DB code: S00388

CATH domain 3.40.109.10 : NADH Oxidase Catalytic domain
E.C. 1.5.1.34 1.-.-.-
CSA
M-CSA
MACiE M0211

CATH domain Related DB codes (homologues)
3.40.109.10 : NADH Oxidase S00385 S00386 S00387

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P38489 Oxygen-insensitive NAD(P)H nitroreductase
EC 1.-.-.-
FMN-dependent nitroreductase
Dihydropteridine reductase
EC 1.5.1.34
NP_415110.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488865.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00881 (Nitroreductase)
[Graphical View]
Q01234 Oxygen-insensitive NAD(P)H nitroreductase
NR
EC 1.-.-.-
PF00881 (Nitroreductase)
[Graphical View]

KEGG enzyme name
6,7-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 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P38489 NFNB_ECOLI A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H. Homodimer. FMN.
Q01234 NFNB_ENTCL Homodimer. FMN.

KEGG Pathways
Map code Pathways E.C.
MAP00633 Trinitrotoluene degradation 1.5.1.34
MAP00790 Folate biosynthesis 1.5.1.34

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00061 C00272 C00003 C00006 C00268 C00004 C00005 C00080
E.C.
Compound FMN 5,6,7,8-Tetrahydrobiopterin NAD+ NADP+ 6,7-Dihydrobiopterin NADH NADPH H+
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion amide group,amine group,aromatic ring (with nitrogen atoms),carbohydrate amide group,amine group,nucleotide amide group,amine group,nucleotide amide group,amine group,aromatic ring (with nitrogen atoms),carbohydrate amide group,amine group,nucleotide amide group,amine group,nucleotide others
ChEBI 17621
 17621
 		59560
 59560
 		15846
 15846
 		18009
 18009
 		16908
 16908
 		16474
 16474
 		15378
 15378
PubChem 643976
 643976
 		44257
 44257
 		5893
 5893
 		5886
 5886
 		133246
 133246
 		439153
 439153
 		5884
 5884
 		1038
 1038
1ds7A Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1ds7B Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1icrA Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icrB Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icuA Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icuB Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icuC Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icuD Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icvA Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icvB Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icvC Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1icvD Bound:FMN Unbound Analogue:NIO Unbound Unbound Unbound Unbound
1idtA Bound:FMN Analogue:CB1 Unbound Unbound Unbound Unbound Unbound
1idtB Bound:FMN Analogue:CB1 Unbound Unbound Unbound Unbound Unbound
1oo5A Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1oo5B Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1oo6A Bound:FMN Analogue:SN2 Unbound Unbound Unbound Unbound Unbound
1oo6B Bound:FMN Analogue:SN2 Unbound Unbound Unbound Unbound Unbound
1oonA Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1oonB Bound:FMN Analogue:BEL Unbound Unbound Unbound Unbound Unbound
1ooqA Bound:FMN Analogue:DTC Unbound Unbound Unbound Unbound Unbound
1ooqB Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqbA Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqbB Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqbC Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqbD Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqcA Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqcB Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqcC Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqcD Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqdA Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqdB Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqdC Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1kqdD Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1necA Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1necB Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1necC Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound
1necD Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [7]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ds7A LYS 14 GLU 165
1ds7B LYS 14 GLU 165
1icrA LYS 14 GLU 165
1icrB LYS 14 GLU 165
1icuA LYS 14 GLU 165
1icuB LYS 14 GLU 165
1icuC LYS 14 GLU 165
1icuD LYS 14 GLU 165
1icvA LYS 14 GLU 165
1icvB LYS 14 GLU 165
1icvC LYS 14 GLU 165
1icvD LYS 14 GLU 165
1idtA LYS 14 GLU 165
1idtB LYS 14 GLU 165
1oo5A LYS 14 GLU 165
1oo5B LYS 14 GLU 165
1oo6A LYS 14 GLU 165
1oo6B LYS 14 GLU 165
1oonA LYS 14 GLU 165
1oonB LYS 14 GLU 165
1ooqA LYS 14 GLU 165
1ooqB LYS 14 GLU 165
1kqbA LYS 14 GLU 165
1kqbB LYS 14 GLU 165
1kqbC LYS 14 GLU 165
1kqbD LYS 14 GLU 165
1kqcA LYS 14 GLU 165
1kqcB LYS 14 GLU 165
1kqcC LYS 14 GLU 165
1kqcD LYS 14 GLU 165
1kqdA LYS 14 GLU 165
1kqdB LYS 14 GLU 165
1kqdC LYS 14 GLU 165
1kqdD LYS 14 GLU 165
1necA LYS 13 GLU 164
1necB LYS 13 GLU 164
1necC LYS 13 GLU 164
1necD LYS 13 GLU 164

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[5]
p.3627
[7]
p.208-210
[11]
p.4017

References
[1]
Resource
Comments
Medline ID
PubMed ID 1999405
Journal J Biol Chem
Year 1991
Volume 266
Pages 4119-25
Authors Bryant C, DeLuca M
Title Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8182754
Journal J Mol Biol
Year 1994
Volume 238
Pages 852-3
Authors Skelly JV, Collins PJ, Knox RJ, Anlezark GM, Melton RG
Title Crystallization and preliminary crystallographic data for an FMN-dependent nitroreductase from Escherichia coli B.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8755909
Journal J Bacteriol
Year 1996
Volume 178
Pages 4731-3
Authors Zenno S, Koike H, Tanokura M, Saigo K
Title Conversion 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.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8947835
Journal J Biochem (Tokyo)
Year 1996
Volume 120
Pages 736-44
Authors Zenno S, Koike H, Tanokura M, Saigo K
Title Gene 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.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS)
Medline ID
PubMed ID 11020276
Journal J Med Chem
Year 2000
Volume 43
Pages 3624-31
Authors Parkinson GN, Skelly JV, Neidle S
Title Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme.
Related PDB 1ds7
Related UniProtKB P38489
[6]
Resource
Comments
Medline ID
PubMed ID 11361014
Journal Arch Biochem Biophys
Year 2001
Volume 385
Pages 170-8
Authors Nivinskas H, Koder RL, Anusevicius Z, Sarlauskas J, Miller AF, Cenas N
Title Quantitative structure-activity relationships in two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H:nitroreductase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11491290
Journal J Mol Biol
Year 2001
Volume 309
Pages 203-13
Authors Lovering AL, Hyde EI, Searle PF, White SA
Title The 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 PDB 1icr 1icu 1icv
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12139974
Journal Arch Biochem Biophys
Year 2002
Volume 403
Pages 249-58
Authors Nivinskas H, Staskeviciene S, Sarlauskas J, Koder RL, Miller AF, Cenas N
Title Two-electron reduction of quinones by Enterobacter cloacae NAD(P)H:nitroreductase: quantitative structure-activity relationships.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 12450383
Journal Biochemistry
Year 2002
Volume 41
Pages 14197-205
Authors Koder RL, Haynes CA, Rodgers ME, Rodgers DW, Miller AF
Title Flavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11805110
Journal J Biol Chem
Year 2002
Volume 277
Pages 11513-20
Authors Haynes CA, Koder RL, Miller AF, Rodgers DW
Title Structures of nitroreductase in three states: effects of inhibitor binding and reduction.
Related PDB 1kqb 1kqc 1kqd
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 12954054
Journal J Med Chem
Year 2003
Volume 46
Pages 4009-20
Authors Johansson E, Parkinson GN, Denny WA, Neidle S
Title Studies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form.
Related PDB 1oo5 1oo6 1oon 1ooq 1idt
Related UniProtKB

Comments

Created Updated
2003-10-31 2009-02-26