ID   NUOCD_SHEON             Reviewed;         601 AA.
AC   Q8EI31;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=SO_1019;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54092.1; -; Genomic_DNA.
DR   RefSeq; NP_716647.1; NC_004347.2.
DR   RefSeq; WP_011071284.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EI31; -.
DR   SMR; Q8EI31; -.
DR   STRING; 211586.SO_1019; -.
DR   PaxDb; Q8EI31; -.
DR   PRIDE; Q8EI31; -.
DR   KEGG; son:SO_1019; -.
DR   PATRIC; fig|211586.12.peg.975; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_6; -.
DR   OMA; GGRMHYM; -.
DR   OrthoDB; 473681at2; -.
DR   PhylomeDB; Q8EI31; -.
DR   BioCyc; SONE211586:G1GMP-945-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0030964; C:NADH dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
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..601
FT                   /note="NADH-quinone oxidoreductase subunit C/D"
FT                   /id="PRO_0000358693"
FT   REGION          1..191
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
FT   REGION          215..601
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
SQ   SEQUENCE   601 AA;  68856 MW;  20D0AE04DDC41D26 CRC64;
     MKLTRDFPHN DTMAQWQPSD HKDAKVVGEL FAHFGAEHFT VQTTRTGVPV VWLPRELLQD
     VVGFLRKLPA PFVMLYDLSA TDERLRSHRD GLPQSDFTVF YHLISIDRNA DVMLKVALAE
     SDLHLPTITN HFPNANWYER EVWDLMGITF DGHPHLTRIM MPKSWQGHPL RKDYPARATE
     FDPFMLDAAK QDMEQENLLF KPEEWGLARG NENEDYMFLN LGPNHPSAHG AFRLVLQLDG
     EEVRNCVPDI GYHHRGAEKM GERQSWHSYI PYTDRVEYLG GVMNNLPYVL AVEKLAGIKV
     PQRVDMIRVM MAELFRIQSH LLFLGTYIQD VGAMTPVFFT FTDRQHIYTI IEAITGARMH
     PAWFRIGGVA HDLPKGWQRL VQDNLLSWLP KRLMDYEKAA MRNSILRGRT IGVAAYTTEQ
     ALAWGTTGAG LRATGLNFDV RKWRPYSGYE QFDFEVPVGS NGDAYDRATV RIEEIRQSMR
     IIEQCMNNMP EGPFKADHPL TTPPPKERTL QHIETLINHF LQVSWGPVMP AAESFQMIEA
     TKGINSYYLT SDGSTMSYRT RIRTPSFAHL QQIPSVIKGS MVSDLIVYLG SIDFVMSDVD
     R