ID   NUOD2_SALAI             Reviewed;         385 AA.
AC   A8M8F6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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}; OrderedLocusNames=Sare_4721;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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 a
CC       menaquinone. 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 membrane {ECO:0000255|HAMAP-Rule:MF_01358};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358};
CC       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; CP000850; ABW00475.1; -; Genomic_DNA.
DR   RefSeq; WP_012184698.1; NC_009953.1.
DR   AlphaFoldDB; A8M8F6; -.
DR   SMR; A8M8F6; -.
DR   STRING; 391037.Sare_4721; -.
DR   EnsemblBacteria; ABW00475; ABW00475; Sare_4721.
DR   GeneID; 5706023; -.
DR   KEGG; saq:Sare_4721; -.
DR   PATRIC; fig|391037.6.peg.4772; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_11; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
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; 2.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Translocase; Transport.
FT   CHAIN           1..385
FT                   /note="NADH-quinone oxidoreductase subunit D 2"
FT                   /id="PRO_0000357924"
SQ   SEQUENCE   385 AA;  42660 MW;  B0FAF800220572FF CRC64;
     MTTDAELREL TVGTGAGGEQ LGTDMVLNIG PQHPSTHGVL RLRLVLDGER VVSAEPIVGY
     MHRGAEKLFE VRDYRQIIVL ANRHDWLSAF ANELGVVLAV ERLMGMEVPE RATWLRMALA
     ELNRVLNHLM FLGSYPLEIG AITPMFYAFR ERETLQAVLE EVSGGRIHYM FNRVGGLKEE
     VPAGWTGRAR TAIGEVRRRM PDLDRLIRRN EIFLARTVGV GVLSAAQAAA FGASGPVARA
     SGLDLDLRRD EPYLAYDQLE VPVVTRTAGD CHSRFEVLLD QVYVSLDLAE QCLDQVDRLT
     GPVNTRLPKV LKAPEGHTYA WTENPLGING YYLVSRGEKT PWRLKLRTAS YANVQALATL
     LPGCLVPDLI AILGSMFFVV GDIDK