NUOCD_ECOSE
ID NUOCD_ECOSE Reviewed; 600 AA.
AC B6I7N6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=ECSE_2543;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(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}.
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DR EMBL; AP009240; BAG78067.1; -; Genomic_DNA.
DR RefSeq; WP_000247878.1; NC_011415.1.
DR AlphaFoldDB; B6I7N6; -.
DR SMR; B6I7N6; -.
DR EnsemblBacteria; BAG78067; BAG78067; ECSE_2543.
DR GeneID; 67416716; -.
DR KEGG; ecy:ECSE_2543; -.
DR HOGENOM; CLU_015134_3_2_6; -.
DR OMA; GGRMHYM; -.
DR Proteomes; UP000008199; 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_01357; NDH1_NuoC; 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; IPR020396; NADH_UbQ_OxRdtase_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; PS00542; COMPLEX1_30K; 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..600
FT /note="NADH-quinone oxidoreductase subunit C/D"
FT /id="PRO_1000143689"
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; 68725 MW; F83080352BB43A0A CRC64;
MVNNMTDLTA QEPAWQTRDH LDDPVIGELR NRFGPDAFTV QATRTGVPVV WIKREQLLEV
GDFLKKLPKP YVMLFDLHGM DERLRTHREG LPAADFSVFY HLISIDRNRD IMLKVALAEN
DLHVPTFTKL FPNANWYERE TWDLFGITFD GHPNLRRIMM PQTWKGHPLR KDYPARATEF
SPFELTKAKQ DLEMEALTFK PEEWGMKRGT ENEDFMFLNL GPNHPSAHGA FRIVLQLDGE
EIVDCVPDIG YHHRGAEKMG ERQSWHSYIP YTDRIEYLGG CVNEMPYVLA VEKLAGITVP
DRVNVIRVML SELFRINSHL LYISTFIQDV GAMTPVFFAF TDRQKIYDLV EAITGFRMHP
AWFRIGGVAH DLPRGWDRLL REFLDWMPKR LASYEKAALQ NTILKGRSQG VAAYGAKEAL
EWGTTGAGLR ATGIDFDVRK ARPYSGYENF DFEIPVGGGV SDCYTRVMLK VEELRQSLRI
LEQCLNNMPE GPFKADHPLT TPPPKERTLQ HIETLITHFL QVSWGPVMPA NESFQMIEAT
KGINSYYLTS DGSTMSYRTR IRTPSYAHLQ QIPAAIRGSL VSDLIVYLGS IDFVMSDVDR
