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Database: UniProt
Entry: Q8F9N0
LinkDB: Q8F9N0
Original site: Q8F9N0 
ID   NUOI_LEPIN              Reviewed;         175 AA.
AC   Q8F9N0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   10-APR-2019, entry version 103.
DE   RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01351};
DE   AltName: Full=NADH dehydrogenase I subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE   AltName: Full=NDH-1 subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
GN   Name=nuoI {ECO:0000255|HAMAP-Rule:MF_01351};
GN   OrderedLocusNames=LA_0161;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai
OS   (strain 56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA   Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA   Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA   Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA   Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA   Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA   Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira
RT   interrogans revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is
CC       believed to be ubiquinone. Couples the redox reaction to proton
CC       translocation (for every two electrons transferred, four hydrogen
CC       ions are translocated across the cytoplasmic membrane), and thus
CC       conserves the redox energy in a proton gradient.
CC       {ECO:0000255|HAMAP-Rule:MF_01351}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01351};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01351};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01351};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
CC       NuoA, H, J, K, L, M, N constitute the membrane sector of the
CC       complex. {ECO:0000255|HAMAP-Rule:MF_01351}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01351}.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01351}.
DR   EMBL; AE010300; AAN47360.1; -; Genomic_DNA.
DR   RefSeq; NP_710342.1; NC_004342.2.
DR   RefSeq; WP_000537600.1; NC_004342.2.
DR   ProteinModelPortal; Q8F9N0; -.
DR   SMR; Q8F9N0; -.
DR   EnsemblBacteria; AAN47360; AAN47360; LA_0161.
DR   GeneID; 1149504; -.
DR   GeneID; 34315653; -.
DR   KEGG; lil:LA_0161; -.
DR   PATRIC; fig|189518.3.peg.162; -.
DR   eggNOG; ENOG4107YK4; Bacteria.
DR   eggNOG; COG1143; LUCA.
DR   HOGENOM; HOG000228290; -.
DR   InParanoid; Q8F9N0; -.
DR   KO; K00338; -.
DR   OMA; LCGLCIE; -.
DR   BioCyc; LINT189518:G1GL4-143-MONOMER; -.
DR   PRO; PR:Q8F9N0; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   HAMAP; MF_01351; NDH1_NuoI; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   PANTHER; PTHR10849; PTHR10849; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   TIGRFAMs; TIGR01971; NuoI; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; NAD; Quinone;
KW   Reference proteome; Repeat; Translocase; Ubiquinone.
FT   CHAIN         1    175       NADH-quinone oxidoreductase subunit I.
FT                                /FTId=PRO_0000245715.
FT   DOMAIN       69     98       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   DOMAIN      115    144       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        78     78       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        81     81       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        84     84       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        88     88       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       124    124       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       127    127       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       130    130       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       134    134       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
SQ   SEQUENCE   175 AA;  20324 MW;  BD72C49B6E931DFE CRC64;
     MGTVNVVRVA SRHKLSWYEK FYFYSIGKGL WITLKHFIKA AILRKAVTIE FPEKKRKYST
     RFRGMHTMKR DEQGRERCTS CFCCMWICPA DAIYIEAAEV TPEIQHLHPE DKYAKKFEID
     LLRCIFCGMC EEACPKGAIY LDGPGEMATD NREDLILTKE RMMQLVGGPI IGERQ
//
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