ID   NUOD2_SALTO             Reviewed;         388 AA.
AC   A4XCQ7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Strop_4286;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP56714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4XCQ7; -.
DR   SMR; A4XCQ7; -.
DR   STRING; 369723.Strop_4286; -.
DR   EnsemblBacteria; ABP56714; ABP56714; Strop_4286.
DR   KEGG; stp:Strop_4286; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_11; -.
DR   OMA; GGRMHYM; -.
DR   Proteomes; UP000000235; 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; 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; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           1..388
FT                   /note="NADH-quinone oxidoreductase subunit D 2"
FT                   /id="PRO_0000357926"
SQ   SEQUENCE   388 AA;  42776 MW;  2B1E8E8EFBEC6675 CRC64;
     MTGMTTDADL RELTVGTGAG GEQLGTDMVL NIGPQHPSTH GVLRLRLVLD GERVVSAEPV
     VGYMHRGAEK LFEVRDYRQI IVLANRHDWL SAFANELGVV LAVERLLGME VPERATWLRM
     ALAELNRVLN HLMFLGSYPL EIGAITPMFY AFRERETLQT ALEEVSGGRI HYMFNRVGGL
     KEEVPAGWTG RARAAIGEVR RSLPDLDNLI RRNEIFLART VGVGVLSAAQ AAAYGASGPV
     ARASGLDLDL RRDEPYLAYD QLDVPVVTRT AGDCHSRFEV LLDQVYVSLD LAEQCLDRVD
     RLTGPINTRL PKVLKAPEGH TYAWTENPLG INGYYLVSRG EKTPWRLKLR TASYANVQAL
     ATLLPGCLVP DLVAILGSMF FVVGDIDK