EC number:7.1.1.2

Enzyme

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EC Tree
     7. Translocases
        7.1 Catalysing the translocation of hydrons
            7.1.1 Linked to oxidoreductase reactions
ID:7.1.1.2
Description:NADH:ubiquinone reductase (H(+)-translocating).
Alternative Name: Ubiquinone reductase.
Reduced nicotinamide adenine dinucleotide-coenzyme Q reductase.
NADH-ubiquinone reductase.
NADH-ubiquinone oxidoreductase.
NADH-CoQ reductase.
NADH-CoQ oxidoreductase.
NADH-coenzyme Q reductase.
NADH dehydrogenase (ubiquinone).
NADH coenzyme Q1 reductase.
Mitochondrial electron transport complex I.
Mitochondrial electron transport complex 1.
Electron transfer complex I.
DPNH-ubiquinone reductase.
DPNH-coenzyme Q reductase.
Dihydronicotinamide adenine dinucleotide-coenzyme Q reductase.
Complex I (mitochondrial electron transport).
Complex I (electron transport chain).
Coenzyme Q reductase.
Prosite: PDOC00858; PDOC00843; PDOC00570; PDOC00555; PDOC00554; PDOC00521; PDOC00468;
PDB:
PDBScop
5XTC 8090229; 8090230; 8054180; 8054181; 8054182; 8054177; 8054178; 8054179; 8054174; 8054175; 8054176;
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;
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3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 7.1.1.2
BRENDA Enzyme Link: BRENDA 7.1.1.2
KEGG Enzyme Link: KEGG7.1.1.2
BioCyc Enzyme Link: BioCyc 7.1.1.2
ExPASy Enzyme Link: ExPASy7.1.1.2
EC2PDB Enzyme Link: EC2PDB 7.1.1.2
ExplorEnz Enzyme Link: ExplorEnz 7.1.1.2
PRIAM enzyme-specific profiles Link: PRIAM 7.1.1.2
IntEnz Enzyme Link: IntEnz 7.1.1.2
MEDLINE Enzyme Link: MEDLINE 7.1.1.2

EC number:7.1.1.2

MSA:

7.1.1.2;
Phylogenetic Tree:

7.1.1.2;
Uniprot:
M-CSA:
RHEA:29091 a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
RULE(radius=1) [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[*:13]-[N;H0;+0:14]1-[CH;+0:15]=[C;H0;+0:16](-[*:17])-[CH2;+0:18]-[CH;+0:19]=[CH;+0:20]-1.[H+;H0:21]>>[*:1]-[c;H0;+0:2]1:[c;H0;+0:11](-[OH;+0:12]):[c;H0;+0:9](-[*:10]):[c;H0;+0:7](-[*:8]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:3]:1-[*:4].[*:13]-[n+;H0:14]1:[cH;+0:15]:[c;H0;+0:16](-[*:17]):[cH;+0:18]:[cH;+0:19]:[cH;+0:20]:1
Reaction
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References

TitleAuthorsDatePubMed ID
The architecture of respiratory complex I.Efremov RG, Baradaran R, Sazanov LA2010 May 2720505720
Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain.Sazanov LA2007 Mar 617274631
Complex I of Rhodobacter capsulatus and its role in reverted electron transport.Herter SM, Kortlüke CM, Drews G1998 Feb9446680
Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications.Wikström M, Hummer G2012 Mar 2022392981
Functional modules and structural basis of conformational coupling in mitochondrial complex I.Hunte C, Zickermann V, Brandt U2010 Jul 2320595580