NUOB1_BURMA
ID NUOB1_BURMA Reviewed; 159 AA.
AC Q62IN6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=NADH-quinone oxidoreductase subunit B 1 {ECO:0000255|HAMAP-Rule:MF_01356};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01356};
DE AltName: Full=NADH dehydrogenase I subunit B 1 {ECO:0000255|HAMAP-Rule:MF_01356};
DE AltName: Full=NDH-1 subunit B 1 {ECO:0000255|HAMAP-Rule:MF_01356};
GN Name=nuoB1 {ECO:0000255|HAMAP-Rule:MF_01356}; OrderedLocusNames=BMA1828;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient (By
CC similarity). {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 Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01356};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC D, E, F, and G constitute the peripheral sector of the complex.
CC {ECO:0000255|HAMAP-Rule:MF_01356}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01356}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01356}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01356}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU49834.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000010; AAU49834.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004186402.1; NC_006348.1.
DR RefSeq; YP_103433.1; NC_006348.1.
DR AlphaFoldDB; Q62IN6; -.
DR SMR; Q62IN6; -.
DR STRING; 243160.BMA1828; -.
DR EnsemblBacteria; AAU49834; AAU49834; BMA1828.
DR GeneID; 60546704; -.
DR GeneID; 66546648; -.
DR KEGG; bma:BMA1828; -.
DR PATRIC; fig|243160.12.peg.1866; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_7_3_4; -.
DR Proteomes; UP000006693; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Quinone; Translocase; Transport; Ubiquinone.
FT CHAIN 1..159
FT /note="NADH-quinone oxidoreductase subunit B 1"
FT /id="PRO_0000358369"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ SEQUENCE 159 AA; 17533 MW; 9E9DC79E05AC522A CRC64;
MSIEGVLKEG FVTTTADKLI NWTRTGSLWP MTFGLACCAV EMMHAGAARY DLDRFGVVFR
PSPRQSDVMI VAGTLCNKMA PALRRVYDQM AEPRWVISMG SCANGGGYYH YSYSVVRGCD
RIVPVDVYVP GCPPTAEALV YGVIQLQAKI RRTSTIARQ
