ID   NUOD_CAMHC              Reviewed;         408 AA.
AC   A7HZV1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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};
GN   OrderedLocusNames=CHAB381_0184;
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
RL   Submitted (JUL-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000776; ABS52082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7HZV1; -.
DR   SMR; A7HZV1; -.
DR   STRING; 360107.CHAB381_0184; -.
DR   EnsemblBacteria; ABS52082; ABS52082; CHAB381_0184.
DR   KEGG; cha:CHAB381_0184; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_7; -.
DR   OMA; IMGTSME; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000002407; 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_0000371845"
SQ   SEQUENCE   408 AA;  46445 MW;  28FB9D2E17CD5F3F CRC64;
     MQDPNKLRPF FENVEFNREG SNMILNFGPQ HPSAHGQLKL VLEVDGEKII KARPGIGYMH
     RGVEKMAENM IYQEFVPVTD RVDYIAAGSN NYGFCATVEK LCGIDVPRRA QIIRTMLLEL
     NRIASHLLFL GTHALDIGAM TVFLYTFRER EYVLDLIEKY SGARLTHHNV KIGGMFVDLP
     DGWLDELLAF CEKFPRDIAD YEALLDTNRI WLLRTQNVGV ITKEQALSCG CSGVMLRASG
     YKWDIRKEEP YLIYDELDFD VPYAEAGDCY ARYKCYVQEM RESVKILTQC VPLYKASEPK
     ILADSPEFVS AGKEQLMSQN YSLMQHFVLI TQGLKPPEGE IYLATESPKG ELGFYIYSVG
     ESSPYRLKIR CPSFWHCAIY EEIMPGQYIA DVTAIIGSSN IILGEVDR