NUBCD_SYNFM
ID NUBCD_SYNFM Reviewed; 787 AA.
AC A0LJM5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=Sfum_1942;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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; CP000478; ABK17627.1; -; Genomic_DNA.
DR RefSeq; WP_011698797.1; NC_008554.1.
DR AlphaFoldDB; A0LJM5; -.
DR SMR; A0LJM5; -.
DR STRING; 335543.Sfum_1942; -.
DR EnsemblBacteria; ABK17627; ABK17627; Sfum_1942.
DR KEGG; sfu:Sfum_1942; -.
DR eggNOG; COG0377; Bacteria.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_015134_5_1_7; -.
DR OMA; GGRMHYM; -.
DR OrthoDB; 473681at2; -.
DR Proteomes; UP000001784; 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..787
FT /note="NADH-quinone oxidoreductase subunit B/C/D"
FT /id="PRO_0000358703"
FT REGION 1..149
FT /note="NADH dehydrogenase I subunit B"
FT /evidence="ECO:0000250"
FT REGION 154..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..380
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000250"
FT REGION 407..787
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000250"
SQ SEQUENCE 787 AA; 88858 MW; 0891300B37D05455 CRC64;
MSDRFLSAAD FVLNWSRKYS LWPLFFGLSC CFVEEATAFT PRYDMARFGA EVLRPSPRQA
DLLIVSGTVF KKIAPVVLRL YEQMAEPKWV ISMGSCSNCG GMYDVYSVVQ GIDQILPVDV
YIPGCPPRPE AVLQGLTLLQ KKIAAEERPA RSVLHLPGGS QGSTRPVLVD GATKSRDPRG
PGMEGTVIRG TANTPPAFTG SRSDLMWTPP ARRIESSERE KELARVLSER FGDAVREEPF
TSDMPTFHVE TNRLKDVLGF LKKEASPRFL RLDDLTAVDE SARRDRSAYP DWTMVYHLLS
FEPAGRVRLK TGLHGRQPAL PSITDIWPSA NWYEREVYDL FGIRFEGHPN LRRIMMPHDW
EGHPLRKDYP GRATQMAPYT LGDARVHQPP DGGIFTKDPG GDRLVLNIGP SHVSTHGLLR
YVVSLDGEEI SDLELEIGYH HRGVEKIGER QTWHQFIPYC ARVDYLAGAA NDLPYVMAVE
TLADIKVPER AQVIRVLLSE LFRLSNHLVW FATYAHDVGA MTPNFYTFTE REMILDIVEL
ITGGRLHPSW FRLGGVAADL PEGWKEAVDA LVRIFPGRLR EYESLIRKNP IFKARTQGVG
RISREDAVDW GVSGPNLRAC GLEWDLRRKF PYSGYENFEF EVPTAVEGDC YARYLVRVEE
MRQSLRIIEQ AAANMPSGRH VTDDYRYVIP DRRDTLKNIE SLIHHFVNVT RGPRIPKGEA
YVSCEIPRGE QGYYVVGDGL GYAYRMRIRG PGFANVQVMP LLARGESIAD LIAIIGSVDY
ILPDIDR
