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Database: UniProt
Entry: A1UD96
LinkDB: A1UD96
Original site: A1UD96 
ID   NUOI_MYCSK              Reviewed;         174 AA.
AC   A1UD96;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   10-APR-2019, entry version 81.
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=Mkms_1596;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Miller C.D., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL90804.1; -; Genomic_DNA.
DR   RefSeq; WP_011558979.1; NC_008705.1.
DR   SMR; A1UD96; -.
DR   EnsemblBacteria; ABL90804; ABL90804; Mkms_1596.
DR   GeneID; 32420800; -.
DR   KEGG; mkm:Mkms_1596; -.
DR   HOGENOM; HOG000228290; -.
DR   KO; K00338; -.
DR   OMA; LCGLCIE; -.
DR   OrthoDB; 1619561at2; -.
DR   Proteomes; UP000000638; 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; Reference proteome; Repeat; Translocase.
FT   CHAIN         1    174       NADH-quinone oxidoreductase subunit I.
FT                                /FTId=PRO_0000298516.
FT   DOMAIN       44     74       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   DOMAIN       90    119       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        54     54       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        57     57       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        60     60       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        64     64       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        99     99       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       102    102       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       105    105       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       109    109       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
SQ   SEQUENCE   174 AA;  19365 MW;  025CC87DC8B1B4E7 CRC64;
     MPKLWDAVAG FAVTFGTLFK KPITEEYPEK PGPVAPRYHG RHQLNRYPDG LEKCIGCELC
     AWACPADAIY VEGDDNTADE RYSPGERYGR VYQINYLRCI GCGLCIEACP TRALTMTNDY
     EMADDNRADL IWGKDKLLAP LQDGMLAPPH PMAPGATDDD YYLGRIGPAT EDVR
//
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