NUOCD_ECOLI
ID NUOCD_ECOLI Reviewed; 596 AA.
AC P33599; P33600; P78089; P78309;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 186.
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};
DE AltName: Full=NUO3/NUO4;
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=b2286, JW5375;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX PubMed=7690854; DOI=10.1006/jmbi.1993.1488;
RA Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
RT "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase
RT in Escherichia coli. Organization of the 14 genes and relationship between
RT the derived proteins and subunits of mitochondrial complex I.";
RL J. Mol. Biol. 233:109-122(1993).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=K12 / AN387;
RA Weidner U.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-5.
RX PubMed=11997136; DOI=10.1016/s0005-2728(01)00248-1;
RA David P., Baumann M., Wikstroem M., Finel M.;
RT "Interaction of purified NDH-1 from Escherichia coli with ubiquinone
RT analogues.";
RL Biochim. Biophys. Acta 1553:268-278(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-596.
RX PubMed=8157582; DOI=10.1128/jb.176.8.2143-2150.1994;
RA Pruss B.M., Nelms J.M., Park C., Wolfe A.J.;
RT "Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect
RT growth on mixed amino acids.";
RL J. Bacteriol. 176:2143-2150(1994).
RN [8]
RP PROTEIN SEQUENCE OF 230-232, AND PRELIMINARY PROTEIN SEQUENCE OF
RP N-TERMINUS.
RX PubMed=7607227; DOI=10.1111/j.1432-1033.1995.tb20594.x;
RA Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T.;
RT "Isolation and characterization of the proton-translocating NADH:
RT ubiquinone oxidoreductase from Escherichia coli.";
RL Eur. J. Biochem. 230:538-548(1995).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
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.
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 -!- INTERACTION:
CC P33599; P33602: nuoG; NbExp=2; IntAct=EBI-552399, EBI-559737;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell
CC inner membrane {ECO:0000255|HAMAP-Rule:MF_01359,
CC ECO:0000269|PubMed:16079137}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01359, ECO:0000269|PubMed:16079137}.
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=AAA03535.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA16115.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA48363.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X68301; CAA48362.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X68301; CAA48363.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75346.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16115.2; ALT_INIT; Genomic_DNA.
DR EMBL; L25055; AAA03535.1; ALT_INIT; Unassigned_DNA.
DR PIR; D65000; D65000.
DR RefSeq; NP_416789.2; NC_000913.3.
DR PDB; 7NYR; EM; 3.30 A; D=1-596.
DR PDB; 7NYU; EM; 3.80 A; D=1-596.
DR PDB; 7NYV; EM; 3.70 A; D=1-596.
DR PDB; 7NZ1; EM; 2.10 A; D=1-596.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR PDBsum; 7NZ1; -.
DR AlphaFoldDB; P33599; -.
DR SMR; P33599; -.
DR BioGRID; 4262976; 70.
DR BioGRID; 851100; 1.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-10380N; -.
DR IntAct; P33599; 6.
DR MINT; P33599; -.
DR STRING; 511145.b2286; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P33599; -.
DR PaxDb; P33599; -.
DR PRIDE; P33599; -.
DR DNASU; 946759; -.
DR EnsemblBacteria; AAC75346; AAC75346; b2286.
DR EnsemblBacteria; BAA16115; BAA16115; BAA16115.
DR GeneID; 946759; -.
DR KEGG; ecj:JW5375; -.
DR KEGG; eco:b2286; -.
DR PATRIC; fig|511145.12.peg.2379; -.
DR EchoBASE; EB2009; -.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_015134_3_2_6; -.
DR InParanoid; P33599; -.
DR OMA; GGRMHYM; -.
DR PhylomeDB; P33599; -.
DR BioCyc; EcoCyc:NUOC-MON; -.
DR BioCyc; MetaCyc:NUOC-MON; -.
DR PRO; PR:P33599; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc.
DR GO; GO:0045271; C:respiratory chain complex I; IC:ComplexPortal.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:EcoCyc.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Multifunctional enzyme; NAD; Quinone;
KW Reference proteome; Translocase; Transport; Ubiquinone.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11997136"
FT CHAIN 2..596
FT /note="NADH-quinone oxidoreductase subunit C/D"
FT /id="PRO_0000118678"
FT REGION 2..186
FT /note="NADH dehydrogenase I subunit C"
FT REGION 210..596
FT /note="NADH dehydrogenase I subunit D"
FT CONFLICT 366
FT /note="H -> D (in Ref. 7; CAA48363)"
FT /evidence="ECO:0000305"
FT CONFLICT 409..412
FT /note="AYGA -> PMAR (in Ref. 1 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="A -> R (in Ref. 7; CAA48363)"
FT /evidence="ECO:0000305"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 277..291
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 297..325
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 335..349
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 372..395
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 459..482
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 508..519
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 536..545
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 560..572
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 591..595
FT /evidence="ECO:0007829|PDB:7NZ1"
SQ SEQUENCE 596 AA; 68236 MW; 5E5EB64FE2D70FDF CRC64;
MTDLTAQEPA WQTRDHLDDP VIGELRNRFG PDAFTVQATR TGVPVVWIKR EQLLEVGDFL
KKLPKPYVML FDLHGMDERL RTHREGLPAA DFSVFYHLIS IDRNRDIMLK VALAENDLHV
PTFTKLFPNA NWYERETWDL FGITFDGHPN LRRIMMPQTW KGHPLRKDYP ARATEFSPFE
LTKAKQDLEM EALTFKPEEW GMKRGTENED FMFLNLGPNH PSAHGAFRIV LQLDGEEIVD
CVPDIGYHHR GAEKMGERQS WHSYIPYTDR IEYLGGCVNE MPYVLAVEKL AGITVPDRVN
VIRVMLSELF RINSHLLYIS TFIQDVGAMT PVFFAFTDRQ KIYDLVEAIT GFRMHPAWFR
IGGVAHDLPR GWDRLLREFL DWMPKRLASY EKAALQNTIL KGRSQGVAAY GAKEALEWGT
TGAGLRATGI DFDVRKARPY SGYENFDFEI PVGGGVSDCY TRVMLKVEEL RQSLRILEQC
LNNMPEGPFK ADHPLTTPPP KERTLQHIET LITHFLQVSW GPVMPANESF QMIEATKGIN
SYYLTSDGST MSYRTRVRTP SFAHLQQIPA AIRGSLVSDL IVYLGSIDFV MSDVDR
