NUBCD_GEOMG
ID NUBCD_GEOMG Reviewed; 791 AA.
AC Q39ZC4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=Gmet_0153;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000148; ABB30400.1; -; Genomic_DNA.
DR RefSeq; WP_004512740.1; NC_007517.1.
DR AlphaFoldDB; Q39ZC4; -.
DR SMR; Q39ZC4; -.
DR STRING; 269799.Gmet_0153; -.
DR EnsemblBacteria; ABB30400; ABB30400; Gmet_0153.
DR KEGG; gme:Gmet_0153; -.
DR eggNOG; COG0377; Bacteria.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_015134_5_0_7; -.
DR OMA; GGRMHYM; -.
DR OrthoDB; 473681at2; -.
DR Proteomes; UP000007073; 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..791
FT /note="NADH-quinone oxidoreductase subunit B/C/D"
FT /id="PRO_0000358643"
FT REGION 1..155
FT /note="NADH dehydrogenase I subunit B"
FT /evidence="ECO:0000250"
FT REGION 229..384
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000250"
FT REGION 411..791
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000250"
SQ SEQUENCE 791 AA; 90369 MW; 8E9C5038E36A6B71 CRC64;
MEETEIPQNI VLTRLDDLIN WGRANSLWPM FFGLSCCFVE MMTSFTSRYD ISRFGAEVLR
GTPREADLMV IAGTVFKKMA PSILRLYEQM AEPKWVISMG SCANSGGMYD VYSVVQGVNQ
IIPVDVHVPG CPPRPEAFLQ GVMLLQEKIR REERPARKVL HMAGGTEGTT RPVLVDGVTK
SRDTRGPGME GIAIRGTPVQ HPRFWMSRSD EMWRPPAPRH DYPDFGLAGE LETIFGGRVA
VEQAATDMLT YRCPPELVPE VLRHLKSRSS APFRRLEDVV CVDESCRRER ERFPDFTVNY
HLLNFDIPGH LRIKTELMGE TPELPSATGV FPAADWYERE AFDMYGIRFA GHPNLRRILM
PPDWEGHPLR KEHPFRATEM PPYTTDDARR HQALPASDFF DRIDEETLII NLGPQHPGTH
GIIRFILKLD GEEIVDMDTD IGYHHRGAEK IGERQHWNQF IPYTDRIDYL AGVQNNLAYV
NSVERLCGIT VPDRAITIRV MLAELFRIAS HLVWLGTFAA DVGAMTPVFY TFTDREKIFD
IIEMVTGGRM HPSWFRIGGV TEDLPEGWDG AVKEFLDWMP GRLKEYEDLL KENPIFKARL
KGVGVITKDE AMEWGITGPN LRACGMAWDL RKKIPYNGYQ HFHFEIPTEE GGDCWARYRI
RVEEIRQSLH IVAQCRKEMP AGRWITDDYR YVLPKKRDTL HDIESLIHHF INATRGMAPP
RGENYSAIEA PKGENGYFVV SDGLNVPYRV RIKTPSFPHI QALPLMSRGW LVADFLAIIG
SIDFVLADLD R
