NUOD_CAUSK
ID NUOD_CAUSK Reviewed; 416 AA.
AC B0SZ49;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=Caul_2833;
OS Caulobacter sp. (strain K31).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX NCBI_TaxID=366602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31;
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., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) 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
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; CP000927; ABZ71960.1; -; Genomic_DNA.
DR RefSeq; WP_012286862.1; NC_010338.1.
DR AlphaFoldDB; B0SZ49; -.
DR SMR; B0SZ49; -.
DR STRING; 366602.Caul_2833; -.
DR PRIDE; B0SZ49; -.
DR EnsemblBacteria; ABZ71960; ABZ71960; Caul_2833.
DR KEGG; cak:Caul_2833; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_1_5; -.
DR OMA; IMGTSME; -.
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; 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; Translocase;
KW Transport; Ubiquinone.
FT CHAIN 1..416
FT /note="NADH-quinone oxidoreductase subunit D"
FT /id="PRO_0000357792"
SQ SEQUENCE 416 AA; 46903 MW; 7C41049CAD76F918 CRC64;
MTGSNSPAAA TDFFHDAPSL PAVPETPVRK FNINFGPQHP AAHGVLRLVL ELDGEIVERV
DPHIGLLHRG TEKLMEARTY LQNIPYFDRL DYVAPMNQEH AFCLAIEKLL GVDVPLRGSL
IRVLFCEIGR VLNHLLNVTT QAMDVGALTP PLWGFEEREK LMVFYERACG ARLHANYFRP
GGVHQDLTPS LIDDIEKWAK AFPKICDDIE GLITDNRIFK QRNVDIGVVT KEDALAWGFS
GVMVRGSGIA WDLRRNQPYE CYNDFEFDIP LGKNGDCYDR YLCRMQEMRE STKIILQAIE
KLRATPGPVM TQDNKVAPPR RAEMKRSMEA LIHHFKLYTE GFRTPEGEVY ACVEAPKGEF
GVFLVSNGTN KPYRCKIKAP GFSHLAAMDW MNRGHQLADV SAILGSLDIV FGEVDR