ID   NUOD_CAMJE              Reviewed;         408 AA.
AC   Q9PM99; Q0P852;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=Cj1576c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35673.1; -; Genomic_DNA.
DR   PIR; F81252; F81252.
DR   RefSeq; WP_002864417.1; NC_002163.1.
DR   RefSeq; YP_002344945.1; NC_002163.1.
DR   AlphaFoldDB; Q9PM99; -.
DR   SMR; Q9PM99; -.
DR   IntAct; Q9PM99; 10.
DR   STRING; 192222.Cj1576c; -.
DR   TCDB; 3.D.1.7.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR   PaxDb; Q9PM99; -.
DR   PRIDE; Q9PM99; -.
DR   EnsemblBacteria; CAL35673; CAL35673; Cj1576c.
DR   GeneID; 905846; -.
DR   KEGG; cje:Cj1576c; -.
DR   PATRIC; fig|192222.6.peg.1552; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_7; -.
DR   OMA; IMGTSME; -.
DR   Proteomes; UP000000799; 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..408
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /id="PRO_0000118618"
SQ   SEQUENCE   408 AA;  46937 MW;  153B593DD39C4908 CRC64;
     MQIPSKLKPY YENIAFEQED SKMIINLGPQ HPSAHGNLRL ILELDGEQVV KARPCIGYMH
     RGMEKMAENM IYQEFIPTTD RMDYIAASAN NYAYCAAVEK LCGLEIPRRA AVIRMILLEL
     NRITSHLLWL ATHALDIGAM SVFLYCFRER EYVLDLIEKY CGARLTHSSM RIGGVMLDLP
     ENYLEEMLAF CDKFPNDLKD YEDLLDDNRI WRLRTENVGV VTKEQALNWG CTGVMLRGSG
     IKYDIRKEEP YLLYNEVEFG VPYATQGDSY ARYKVYMQEF RESLKILRQC AMLYKDTSPE
     ILATHPEYVS ASKEQILTQN YSLMQHFVLI TQGLKPPKGE VYVPTESPKG ELGFFIHSDG
     TGRPYRLKAR TPSYWHCAFF EEMLVGTYLA DVVAIMGNVN IVLGEIDR