PDRP_BRUAB
ID PDRP_BRUAB Reviewed; 279 AA.
AC Q57AJ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Putative pyruvate, phosphate dikinase regulatory protein {ECO:0000255|HAMAP-Rule:MF_00921};
DE Short=PPDK regulatory protein {ECO:0000255|HAMAP-Rule:MF_00921};
DE EC=2.7.11.32 {ECO:0000255|HAMAP-Rule:MF_00921};
DE EC=2.7.4.27 {ECO:0000255|HAMAP-Rule:MF_00921};
GN OrderedLocusNames=BruAb1_2042;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
CC -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC involved in the regulation of the pyruvate, phosphate dikinase (PPDK)
CC by catalyzing its phosphorylation/dephosphorylation.
CC {ECO:0000255|HAMAP-Rule:MF_00921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate,
CC phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-
CC phospho-L-threonyl-[pyruvate, phosphate dikinase];
CC Xref=Rhea:RHEA:43692, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:83586, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.11.32; Evidence={ECO:0000255|HAMAP-Rule:MF_00921};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-
CC [pyruvate, phosphate dikinase] + phosphate = diphosphate + N(tele)-
CC phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase];
CC Xref=Rhea:RHEA:43696, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61977, ChEBI:CHEBI:83586; EC=2.7.4.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00921};
CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC regulatory protein family. PDRP subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00921}.
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DR EMBL; AE017223; AAX75343.1; -; Genomic_DNA.
DR RefSeq; WP_002965131.1; NC_006932.1.
DR AlphaFoldDB; Q57AJ1; -.
DR SMR; Q57AJ1; -.
DR EnsemblBacteria; AAX75343; AAX75343; BruAb1_2042.
DR GeneID; 45125321; -.
DR GeneID; 55591637; -.
DR KEGG; bmb:BruAb1_2042; -.
DR HOGENOM; CLU_046206_2_0_5; -.
DR OMA; YAQCEFE; -.
DR Proteomes; UP000000540; Chromosome I.
DR GO; GO:0043531; F:ADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006468; P:protein phosphorylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00921; PDRP; 1.
DR InterPro; IPR005177; Kinase-pyrophosphorylase.
DR InterPro; IPR026565; PPDK_reg.
DR PANTHER; PTHR31756; PTHR31756; 1.
DR Pfam; PF03618; Kinase-PPPase; 1.
PE 3: Inferred from homology;
KW Kinase; Nucleotide-binding; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..279
FT /note="Putative pyruvate, phosphate dikinase regulatory
FT protein"
FT /id="PRO_0000316641"
FT BINDING 153..160
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ SEQUENCE 279 AA; 30481 MW; 452110EFCD636FA5 CRC64;
MTRPLSYFHL HLISDATGET LLAAGRAAAA QYANARAIEH IYPLIRTEKQ LRKVLEGIDA
EPGIVLYTVV DQKLAAIIDE SCADMGVPSV SVLEPVLNTF QSYLGAPAHR RASAQHVLNA
DYFRRIDALN FMMEHDDGQL PLDIEEADVI IVGISRTSKT PTSIYLANRG IKAANVPLVL
GIPVPEILFA AKRPLIVGLV ATAERISQIR QNRPLGNIPS LDTGLYTDRV SISEELAYAR
NLCNRHGWPI IDVSRRSIEE TAAAILALLR NGKKEGSSS
