ID   NUBCD_GEOSL             Reviewed;         792 AA.
AC   Q746S4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 124.
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=GSU3444;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR36834.1; -; Genomic_DNA.
DR   RefSeq; NP_954484.1; NC_002939.5.
DR   RefSeq; WP_010944054.1; NC_002939.5.
DR   AlphaFoldDB; Q746S4; -.
DR   SMR; Q746S4; -.
DR   STRING; 243231.GSU3444; -.
DR   EnsemblBacteria; AAR36834; AAR36834; GSU3444.
DR   KEGG; gsu:GSU3444; -.
DR   PATRIC; fig|243231.5.peg.3466; -.
DR   eggNOG; COG0377; Bacteria.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_5_0_7; -.
DR   InParanoid; Q746S4; -.
DR   OMA; GGRMHYM; -.
DR   Proteomes; UP000000577; 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; IBA:GO_Central.
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..792
FT                   /note="NADH-quinone oxidoreductase subunit B/C/D"
FT                   /id="PRO_0000358644"
FT   REGION          1..156
FT                   /note="NADH dehydrogenase I subunit B"
FT                   /evidence="ECO:0000250"
FT   REGION          230..385
FT                   /note="NADH dehydrogenase I subunit C"
FT                   /evidence="ECO:0000250"
FT   REGION          412..792
FT                   /note="NADH dehydrogenase I subunit D"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   792 AA;  90137 MW;  8BE2808B4070E130 CRC64;
     MSETEVPQNN IILASLDDLI NWGRANSLWP MFFGLSCCFV EMMTSFTSRY DVSRFGAEVL
     RGTPREADLM VIAGTVFKKM APSILRLYEQ MAEPKWVISM GSCANSGGMY DVYSVVQGVN
     QIIPVDVHVP GCPPRPEAFL QGLMLLQEKI RREERPARKV LHLAGGSEGT TRPVLVDGVT
     KSRDTRGPGM EGIAIRGTSV QHPHFPMPRS DEMWRPPAPK HQFPDFGLAG ELETAFGHRV
     VRDDHATDML TYRCPPELLP DVLRHLKTRS AAPFRRLEDV ACVDESCRRE RSRFPDFTVN
     YHLLNFHIPG HLRIKAELRG DTPEIPSATS VFPAADWYER EAFDMYGIQF AGHPNLRRIL
     MPPDWEGHPL RKNHPFRATE MHPYTTDDAR RHQALPASDF FDRIDEETLI LNLGPQHPGT
     HGIIRFVLKL DGEEIVDMDT DIGYHHRGAE KIGERQHWNQ FIPYTDRIDY LAGVQNNLAY
     VNSVERLCGI TVPDRGIAIR VMLAELFRIA NHLVWLGTFA ADVGAMTPVF YTFTDREKIF
     DIVEMVTGGR MHPSWFRIGG VADDLPEGWD GAVKAFLDWM PGRLKEYEDL LKGNPIFRER
     LKGVGVITGD EALEWGITGP NLRACGVEWD LRKKIPYNGY QHFHFEVPTE EGGDCWARYR
     VRIEEIRQSL HIVRQCWKEM PAGRWITDDY RYVLPKKRDA LHDIESLIHH FINATRGMAP
     PKGENYSAIE APKGENGYFV VSDGLNVPYR VRIKTPSFPH IQALPLMSRG WLVADFLAII
     GSIDFVLADL DR