PDRP_BRUMB
ID PDRP_BRUMB Reviewed; 279 AA.
AC C0RFV5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=BMEA_A2129;
OS Brucella melitensis biotype 2 (strain ATCC 23457).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=546272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23457;
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Han C., Detter J.C., Bruce D., Brettin T.S.;
RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001488; ACO01777.1; -; Genomic_DNA.
DR RefSeq; WP_004686215.1; NC_012441.1.
DR AlphaFoldDB; C0RFV5; -.
DR SMR; C0RFV5; -.
DR EnsemblBacteria; ACO01777; ACO01777; BMEA_A2129.
DR KEGG; bmi:BMEA_A2129; -.
DR HOGENOM; CLU_046206_2_0_5; -.
DR OMA; YAQCEFE; -.
DR Proteomes; UP000001748; 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_1000149701"
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; 425660E8BA136FA5 CRC64;
MTRPLSYFHL HLISDATGET LLAAGRAAAA QYANARAIEH IYPLIRTEKQ LRKVLEGIDA
EPGIVLYTVV DQKLAAIIDE SCADMGVPSV SVLEPVLNTF QSYLGAPAHR RASAQHVLNA
DYFRRIDALN FMMEHDDGQL PLDIEEADVI IVGISRTSKT PTSIYLANRG IKAANVPLVL
GIPVPEILFA AKRPLIVGLV ATAERISQIR QNRPIGNIPS LDTGLYTDRV SISEELAYAR
NLCNRHGWPI IDVSRRSIEE TAAAILALLR NGKKEGSSS
