Enzyme

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     1. Oxidoreductases
        1.7 Acting on other nitrogenous compounds as donors
            1.7.5 With a quinone or similar compound as acceptor
ID:1.7.5.1
Description:Nitrate reductase (quinone).
Alternative Name: Quinol/nitrate oxidoreductase.
Quinol-nitrate oxidoreductase.
Nitrate reductase Z.
Nitrate reductase A.
Dissimilatory nitrate reductase.
Prosite: PDOC00392;
PDB:
PDBScop
6G72 8085720; 8085721;
6G2J 8085720; 8085721;
5XTD 8054174; 8054175; 8054176; 8054177; 8054178; 8054179; 8054180; 8054181; 8054182; 8019958; 8032338; 8090229; 8090230; 8085728; 8085729; 8053973; 8053979;
5XTB 8053973; 8053979; 8085728; 8085729; 8019958; 8032338;
5O31 8051763; 8053972; 8053978; 8091045; 8047666; 8048046; 8048259; 8047488; 8054147; 8051655; 8090228; 8047668; 8048502; 8054157; 8047671; 8048245; 8054161; 8047844; 8053516; 8085722; 8085723; 8047738; 8053511;
 » show all

Cath: 3.40.50.740; 2.40.40.20; 3.40.228.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.7.5.1
BRENDA Enzyme Link: BRENDA 1.7.5.1
KEGG Enzyme Link: KEGG1.7.5.1
BioCyc Enzyme Link: BioCyc 1.7.5.1
ExPASy Enzyme Link: ExPASy1.7.5.1
EC2PDB Enzyme Link: EC2PDB 1.7.5.1
ExplorEnz Enzyme Link: ExplorEnz 1.7.5.1
PRIAM enzyme-specific profiles Link: PRIAM 1.7.5.1
IntEnz Enzyme Link: IntEnz 1.7.5.1
MEDLINE Enzyme Link: MEDLINE 1.7.5.1
MSA:

1.7.5.1;

Phylogenetic Tree:

1.7.5.1;

Uniprot:
M-CSA:
RHEA:56144 a quinol + nitrate = a quinone + H2O + nitrite
RULE(radius=1) [*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[OH;+0:4]):[c;H0;+0:5](-[*:6]):[c;H0;+0:7](-[*:8]):[c;H0;+0:9](-[OH;+0:10]):[c;H0;+0:11]:1-[*:12].[*:13]=[N+;H0:14](-[*:15])-[OH;+0:16]>>[*:1]-[C;H0;+0:2]1=[C;H0;+0:11](-[*:12])-[C;H0;+0:9](=[O;H0;+0:10])-[C;H0;+0:7](-[*:8])=[C;H0;+0:5](-[*:6])-[C;H0;+0:3]-1=[O;H0;+0:4].[*:13]=[N;H0;+0:14]-[*:15].[OH2;+0:16]
Reaction
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References

TitleAuthorsDatePubMed ID
Nitrate reductases in Escherichia coli.Bonnefoy V, Demoss JA19947747940
The role of a novel cytochrome b-containing nitrate reductase and quinone in the in vitro reconstruction of formate-nitrate reductase activity of E. coli.Enoch HG, Lester RL1974 Dec 234616697
Purification and further characterization of the second nitrate reductase of Escherichia coli K12.Iobbi-Nivol C, Santini CL, Blasco F, Giordano G1990 Mar 302139607
High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD.Lanciano P, Magalon A, Bertrand P, Guigliarelli B, Grimaldi S2007 May 817439244
Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A.Bertero MG, Rothery RA, Boroumand N, Palak M, Blasco F, Ginet N, Weiner JH, Strynadka NC2005 Apr 1515615728
EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism.Guigliarelli B, Asso M, More C, Augier V, Blasco F, Pommier J, Giordano G, Bertrand P1992 Jul 11321049
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A.Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC2003 Sep12910261