|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
|
[2]
|
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.
|
[3]
|
EXPRESSION OF 240-324 FOR CHARACTERIZATION OF A FOURTH [4FE-4S] CENTER, AND MUTAGENESIS OF CYS-256; CYS-259; CYS-263 AND CYS-291.
DOI=10.1074/jbc.M108796200; PubMed=11704668 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamaru-Ogiso E.,
Yano T.,
Ohnishi T.,
Yagi T.;
"Characterization of the iron-sulfur cluster coordinated by a cysteine cluster motif (CXXCXXXCX27C) in the Nqo3 subunit in the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus HB-8.";
J. Biol. Chem. 277:1680-1688(2002).
|
[4]
|
PROTEIN SEQUENCE OF 1-8, 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).
|
[5]
|
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).
|
|
|
|
- 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 per subunit. The 2Fe-2S cluster 1 is referred to as N1b.
- COFACTOR: Binds 3 4Fe-4S clusters per subunit. The 4Fe-4S clusters 2, 3, and 4 are referred to as N5, N4, and N7, respectively. The 4Fe-4S cluster 4 is too far away from the main redox chain to participate in electron transfer but probably confers structural stability.
- 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 comprises two main parts, an N-terminal [FeFe]-hydrogenase-like domain (residues 1 to 240) that coordinates clusters 1, 2 and 3, and a domain similar to molybdopterin-containing enzymes (residues 241 to 767) whose first subdomain coordinates cluster 4.
- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 783 AA [This is the length of the unprocessed precursor] |
Molecular weight: 86529 Da [This is the MW of the unprocessed precursor] |
CRC64: 19A56201A20F9B82 [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MVRVKVNDRI VEVPPGTSVM DAVFHAGYDV PLFCSEKHLS PIGACRMCLV RIGLPKKGPD
70 80 90 100 110 120
GKPLLNEKGE PEIQWQPKLA ASCVTAVADG MVVDTLSDVV REAQAGMVEF TLLNHPLDCP
130 140 150 160 170 180
TCDKGGACEL QDRTVEYGLY EKYYQKGPLE LPVYTRFEFT RRHVDKHHPL SPFVILDRER
190 200 210 220 230 240
CIHCKRCVRY FEEVPGDEVL DFIERGVHTF IGTMDFGLPS GFSGNITDIC PVGALLDLTA
250 260 270 280 290 300
RFRARNWEME ETPTTCALCP VGCGITADTR SGELLRIRAR EVPEVNEIWI CDAGRFGHEW
310 320 330 340 350 360
ADQNRLKTPL VRKEGRLVEA TWEEAFLALK EGLKEARGEE VGLYLAHDAT LEEGLLASEL
370 380 390 400 410 420
AKALKTPHLD FQGRTAAPAS LFPPASLEDL LQADFALVLG DPTEEAPILH LRLSEFVRDL
430 440 450 460 470 480
KPPHRYNHGT PFADLQIKER MPRRTDKMAL FAPYRAPLMK WAAIHEVHRP GEEREILLAL
490 500 510 520 530 540
LGDKEGSEMV AKAKEAWEKA KNPVLILGAG VLQDTVAAER ARLLAERKGA KVLAMTPAAN
550 560 570 580 590 600
ARGLEAMGVL PGAKGASWDE PGALYAYYGF VPPEEALKGK RFVVMHLSHL HPLAERYAHV
610 620 630 640 650 660
VLPAPTFYEK RGHLVNLEGR VLPLSPAPIE NGEAEGALQV LALLAEALGV RPPFRLHLEA
670 680 690 700 710 720
QKALKARKVP EAMGRLSFRL KELRPKERKG AFYLRPTMWK AHQAVGKAQE AARAELWAHP
730 740 750 760 770 780
ETARAEALPE GAQVAVETPF GRVEARVVHR EDVPKGHLYL SALGPAAGLR VEGRVLVPAG
GEA
|
Q56223 in FASTA format |
|
ExPASy Home page
YPRC Korea
