NUOB1_GLUDA
ID NUOB1_GLUDA Reviewed; 211 AA.
AC A9HN98;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
GN OrderedLocusNames=GDI2470, Gdia_0717;
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., de Souza Filho G.,
RA Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P.,
RA Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O.,
RA Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=21304715; DOI=10.4056/sigs.972221;
RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT diazotrophicus PAl 5, suggest a new standard in genome sequence
RT submission.";
RL Stand. Genomic Sci. 2:309-317(2010).
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:0000255|HAMAP-Rule:MF_01356}.
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}.
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DR EMBL; CP001189; ACI50507.1; -; Genomic_DNA.
DR EMBL; AM889285; CAP56413.1; -; Genomic_DNA.
DR RefSeq; WP_012226477.1; NC_011365.1.
DR AlphaFoldDB; A9HN98; -.
DR SMR; A9HN98; -.
DR STRING; 272568.GDI2470; -.
DR EnsemblBacteria; ACI50507; ACI50507; Gdia_0717.
DR EnsemblBacteria; CAP56413; CAP56413; GDI2470.
DR KEGG; gdi:GDI2470; -.
DR KEGG; gdj:Gdia_0717; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_7_3_5; -.
DR OMA; GPYWEHG; -.
DR OrthoDB; 1904620at2; -.
DR Proteomes; UP000000736; Chromosome.
DR Proteomes; UP000001176; Chromosome.
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; Reference proteome; Translocase; Transport;
KW Ubiquinone.
FT CHAIN 1..211
FT /note="NADH-quinone oxidoreductase subunit B 1"
FT /id="PRO_0000376244"
FT REGION 187..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ SEQUENCE 211 AA; 23630 MW; 6ADFAC31B008240B CRC64;
MRWSLTRPGE EPGTPRDATM TETVKRNLVM GRLQDFVSWG QKNSIWPFNF GLSCCYVEMA
TAFTSKYDIA RFGSEVLRAT PREADLIVIS GTVFVKMAPI VKYLYDQMLE PRWVISMGSC
ANSGGMYDIY SVVQGVDSFL PVDVYVPGCP PRPDALLEGL MLLQDSVGTQ RRPLSWMVGP
QGVERVTPPS LRDAKRDQRR AAQTLRSPDT I
