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Database: UniProt
Entry: A1AVS0
LinkDB: A1AVS0
Original site: A1AVS0 
ID   NUOI_RUTMC              Reviewed;         163 AA.
AC   A1AVS0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JAN-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=Rmag_0245;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria;
OC   sulfur-oxidizing symbionts; Candidatus Ruthia.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A.,
RA   Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(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 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; CP000488; ABL02027.1; -; Genomic_DNA.
DR   RefSeq; WP_011737652.1; NC_008610.1.
DR   ProteinModelPortal; A1AVS0; -.
DR   SMR; A1AVS0; -.
DR   STRING; 413404.Rmag_0245; -.
DR   PRIDE; A1AVS0; -.
DR   EnsemblBacteria; ABL02027; ABL02027; Rmag_0245.
DR   KEGG; rma:Rmag_0245; -.
DR   eggNOG; ENOG4105P3U; Bacteria.
DR   eggNOG; COG1143; LUCA.
DR   HOGENOM; HOG000228289; -.
DR   KO; K00338; -.
DR   OMA; LCGLCIE; -.
DR   OrthoDB; 1619561at2; -.
DR   BioCyc; CRUT413404:G1G7M-255-MONOMER; -.
DR   Proteomes; UP000002587; 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 inner membrane; Cell membrane; Complete proteome; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; NAD; Quinone;
KW   Reference proteome; Repeat; Translocase; Ubiquinone.
FT   CHAIN         1    163       NADH-quinone oxidoreductase subunit I.
FT                                /FTId=PRO_0000298546.
FT   DOMAIN       54     84       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   DOMAIN       94    123       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        64     64       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        67     67       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        70     70       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        74     74       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       103    103       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       106    106       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       109    109       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       113    113       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
SQ   SEQUENCE   163 AA;  18677 MW;  4CF83A55527F6EF8 CRC64;
     MIKKLSKLVK DFTLSELRTG MKITAKELVN KKITVQFPEE RTPISPRFRG LHALRRYPNG
     EERCIACKLC EAVCPANAIT IESEMRDDGT RRTIVYDIDL FKCIFCGFCE EACPVDAIVE
     TQIFDYAFKS RQGSIMTKER LLEVGSQNEQ AINQARLEDA KYK
//
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