NUBCD_SYNC1
ID NUBCD_SYNC1 Reviewed; 794 AA.
AC Q3A825;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=NADH-quinone oxidoreductase subunit B/C/D;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit B/C/D;
DE AltName: Full=NDH-1 subunit B/C/D;
GN Name=nuoBCD; Synonyms=nuoB, nuoC, nuoD; OrderedLocusNames=Pcar_0206;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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 -!- SUBUNIT: NDH-1 is composed of about 13 different subunits. Subunits
CC NuoBCD, E, F, and G constitute the peripheral sector of the complex (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the complex I 20 kDa
CC subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the complex I 30 kDa
CC subunit family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC subunit family. {ECO:0000305}.
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DR EMBL; CP000142; ABA87467.1; -; Genomic_DNA.
DR RefSeq; WP_011339867.1; NC_007498.2.
DR AlphaFoldDB; Q3A825; -.
DR SMR; Q3A825; -.
DR STRING; 338963.Pcar_0206; -.
DR EnsemblBacteria; ABA87467; ABA87467; Pcar_0206.
DR KEGG; pca:Pcar_0206; -.
DR eggNOG; COG0377; Bacteria.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_5_0_7; -.
DR OMA; GGRMHYM; -.
DR OrthoDB; 473681at2; -.
DR Proteomes; UP000002534; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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; 1.10.645.10; -; 1.
DR Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
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; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
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 Pfam; PF01058; Oxidored_q6; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 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..794
FT /note="NADH-quinone oxidoreductase subunit B/C/D"
FT /id="PRO_0000358652"
FT REGION 1..154
FT /note="NADH dehydrogenase I subunit B"
FT /evidence="ECO:0000250"
FT REGION 230..383
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000250"
FT REGION 414..794
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000250"
SQ SEQUENCE 794 AA; 88844 MW; 61FB467B9AC50FC4 CRC64;
MSESIPKNII LTTLDDAINW GRKNSMWPMF FGLSCCFVEM MGSMTPRFDL ARFGAEVLRG
TPREADLMVI AGTPFKKMAA SMLRVYEEMA NPKWVIAMGS CANSGGMYDV YSVMQGVNQV
LPVDVYIPGC PPRPEAFMQG LMTLQEKIAR KESPARPVLN LRGGNEGTTV PILIDGSSKT
RDTRGPGYGH CPIRGTAQQH PDFKGHRAAG MWGPPQPKIA FSASTAPLLE QLRERFGDDV
RQEEGADMPT LVADPAQVPE LLRFLKQDID QPYERLEDLT AIDETARSQR PAHDLTMVYH
LLSFERAGYL RVKAPLRNDR AEVPSITGLW PAANWYEREA FDMFGVRFAG HPDLRRILMP
EGWQGHPLRK SHPSRATDMP PFTRDTATTM VPPEGSHFFS NRAPVDNQSL SILNLGPQHP
GTHGILRVIL QLAGEEIVDL DSEIGYHHRG AEKIAERQHW NQYIPYTDRI DYLAGSLNNL
AYLYSVETLC GVEVPPRARY IRVLLSELFR IASHLVWLGT FAHDVGAMTP VFYAFDSREK
IFDIIELITG GRMHPAWFRI GGVPDDLPDG WLAAVEAFTR DFEARIDEFD RLLTGGPIFR
ARTEGIGTVS RQQAVELGFS GPNLRATGLA WDLRKSMPYG GYDEFDFDVV TAGGGDCFAR
YLVRLGELRQ SLRIVRQAAE GMPQGRWISD QYRYAYPKRE DGLQDIESLI HHFLHVSRGP
AAPRGECYRA IESSKGECGY YAVSDGGTGA YRLRIRTPSF PHLQALPQLS RGRLVADVIT
ILGSLDYVLA DLDR
