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NUOD_BRUA2
ID   NUOD_BRUA2              Reviewed;         396 AA.
AC   Q2YNG0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=nuoD {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=BAB1_0825;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01358}.
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, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01358};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR   EMBL; AM040264; CAJ10781.1; -; Genomic_DNA.
DR   RefSeq; WP_002966770.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YNG0; -.
DR   SMR; Q2YNG0; -.
DR   STRING; 359391.BAB1_0825; -.
DR   EnsemblBacteria; CAJ10781; CAJ10781; BAB1_0825.
DR   GeneID; 3787517; -.
DR   KEGG; bmf:BAB1_0825; -.
DR   PATRIC; fig|359391.11.peg.3135; -.
DR   HOGENOM; CLU_015134_1_1_5; -.
DR   OMA; IMGTSME; -.
DR   PhylomeDB; Q2YNG0; -.
DR   Proteomes; UP000002719; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..396
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000357783"
SQ   SEQUENCE   396 AA;  45027 MW;  B030C5D34855971D CRC64;
     MAETQVRNFN INFGPQHPAA HGVLRLVLEL DGEVVERVDP HIGLLHRGTE KLMEAKTYLQ
     AVPYLDRLDY VAPMNQEHAY ALAVERLLDI EVPKRGQLIR VLYSEIGRIL NHLLNVTTQA
     MDVGALTPPL WGFEEREKLM VFYERACGAR MHAAYFRPGG VHQDLPDQLI EDIGKWIDPF
     FTTLKNLDDL ITPNRIFKQR NVDIGVVKLE DAWAWGFSGV MVRGSGAAWD LRKSQPYECY
     SEMEFDIPVG KNGDCYDRYL IRMEEMRQSA RIMRQCVDLL LGKERVGPVS NTDHKIVPPK
     RGEMKRSMEA LIHHFKLYTE GYHVPAGEVY AAVEAPKGEF GVYLVSDGSN KPYRFKLRAP
     GFAHLQAMDF LCRGHMLADV SAILGSLDIV FGEVDR
 
 
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