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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
DOI=10.1074/jbc.272.7.4201; PubMed=9020134 [NCBI, ExPASy, EBI, Israel, Japan]
Yano T.,
Chu S.S.,
Sled' V.D.,
Ohnishi T.,
Yagi T.;
"The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQO2 subunit.";
J. Biol. Chem. 272:4201-4211(1997).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Masui R.,
Kurokawa K.,
Nakagawa N.,
Tokunaga F.,
Koyama Y.,
Shibata T.,
Oshima T.,
Yokoyama S.,
Yasunaga T.,
Kuramitsu S.;
"Complete genome sequence of Thermus thermophilus HB8.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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[3]
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PROTEIN SEQUENCE OF 2-9, IDENTIFICATION BY MASS SPECTROMETRY, EPR SPECTROSCOPY, AND SUBUNIT.
DOI=10.1021/bi0600998; PubMed=16584177 [NCBI, ExPASy, EBI, Israel, Japan]
Hinchliffe P.,
Carroll J.,
Sazanov L.A.;
"Identification of a novel subunit of respiratory complex I from Thermus thermophilus.";
Biochemistry 45:4413-4420(2006).
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[4]
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X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), SUBUNIT, AND ELECTRON TRANSFER MECHANISM.
DOI=10.1126/science.1123809; PubMed=16469879 [NCBI, ExPASy, EBI, Israel, Japan]
Sazanov L.A.,
Hinchliffe P.;
"Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.";
Science 311:1430-1436(2006).
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- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.
- CATALYTIC ACTIVITY: NADH + quinone = NAD+ + quinol.
- COFACTOR: Binds 1 2Fe-2S cluster. This 2Fe-2S cluster is referred to as N1a.
- SUBUNIT: NDH-1 is composed of 15 different subunits, nqo1 to nqo15. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8 and nqo10 to nqo14) embedded in the membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9 and nqo15) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers.
- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
- DOMAIN: The subunit can be divided into two domains: an N-terminal four-helical bundle (residues 2 to 74) involved in interactions with subunits nqo1 and nqo3, and a thioredoxin-like C-terminal domain (residues 75 to 180) that coordinates the binuclear cluster N1a.
- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 181 AA [This is the length of the unprocessed precursor] |
Molecular weight: 20286 Da [This is the MW of the unprocessed precursor] |
CRC64: 484FE09245C613EE [This is a checksum on the sequence] |
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10 20 30 40 50 60
MGFFDDKQDF LEETFAKYPP EGRRAAIMPL LRRVQQEEGW IRPERIEEIA RLVGTTPTEV
70 80 90 100 110 120
MGVASFYSYY QFVPTGKYHL QVCATLSCKL AGAEELWDYL TETLGIGPGE VTPDGLFSVQ
130 140 150 160 170 180
KVECLGSCHT APVIQVNDEP YVECVTRARL EALLAGLRAG KRLEEIELPG KCGHHVHEVE
V
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Q56221 in FASTA format |
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