF
TitleFlavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases.
[10]
PubMed ID11805110
JournalJ Biol Chem
Year2002
Volume277
Pages11513-20
AuthorsHaynes CA, Koder RL, Miller AF, Rodgers DW
TitleStructures of nitroreductase in three states: effects of inhibitor binding and reduction.
Related PDB1kqb,1kqc,1kqd
[11]
PubMed ID12954054
JournalJ Med Chem
Year2003
Volume46
Pages4009-20
AuthorsJohansson E, Parkinson GN, Denny WA, Neidle S
TitleStudies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form.
Related PDB1oo5,1oo6,1oon,1ooq,1idt


createdupdated
2003-10-312009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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