NUBCD_GEOUR
ID NUBCD_GEOUR Reviewed; 793 AA.
AC A5GCZ4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, 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=Gura_0333;
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4;
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., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-2007) 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; CP000698; ABQ24549.1; -; Genomic_DNA.
DR RefSeq; WP_011937275.1; NC_009483.1.
DR AlphaFoldDB; A5GCZ4; -.
DR SMR; A5GCZ4; -.
DR STRING; 351605.Gura_0333; -.
DR EnsemblBacteria; ABQ24549; ABQ24549; Gura_0333.
DR KEGG; gur:Gura_0333; -.
DR HOGENOM; CLU_015134_5_0_7; -.
DR OMA; GGRMHYM; -.
DR OrthoDB; 473681at2; -.
DR Proteomes; UP000006695; 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..793
FT /note="NADH-quinone oxidoreductase subunit B/C/D"
FT /id="PRO_0000358645"
FT REGION 1..157
FT /note="NADH dehydrogenase I subunit B"
FT /evidence="ECO:0000250"
FT REGION 162..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..386
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000250"
FT REGION 413..793
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000250"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 89868 MW; A4DA445AE43EA6A3 CRC64;
MTEQDATPHN NVILANLDDL INWGRANSLW PMFFGLSCCF VEMMTSFTSR YDISRFGAEV
LRGTPREADL MVIAGTVFKK MAPSILRLYE QMAEPRWVIS MGSCANSGGM YDVYSVVQGV
NQIIPVDVYV PGCPPRPEAF LQGLMLLQEK IKTCERPARP VLHMQGGSQG TTTPVLVDGV
SKSRDTRGPG MEATSIRGTS VQHPKFLLPR SDEMWRPPAA KHAYPDFDLT GELELAFDHR
LTVDRNATDM LTYRCPAELV PDVLKHLKQR GSKPFRRLED IAAVDESCRR ERGKFRDFTV
NYHLLCFDTP GHIRIKTELS GASPELPTAT AVFSAANWYE REVFDMYGIR FSGHPDLRRI
LMPPDWEGHP LRKEHPFRAT EMPPYTTDDA RKLQPLPAGD FFDRLDEETL ILNLGPQHPG
THGIIRFILK LKGEEIVDMD TDIGFHHRGA EKMGERQHWN QFIPYTDRID YLAGVQNNLA
YVNSVERLCS ITVPDRAVYI RVMLAELFRI ASHLVWLGTF AADVGAMTPV FYTFTDREKI
FDIVEMITGG RMHPAWFRIG GVAEDLPEGW EEPVKAFLAW FPPRLKEYEE LLNGNPIFKA
RLKGVGAIGQ AEAIDWGVSG PNLRACGLEW DLRKKMPYAG YERFHFDVAV AEGGDCYARY
LVRIEEMKQS LHIVRQCLHD MPGGRWITDD YRFVLPQKRD TLNDIESLIH HFVNSTRGMA
PPPGECYTAI EAPKGENGYF VVSDGINIPY RVRIKTPSFP HIQALPLMSK GWLVADFLAI
IGSIDFVLAD LDR
