NUOD_CAMJ8
ID NUOD_CAMJ8 Reviewed; 408 AA.
AC A8FNN4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=C8J_1473;
OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS 11828).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=407148;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81116 / NCTC 11828;
RX PubMed=17873037; DOI=10.1128/jb.01404-07;
RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA van Vliet A.H.M.;
RT "The complete genome sequence of Campylobacter jejuni strain 81116
RT (NCTC11828).";
RL J. Bacteriol. 189:8402-8403(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
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; CP000814; ABV53071.1; -; Genomic_DNA.
DR RefSeq; WP_002866864.1; NC_009839.1.
DR AlphaFoldDB; A8FNN4; -.
DR SMR; A8FNN4; -.
DR KEGG; cju:C8J_1473; -.
DR HOGENOM; CLU_015134_1_2_7; -.
DR OMA; IMGTSME; -.
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; Translocase;
KW Transport; Ubiquinone.
FT CHAIN 1..408
FT /note="NADH-quinone oxidoreductase subunit D"
FT /id="PRO_0000371849"
SQ SEQUENCE 408 AA; 46915 MW; 82E92D126C874CE5 CRC64;
MQIPSKLKPY YENIAFEQED SKMIINLGPQ HPSAHGNLRL ILELDGEQVV KARPCIGYMH
RGMEKMAENM IYQEFIPTTD RMDYIAASAN NYAYCAAVEK LCGLEIPRRA AVIRMILLEL
NRIASHLLWL ATHALDIGAM SVFLYCFRER EYVLDLIEKY CGARLTHSSM RIGGVMLDLP
ENYLEEMLVF CDKFPNDLKD YEDLLDDNRI WRLRTENVGV VTKEQALNWG CTGVMLRGSG
IKYDIRKEEP YLLYNEVEFG VPYATQGDSY ARYKVYMQEF RESLKILRQC ATLYKDTPPE
ILATHPEYVS ASKEQILTQN YSLMQHFVLI TQGLKPPKGE VYVPTESPKG ELGFFIHSDG
TGRPYRLKAR TPSYWHCAFF EEMLVGTYLA DVVAIMGNVN IVLGEIDR