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Database: UniProt
Entry: Q8RQ74
LinkDB: Q8RQ74
Original site: Q8RQ74 
ID   NUOI_PSEFL              Reviewed;         182 AA.
AC   Q8RQ74;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   10-APR-2019, entry version 88.
DE   RecName: Full=NADH-quinone oxidoreductase subunit I;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit I;
DE   AltName: Full=NDH-1 subunit I;
GN   Name=nuoI;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=WCS365;
RX   PubMed=12118882; DOI=10.1094/MPMI.2002.15.7.662;
RA   Camacho-Carvajal M.M., Wijfjes A.H.M., Mulders I.H.M.,
RA   Lugtenberg B.J.J., Bloemberg G.V.;
RT   "Characterization of NADH dehydrogenases of Pseudomonas fluorescens
RT   WCS365 and their role in competitive root colonization.";
RL   Mol. Plant Microbe Interact. 15:662-671(2002).
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 (By similarity).
CC       Required for plants roots colonization. {ECO:0000250,
CC       ECO:0000269|PubMed:12118882}.
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;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits
CC       NuoA, H, J, K, L, M, N constitute the membrane sector of the
CC       complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By low oxygen growth conditions, especially in
CC       rhizosphere. {ECO:0000269|PubMed:12118882}.
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC       {ECO:0000305}.
DR   EMBL; AF281148; AAL89571.1; -; Genomic_DNA.
DR   RefSeq; WP_003180051.1; NZ_QQAQ01000007.1.
DR   ProteinModelPortal; Q8RQ74; -.
DR   SMR; Q8RQ74; -.
DR   STRING; 690597.JH730963_gene2519; -.
DR   GeneID; 11830244; -.
DR   eggNOG; ENOG4105P3U; Bacteria.
DR   eggNOG; COG1143; LUCA.
DR   OrthoDB; 1619561at2; -.
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   2: Evidence at transcript level;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; NAD; Quinone; Repeat; Translocase;
KW   Ubiquinone.
FT   CHAIN         1    182       NADH-quinone oxidoreductase subunit I.
FT                                /FTId=PRO_0000245729.
FT   DOMAIN       52     82       4Fe-4S ferredoxin-type 1.
FT   DOMAIN       92    121       4Fe-4S ferredoxin-type 2.
FT   METAL        62     62       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        65     65       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        68     68       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        72     72       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       101    101       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       104    104       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       107    107       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       111    111       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   182 AA;  20474 MW;  816D9146215C042C CRC64;
     MFKYIGDIVK GTGTQLRSLV MIFGHGFRKR DTLQYPEEPV YLAPRYRGRI VLTRDPDGEE
     RCVACNLCAV ACPVGCISLQ KAETEDGRWY PDFFRINFSR CIFCGLCEEA CPTTAIQLTP
     DFEMAEFKRQ DLVYEKEDLL ISGPGKNPDY NFYRVAGMAI AGKPKGAAQN EAEPINVKSL
     LP
//
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