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NUOCD_SALG2
ID   NUOCD_SALG2             Reviewed;         596 AA.
AC   B5RCF1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C/D {ECO:0000255|HAMAP-Rule:MF_01359};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01359};
DE   AltName: Full=NADH dehydrogenase I subunit C/D {ECO:0000255|HAMAP-Rule:MF_01359};
DE   AltName: Full=NDH-1 subunit C/D {ECO:0000255|HAMAP-Rule:MF_01359};
GN   Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01359};
GN   Synonyms=nuoCD {ECO:0000255|HAMAP-Rule:MF_01359},
GN   nuoD {ECO:0000255|HAMAP-Rule:MF_01359}; OrderedLocusNames=SG2355;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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_01359}.
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_01359};
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_01359}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01359}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01359}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01359}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01359}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_01359}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAR38185.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM933173; CAR38185.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B5RCF1; -.
DR   SMR; B5RCF1; -.
DR   EnsemblBacteria; CAR38185; CAR38185; SG2355.
DR   KEGG; seg:SG2355; -.
DR   HOGENOM; CLU_015134_3_2_6; -.
DR   OMA; GGRMHYM; -.
DR   Proteomes; UP000008321; 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   GO; GO:0022904; P:respiratory electron transport chain; IEA:UniProt.
DR   Gene3D; 1.10.645.10; -; 1.
DR   Gene3D; 3.30.460.80; -; 1.
DR   HAMAP; MF_01359; NDH1_NuoCD_1; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR010218; NADH_DH_suC.
DR   InterPro; IPR023062; NADH_DH_suCD.
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; 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; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Multifunctional enzyme; NAD;
KW   Quinone; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..596
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358685"
FT   REGION          1..186
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
FT   REGION          210..596
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
SQ   SEQUENCE   596 AA;  68402 MW;  362B1FBD9A864F46 CRC64;
     MTDLTAQDAA WSTRDHLDDP VIGELRNRFG PDAFTVQATR TGIPVVWVKR EQLLEVGDFL
     KKLPKPYVML FDLHGMDERL RTHRDGLPAA DFSVFYHLIS IERNRDIMLK VALSENDLRV
     PTFTKLFPNA NWYERETWEM FGIDIEGHPH LTRIMMPQTW EGHPLRKDYP ARATEFDPFE
     LTKAKQDLEM EALTFKPEDW GMKRGTDNED FMFLNLGPNH PSAHGAFRII LQLDGEEIVD
     CVPDIGYHHR GAEKMGERQS WHSYIPYTDR IEYLGGCVNE MPYVLAVEKL AGITVPDRVN
     VIRVMLSELF RINSHLLYIS TFIQDVGAMT PVFFAFTDRQ KIYDLVEAIT GFRMHPAWFR
     IGGVAHDLPR GWDRLLREFL EWMPKRLDSY EKAALRNTIL KGRSQGVAAY GAKEALEWGT
     TGAGLRATGI DFDVRKWRPY SGYENFDFEV PVGGGVSDCY TRVMLKVEEL RQSLRILQQC
     LDNMPEGPFK ADHPLTTPPP KERTLQHIET LITHFLQVSW GPVMPAQESF QMVEATKGIN
     SYYLTSDGST MSYRTRVRTP SFAHLQQIPS AIRGSLVSDL IVYLGSIDFV MSDVDR
 
 
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