ID   NUOCD_ALIB4             Reviewed;         544 AA.
AC   A8ERL4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01397};
DE   AltName: Full=NADH dehydrogenase I subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
DE   AltName: Full=NDH-1 subunit C/D {ECO:0000255|HAMAP-Rule:MF_01397};
GN   Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01397}; Synonyms=nuoCD, nuoD;
GN   OrderedLocusNames=Abu_0313;
OS   Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Aliarcobacter.
OX   NCBI_TaxID=367737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018;
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA   Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the Epsilonproteobacterium
RT   Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(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_01397}.
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_01397};
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoB, CD,
CC       E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01397}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01397}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01397}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01397}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01397}.
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DR   EMBL; CP000361; ABV66588.1; -; Genomic_DNA.
DR   RefSeq; WP_012012152.1; NC_009850.1.
DR   AlphaFoldDB; A8ERL4; -.
DR   SMR; A8ERL4; -.
DR   STRING; 367737.Abu_0313; -.
DR   EnsemblBacteria; ABV66588; ABV66588; Abu_0313.
DR   KEGG; abu:Abu_0313; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_7; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000001136; Chromosome.
DR   GO; GO:0030964; C:NADH dehydrogenase complex; IEA:InterPro.
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; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   Gene3D; 3.30.460.80; -; 1.
DR   HAMAP; MF_01397; NDH1_NuoCD_2; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR026662; NDH-1_subunit_CD.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Multifunctional enzyme; NAD;
KW   Quinone; Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..544
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358615"
FT   REGION          1..138
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01397"
FT   REGION          161..544
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01397"
SQ   SEQUENCE   544 AA;  61556 MW;  CBF983CB6E7BAE69 CRC64;
     MLNCDMLIDS KELKSTISKL KNEDNYTILL DVTAVDYLKF PDVTPSRFAV IYILRDSTFT
     KEITIKSYVD DNTLEIDSLY DLYESADWAE RETFDQYGIK FVGHPNLKRV LNHHQFIGHP
     LRKDYKITKG QICTETEDLM DEMVPKLKSK GYKKEEIDDL MLLNVGPSHP ASHGTIRNFV
     AMEGETITAC VTEIGYLHRG FEKACEHHTY SQIIPYTDRL NYCSAILNNI GYSKAVEEML
     GIEITPRAKM IRVIIGELSR ILDHLVCNAA NMVDLGGLTN FWYLFSPRDM AYDLLSKLTG
     ARLTNTYTRI GGLEFDLYDG FDKDLEEVLK AVEKGVEDAL SLIAHNRIYH DRTQDVGVIK
     ADFALRNGIS GPNLRAAGVA CDLRKDKPYY GYENFDFDVV IGSHGDVYDR MMCRFEEMRQ
     STKIIRQAMK NLPDGAINVY APGVILPSKK DVYGNIEGLM NQFKLTFEGI QVPKGEYYSF
     SEAANGELGF FIVSDGSGRP YKVKCRPPCF YSLAAYSKIV EGTMLADAVV TMASMNFIAG
     EFDR