NUOCD_CROS8
ID NUOCD_CROS8 Reviewed; 603 AA.
AC A7MH24;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=ESA_00934;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU76204.1; -; Genomic_DNA.
DR AlphaFoldDB; A7MH24; -.
DR SMR; A7MH24; -.
DR PRIDE; A7MH24; -.
DR EnsemblBacteria; ABU76204; ABU76204; ESA_00934.
DR KEGG; esa:ESA_00934; -.
DR HOGENOM; CLU_015134_3_2_6; -.
DR OMA; GGRMHYM; -.
DR Proteomes; UP000000260; 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..603
FT /note="NADH-quinone oxidoreductase subunit C/D"
FT /id="PRO_0000358628"
FT REGION 1..193
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
FT REGION 217..603
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01359"
SQ SEQUENCE 603 AA; 69227 MW; B8B49DB2E3AAF79B CRC64;
MVNNMTDLTA QDAVLPVWQT RDHLDDPVIG ELRNRFGPDA FTVQATRTGV PVVWVKREQL
LEVGEFLRKL PKPYVMLYDL HGMDERLRTH RNGLPAADFS VFYHLLSIDR NRDIMLKVAL
SENDLNVPTF TRLFPNANWY ERETWEMFGI TFTGHPNLRR IMMPPTWEGH PLRKDYPARA
TEFDPFTLTK QKEELEMEAL TFKPEEWGMK RGNDTEDFMF LNLGPNHPSA HGAFRIILQL
DGEEIVDCVP DIGYHHRGAE KMGERQSWHS YIPYTDRVEY LGGCVNEMPY VLAVEKLAGI
QVPERVEVIR VMLSELFRIN SHLLYISTFI QDVGAMTPVF FAFTDRQKIY DLVEAITGFR
MHPAWFRIGG VAHDLPRGWD RLLKEFLEWM PKRLDSYVKA ALKNTILKGR SQGVAAYDAK
EALAWGTTGA GLRATGIDFD VRKARPYSGY QNFEFEVPVG GGISDCYTRV MLKVEEVRQS
LRILEQCLKN MPEGPFKADH PLTTPPPKER TLQHIETLIT HFLQVSWGPV MPANESFQMI
EATKGINSYY LTSDGSTMSY RTRVRTPSFP HLQQIPSVIR GSLVSDLIVY LGSIDFVMSD
VDR
