ID   NUOD2_RHIEC             Reviewed;         404 AA.
AC   Q2K3U2;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D 2 {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=nuoD2 {ECO:0000255|HAMAP-Rule:MF_01358};
GN   OrderedLocusNames=RHE_CH03739;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC92494.1; -; Genomic_DNA.
DR   RefSeq; WP_011426946.1; NC_007761.1.
DR   AlphaFoldDB; Q2K3U2; -.
DR   SMR; Q2K3U2; -.
DR   STRING; 347834.RHE_CH03739; -.
DR   EnsemblBacteria; ABC92494; ABC92494; RHE_CH03739.
DR   KEGG; ret:RHE_CH03739; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_5; -.
DR   OMA; GGRMHYM; -.
DR   Proteomes; UP000001936; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..404
FT                   /note="NADH-quinone oxidoreductase subunit D 2"
FT                   /id="PRO_0000357893"
SQ   SEQUENCE   404 AA;  45831 MW;  3A0A356C9C305226 CRC64;
     MTEVTELSRP EGEALNTREV LLNLGPQHPS THGVLRLVLE LDGEFVERVD PHIGYLHRGT
     EKLAESFTYT QIFPLTDRLD YLCPPSNNLA FALAVEKLLG IEAPIRAQYI RVMMAELARI
     SGHLLITGAL PMDLGAMTAL LYVMREREMI MDLLEMITGA RMHTSFCRVG GVREDLPDGF
     FPKIREFCDI FPNRIRDYER LLEDNRVFLN RTKGIGVISA EDAVDLGLSG PNLRASGVDW
     DIRRDEPYEI YDRLDFNVIT RDEGDCYARW RCRVDEMRES MRIIEQCIDQ MPEGPFQIDM
     PTIAFPLDKD RVHCSMEALI QHFDLSAYGF KVPKGEVYSA IEAPKGELGF YIISDGSPKP
     FRMKVRAPSF VNLQALFGVT NARYLADMIA VLGSLDPVMA EVDK