ID A0A075P1K9_9ALTE Unreviewed; 270 AA.
AC A0A075P1K9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 ORFNames=EP13_08965 {ECO:0000313|EMBL:AIF98795.1};
OS Alteromonas australica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=589873 {ECO:0000313|EMBL:AIF98795.1, ECO:0000313|Proteomes:UP000056090};
RN [1] {ECO:0000313|EMBL:AIF98795.1, ECO:0000313|Proteomes:UP000056090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 17 {ECO:0000313|EMBL:AIF98795.1,
RC ECO:0000313|Proteomes:UP000056090};
RA Gonzaga A., Lopez-Perez M., Rodriguez-Valera F.;
RT "Genomes of Alteromonas australica, a world apart.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; CP008849; AIF98795.1; -; Genomic_DNA.
DR RefSeq; WP_044056953.1; NZ_CP008849.1.
DR AlphaFoldDB; A0A075P1K9; -.
DR GeneID; 78255042; -.
DR KEGG; aal:EP13_08965; -.
DR eggNOG; COG1806; Bacteria.
DR Proteomes; UP000056090; Chromosome.
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:UP000056090};
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 149..156
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01062"
SQ SEQUENCE 270 AA; 30865 MW; 58859DDDE7DDE08C CRC64;
MRTAFYISDG TAITAEVFGH ALLSLFPVEF NHNTIPFVET EEHAQKVLEK ISESFQDTGE
RPLVFYTIVN VDVRKIIAKS VGINYNFLDQ FVAPLEKVLG VPSKPEKHRT HSIHETTYDI
RIEAVNYALA NDDGSNLKDY DEADIILTGV SRSGKTPTSL YLALQFGIKA ANYPFTEDDM
GDMLKLPPAL RRYKHKLFGL TIAAERLHQI RSERRANSKY ASIQQCRMEL REVENLYRKE
KIPFLNSTKY SIEEISAKIL AETGLKRRKY
//
