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Database: UniProt
Entry: A1K5B6
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ID   NUOI_AZOSB              Reviewed;         161 AA.
AC   A1K5B6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JAN-2019, entry version 79.
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=azo1404;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Azoarcus.
OX   NCBI_TaxID=62928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte
RT   Azoarcus sp. strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL94021.1; -; Genomic_DNA.
DR   RefSeq; WP_011765137.1; NC_008702.1.
DR   ProteinModelPortal; A1K5B6; -.
DR   SMR; A1K5B6; -.
DR   STRING; 62928.azo1404; -.
DR   EnsemblBacteria; CAL94021; CAL94021; azo1404.
DR   KEGG; azo:azo1404; -.
DR   eggNOG; ENOG4105P3U; Bacteria.
DR   eggNOG; COG1143; LUCA.
DR   HOGENOM; HOG000228289; -.
DR   KO; K00338; -.
DR   OMA; LCGLCIE; -.
DR   OrthoDB; 1619561at2; -.
DR   BioCyc; ASP62928:AZO_RS07105-MONOMER; -.
DR   Proteomes; UP000002588; 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    161       NADH-quinone oxidoreductase subunit I.
FT                                /FTId=PRO_0000298480.
FT   DOMAIN       52     82       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   DOMAIN       92    121       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        62     62       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        65     65       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        68     68       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL        72     72       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       101    101       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       104    104       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       107    107       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
FT   METAL       111    111       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01351}.
SQ   SEQUENCE   161 AA;  18508 MW;  018EF7317CF83BA1 CRC64;
     MGAKDYIGSL FLKELVKGMA LTGRHFFARK ITVQFPEEKT PQSARFRGLH ALRRYPNGEE
     RCIACKLCEA ICPAMAITIE SEQREDGSRR TSRYDIDLTK CIFCGFCEEA CPVDAVVETR
     VFEYHGEQRG DLYYTKQMLL AVGDRHEQQI AADREQEAKF R
//
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