(data stored in ACNUC29543 zone)

SWISSPROT: NUOCD_ACIBT

ID   NUOCD_ACIBT             Reviewed;         595 AA.
AC   A3M2Q0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, 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=A1S_0754;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is
CC       believed to be ubiquinone. Couples the redox reaction to proton
CC       translocation (for every two electrons transferred, four hydrogen
CC       ions are translocated across the cytoplasmic membrane), and thus
CC       conserves the redox energy in a proton gradient.
CC       {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,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01359};
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits
CC       NuoB, CD, E, F, and G constitute the peripheral sector of the
CC       complex. {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-
CC       Rule:MF_01359}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30
CC       kDa subunit family. {ECO:0000255|HAMAP-Rule:MF_01359}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49
CC       kDa subunit family. {ECO:0000255|HAMAP-Rule:MF_01359}.
DR   EMBL; CP000521; ABO11194.2; -; Genomic_DNA.
DR   SMR; A3M2Q0; -.
DR   EnsemblBacteria; ABO11194; ABO11194; A1S_0754.
DR   KEGG; acb:A1S_0754; -.
DR   HOGENOM; HOG000228264; -.
DR   KO; K13378; -.
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; 1.10.645.20; -; 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; IPR038290; NADH_Q_OxRdtase_suD_sf.
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   Pfam; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   ProDom; PD001581; NADH_UbQ_OxRdtase_30kDa_su; 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;
DR   PRODOM; A3M2Q0.
DR   SWISS-2DPAGE; A3M2Q0.
KW   Cell inner membrane; Cell membrane; Membrane; Multifunctional enzyme;
KW   NAD; Quinone; Translocase; Transport; Ubiquinone.
FT   CHAIN         1    595       NADH-quinone oxidoreductase subunit C/D.
FT                                /FTId=PRO_0000358607.
FT   REGION        1    186       NADH dehydrogenase I subunit C.
FT                                {ECO:0000255|HAMAP-Rule:MF_01359}.
FT   REGION      210    595       NADH dehydrogenase I subunit D.
FT                                {ECO:0000255|HAMAP-Rule:MF_01359}.
SQ   SEQUENCE   595 AA;  68580 MW;  FDEFC80E5F760D9C CRC64;
     MAETDIAMPE STPVDSRPAF AIVEELKTKF GENFYVQATF EEFPTVWVER ARVQEVLMFL
     RKVERPYVML FDLSAMDERL RQHRDGLPAS DFTVFYHLLS LERNSDIRIK VALNENDLNL
     PTATNIWPNA NWYEREAYDM FGINFEGHPM LRRILLPTYW EGHPLRKEYS ARATEYTPYM
     QDKAKQDFEQ EHLRFVPEDW GLKRGNADED FMFLNLGPNH PSAHGAFRIV LQLDGEEVKD
     CVPDIGYHHR GVEKMAERQT WHSFIPYTDR VDYLGGCAQN MPYVMAVEQL AGIKVPERAQ
     VIRVMLNELF RINNHLLYCG TAIQDAGGMT PVFYMFADRQ KVYDIVEAIT GYRMHPAWFR
     IGGTAHDLPN NWQKLVKELL DWMPKRLNEY YTAAFKNSVF IGRTRNVAQY DAKSALAWGV
     TGTGLRATGI DFDVRKYRPY SGYENFDFEV PVEYEGDAYA RVLVHFREIE QSLKIIKQCL
     DNMPSGPYKA DHPLAVPPPK DKTLQDIETL ITHFLSVSWG PVMPAGEASF MTEVVKGAST
     YYLTSDKATM SYRTRIRTPT FTHLQQIPSV INGSLVSDLI IYLATIDVVM ADVDR
//

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