NUBCD_CITBB
ID NUBCD_CITBB Reviewed; 794 AA.
AC B5E972;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=Gbem_0178;
OS Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS Bem) (Geobacter bemidjiensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Citrifermentans.
OX NCBI_TaxID=404380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Lovley D., Richardson P.;
RT "Complete sequence of Geobacter bemidjiensis BEM.";
RL Submitted (JUL-2008) 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; CP001124; ACH37209.1; -; Genomic_DNA.
DR AlphaFoldDB; B5E972; -.
DR SMR; B5E972; -.
DR STRING; 404380.Gbem_0178; -.
DR EnsemblBacteria; ACH37209; ACH37209; Gbem_0178.
DR KEGG; gbm:Gbem_0178; -.
DR eggNOG; COG0377; Bacteria.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_015134_5_0_7; -.
DR OMA; GGRMHYM; -.
DR Proteomes; UP000008825; 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; 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_0000358642"
FT REGION 1..158
FT /note="NADH dehydrogenase I subunit B"
FT /evidence="ECO:0000250"
FT REGION 232..387
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; 89984 MW; 401E3A17C0EBB7C1 CRC64;
MSQGDDDKIP ENVLLASLDD MINWGRANSL WPMFFGLSCC FVEMMTSFTS RYDVSRFGAE
VLRGTPRESD LMVIAGTVFK KMAPSILRLY DQMAEPKWVI SMGSCANSGG MYDVYSVVQG
VNQILPVDLY IPGCPPRPES FLEGLMLLQQ KIRSEERPTR PVLRMQGGTQ GTVAPILVDG
ATKSRDTRGP GMEGIAIRGS AMQPPYFAAP RSDELWRPKQ PRLPYPDFNL QAELQGAFAG
QVVLDETACD MLTYRAPARL VPELLRHLKE RKESPFRRLE DIACVDESCR RDREKYKDFT
VNYHLTCFDT PGRIRIKTEL EGSYPEAPSI TSVFPVANWY EREAYDMFGI RFAGHPNLRR
ILMPPDWDGH PLRKEHPARA TELPPYTAED ARRQKALPAG DFFDRVDDET LILNLGPQHP
GTHGVIRFVL KLSGEEIVDM DSDIGYHHRA AEKTGERQNW HQYIPYTDRV DYLSGVQNNL
AYLNSVETLC GIEIPDRAIY IRVMLCELFR IANHLVWLGT FASDLGAMTP VFYTFTDREK
IFDIVEFITG GRMHPAWFRI GGVAEDLPEG WQEKVHSFLE WFPGRLAEYE KLLSGNPIFV
ARLKGVSAIT VDTALEWGIT GPNLRACDFA WDLRKKMPYG GYDRFEFEVA TAQGGDCYAR
YQVRMEEMRQ SLSIVRQAAA GMPGGRFISP DYRYTLPQKR DALEDIESLI HHFVNSTRGI
SPPKGECYAP IEGSKGEYGY FAVSDGLHTA YRMRIRTATF PHIQSLPVLS RGWLVSDFLA
ILGSLDFVLS DLDR
