NUOCD_PHOLL
ID NUOCD_PHOLL Reviewed; 599 AA.
AC Q7N2I9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=plu3087;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571869; CAE15461.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7N2I9; -.
DR SMR; Q7N2I9; -.
DR STRING; 243265.plu3087; -.
DR PRIDE; Q7N2I9; -.
DR EnsemblBacteria; CAE15461; CAE15461; plu3087.
DR KEGG; plu:plu3087; -.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_015134_3_2_6; -.
DR OMA; GGRMHYM; -.
DR Proteomes; UP000002514; 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; Reference proteome; Translocase; Transport; Ubiquinone.
FT CHAIN 1..599
FT /note="NADH-quinone oxidoreductase subunit C/D"
FT /id="PRO_0000358653"
FT REGION 1..190
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
FT REGION 214..599
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
SQ SEQUENCE 599 AA; 69023 MW; 6C8AA9F21A72771A CRC64;
MMIDQIAQES ARPAWQTHDH LDDPVMGELR NHFGPDAFTV QPTRTGIPVV WVKREQLLEV
MTFLKKLPKP YVMLFDLHGM DERQRTHRQG LPAADFSVFY HLLSIERNRD IMLKVALSEK
ELNLPTATPL FPNANWYERE TWEMFGVVFN GHPNLRRIML PPTWEGHPLR KDYPARATEF
DPFELTRQKE DLEMEALTFK PEEWGMKRGT ENEDFMFLNL GPNHPSSHGA FRIILQLDGE
EIVDCVPDIG YHHRGAEKMG ERQSWHSYIP YTDRIEYLGG CVNEMPYVLA VEKLAGIEVP
DRVKTIRVML SELFRINSHL LYISTFIQDV GGMTPVFFAF TDRQKVYDLV EAITGFRMHP
AWFRIGGVAH DLPRGWDRLL RDFLNWMPKR LDSYVKAALK NSILKGRAIG VAAYNSKQAL
EWGTTGAGLR ATGIAFDVRK WRPYSGYENF DFDVPIGNNG DCYDRVMLKV EEVRQSLRIL
KQCLDNMPEG PFKADHPLTT PPPKERTLQH IETMINHFLQ VSWGPVMPAN ESFQMIEATK
GINSYYLTSD GSTVSYRTRV RTPSYPHLQQ IPSVIRGSLV SDLIVYLGSI DFVMSDVDR
