ID   NUOCD_CITK8             Reviewed;         600 AA.
AC   A8ADV3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=CKO_00510;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-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_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}.
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DR   EMBL; CP000822; ABV11666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8ADV3; -.
DR   SMR; A8ADV3; -.
DR   STRING; 290338.CKO_00510; -.
DR   PRIDE; A8ADV3; -.
DR   EnsemblBacteria; ABV11666; ABV11666; CKO_00510.
DR   KEGG; cko:CKO_00510; -.
DR   HOGENOM; CLU_015134_3_2_6; -.
DR   OMA; GGRMHYM; -.
DR   Proteomes; UP000008148; 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; Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..600
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358627"
FT   REGION          1..190
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
FT   REGION          214..600
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
SQ   SEQUENCE   600 AA;  68776 MW;  D58DBF0A3B3D04AC CRC64;
     MVNNMTDLTA QDAVWQTRDH LDDPVIGELR NRFGPDAFTV QATRTGVPVV WVKREQLLEV
     GDFLKKLPKP YVMLFDLHGM DERLRTHRDG LPAADFSVFY HLISIDRNRD IMLKVALSEN
     DLHVPTFTKL FPNANWYERE TWEMFGITFD GHPHLTRLLM PPTWEGHPLR KDYPARATEF
     DPFELTKAKQ DLEMEALTFK PEDWGMQRGT ENEDFMFLNL GPNHPSSHGA FRIVLQLDGE
     EIVDCVPDIG YHHRGAEKMG ERQSWHSYIP YTDRIEYLGG CVNEMPYVLA VEKLAGITVP
     DRVNVIRVML SELFRINSHL LYISTFIQDV GAMTPVFFAF TDRQKIYDVV EAITGFRMHP
     AWFRIGGVAH DLPRGWDRLL RDFLDWMPKR LDSYEKAALR NTILKGRSQG VAAYGKKEAL
     DWGCTGAALR ATGIDFDVRK SRPYSGYENF DFEIPVGGGV SDCYTRVMLK VEELRQSLRI
     LEQCLNNMPE GPFKADHPLT TPPPKERTLQ HIETLITHFL QVSWGPVMPA NESFQMVEAT
     KGINSYYLTS DGSTMSYRTR IRTPSYAHLQ QIPVAVRGSL VSDLIVHLGS IDFVMSDVDR