ID B2JIB0_PARP8 Unreviewed; 277 AA.
AC B2JIB0;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Putative phosphoenolpyruvate synthase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
DE Short=PEP synthase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
DE Short=PSRP {ECO:0000256|HAMAP-Rule:MF_01062};
DE EC=2.7.11.33 {ECO:0000256|HAMAP-Rule:MF_01062};
DE EC=2.7.4.28 {ECO:0000256|HAMAP-Rule:MF_01062};
DE AltName: Full=Pyruvate, water dikinase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
GN OrderedLocusNames=Bphy_1322 {ECO:0000313|EMBL:ACC70504.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC70504.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
CC -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC involved in the regulation of the phosphoenolpyruvate synthase (PEPS)
CC by catalyzing its phosphorylation/dephosphorylation.
CC {ECO:0000256|HAMAP-Rule:MF_01062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-
CC phosphate + AMP + H(+); Xref=Rhea:RHEA:46020, Rhea:RHEA-COMP:11425,
CC Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378, ChEBI:CHEBI:43176,
CC ChEBI:CHEBI:68546, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.11.33; Evidence={ECO:0000256|HAMAP-Rule:MF_01062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[pyruvate, water dikinase]-phosphate + H(+) + phosphate =
CC [pyruvate, water dikinase] + diphosphate; Xref=Rhea:RHEA:48580,
CC Rhea:RHEA-COMP:11425, Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43176, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:68546; EC=2.7.4.28; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01062};
CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC regulatory protein family. PSRP subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01062}.
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DR EMBL; CP001043; ACC70504.1; -; Genomic_DNA.
DR AlphaFoldDB; B2JIB0; -.
DR STRING; 391038.Bphy_1322; -.
DR KEGG; bph:Bphy_1322; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_1_0_4; -.
DR Proteomes; UP000001192; Chromosome 1.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_01062; PSRP; 1.
DR InterPro; IPR005177; Kinase-pyrophosphorylase.
DR InterPro; IPR026530; PSRP.
DR PANTHER; PTHR31756; PYRUVATE, PHOSPHATE DIKINASE REGULATORY PROTEIN 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31756:SF3; PYRUVATE, PHOSPHATE DIKINASE REGULATORY PROTEIN 1, CHLOROPLASTIC; 1.
DR Pfam; PF03618; Kinase-PPPase; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01062}; Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_01062};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01062}.
FT BINDING 157..164
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01062"
SQ SEQUENCE 277 AA; 31369 MW; CADC85225E90BCCE CRC64;
MFPCPLMPPT VFIVSDGTGI TAETFAHSIL SQFDQKFRLV RVPFVDSTEK AYATLEKINE
AAHHEGRRPI VFTTLVNSAS NQIVKDSNAL VLDMFQTFVE PLEQELELKS SHAMGRGHQN
ADTEEYKNRI EAINFSLAHD DGQSNRNLEE ADVILVGVSR SGKTPTSLYL AMQYGVKAAN
YPLIPEDFER GKLPTPLYAH RAKMFGLSID PQRLSEIRNE RRPGSKYAAL ENCRYEINEA
ETMMRREGIK WLSSTHKSIE EIATTILQEI RLDRSSY
//
