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Database: UniProt
Entry: A1KNE9
LinkDB: A1KNE9
Original site: A1KNE9 
ID   NUOI_MYCBP              Reviewed;         211 AA.
AC   A1KNE9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JAN-2019, entry version 82.
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=BCG_3176;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W.,
RA   Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C.,
RA   Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A.,
RA   Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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 menaquinone. 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 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; AM408590; CAL73165.1; -; Genomic_DNA.
DR   RefSeq; WP_003416447.1; NC_008769.1.
DR   ProteinModelPortal; A1KNE9; -.
DR   SMR; A1KNE9; -.
DR   EnsemblBacteria; CAL73165; CAL73165; BCG_3176.
DR   KEGG; mbb:BCG_3176; -.
DR   HOGENOM; HOG000228290; -.
DR   KO; K00338; -.
DR   OMA; LCGLCIE; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   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 membrane; Complete proteome; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; NAD; Quinone; Repeat; Translocase.
FT   CHAIN         1    211       NADH-quinone oxidoreductase subunit I.
FT                                /FTId=PRO_0000298513.
FT   DOMAIN       71    101       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   DOMAIN      117    146       4Fe-4S ferredoxin-type 2.
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        87     87       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        91     91       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       126    126       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       129    129       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       132    132       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       136    136       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
SQ   SEQUENCE   211 AA;  23436 MW;  A538F11A52D5EB3E CRC64;
     MANTDRPALP HKRAVPPSRA DSGPRRRRTK LLDAVAGFGV TLGSMFKKTV TEEYPERPGP
     VAARYHGRHQ LNRYPDGLEK CIGCELCAWA CPADAIYVEG ADNTEEERFS PGERYGRVYQ
     INYLRCIGCG LCIEACPTRA LTMTYDYELA DDNRADLIYE KDRLLAPLLP EMAAPPHPRA
     PGATDKDYYL GNVTAEGLRG VRESQTTGDS R
//
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