ID   NUOD2_CHLAA             Reviewed;         411 AA.
AC   A9WFB4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Caur_2899;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
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 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; CP000909; ABY36098.1; -; Genomic_DNA.
DR   RefSeq; WP_012258751.1; NC_010175.1.
DR   RefSeq; YP_001636487.1; NC_010175.1.
DR   AlphaFoldDB; A9WFB4; -.
DR   SMR; A9WFB4; -.
DR   STRING; 324602.Caur_2899; -.
DR   EnsemblBacteria; ABY36098; ABY36098; Caur_2899.
DR   KEGG; cau:Caur_2899; -.
DR   PATRIC; fig|324602.8.peg.3265; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_0; -.
DR   InParanoid; A9WFB4; -.
DR   OMA; RDSHTIW; -.
DR   Proteomes; UP000002008; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
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 membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..411
FT                   /note="NADH-quinone oxidoreductase subunit D 2"
FT                   /id="PRO_0000357799"
SQ   SEQUENCE   411 AA;  45712 MW;  E988F1E30DC9FDCD CRC64;
     MTEPITVPTP QQIIEPAVAG RTETMVLNMG PHHPSTHGVL RLVLELDGEV VVNVAPDVGY
     LHTGIEKTME SKTYQKAVVL TDRMDYLAPL SNNLCYALAV EKLLDVEIPE RAQIARVLLT
     ELQRISSHLV WLGTHALDLA AMSVFLYAFR EREQILDIFE LVSGARMMTS YFRIGGLAYD
     LPSDFIPTVE QFLAVMPSRI DEYEDLLTAN PLWLERTVGV GVIDAQSAIA LGLTGANLRA
     TGVAYDVRKA MPYSGYETYS FEIPVGKNGD IYDRYRVRIA EMRQSVKIVQ QATERLRELG
     PGPVVTSNRK VAPPPKREIT ESMESLIHHF KLWTEGFKPP RGDAYVSIES PRGILGCYVV
     SDGSPKPWRV HFRAPSFINL QSLAHMAKGR MVADLVALIA SLDPVLGEVD R