(data stored in ACNUC7421 zone)

SWISSPROT: PDRP_RHOPS

ID   PDRP_RHOPS              Reviewed;         279 AA.
AC   Q13E25;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JAN-2019, 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=RPD_0426;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC       involved in the regulation of the pyruvate, phosphate dikinase
CC       (PPDK) 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-
CC         COMP:10651, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:83586, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; EC=2.7.11.32; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00921};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-
CC         [pyruvate, phosphate dikinase] + phosphate = diphosphate +
CC         N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate
CC         dikinase]; Xref=Rhea:RHEA:43696, Rhea:RHEA-COMP:10650,
CC         Rhea:RHEA-COMP:10651, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:83586; EC=2.7.4.27; Evidence={ECO:0000255|HAMAP-
CC         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}.
DR   EMBL; CP000283; ABE37664.1; -; Genomic_DNA.
DR   RefSeq; WP_011500852.1; NC_007958.1.
DR   SMR; Q13E25; -.
DR   STRING; 316057.RPD_0426; -.
DR   PRIDE; Q13E25; -.
DR   EnsemblBacteria; ABE37664; ABE37664; RPD_0426.
DR   KEGG; rpd:RPD_0426; -.
DR   eggNOG; ENOG4105CF9; Bacteria.
DR   eggNOG; COG1806; LUCA.
DR   HOGENOM; HOG000218052; -.
DR   KO; K09773; -.
DR   OMA; TSKTPTC; -.
DR   OrthoDB; 980472at2; -.
DR   BioCyc; RPAL316057:RPD_RS02190-MONOMER; -.
DR   Proteomes; UP000001818; 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:0006470; P:protein dephosphorylation; 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;
DR   PRODOM; Q13E25.
DR   SWISS-2DPAGE; Q13E25.
KW   Complete proteome; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    279       Putative pyruvate, phosphate dikinase
FT                                regulatory protein.
FT                                /FTId=PRO_0000316727.
FT   NP_BIND     153    160       ADP. {ECO:0000255|HAMAP-Rule:MF_00921}.
SQ   SEQUENCE   279 AA;  30783 MW;  99318A04E86E20E0 CRC64;
     MLTDGSYFHL HLVSDSTGET LITVSRAVAA QYANVSPVEH VYPLVRSQKQ LDRVLQEIEE
     SPGIVLFTLL ESELVNRLEA KCQQINSPSL SIIGPVMQLF EAYLGASTTG RVGAQHTLNA
     EYFKRIDALN YSMMHDDGQH VEGLEEADVV LVGVSRTSKT PTSIYLANRG IRTANVPLVA
     GIPIPHQLET LKKPLVVSLH ASPDRLIQVR QNRLLSLGAG AGNDSYIDRQ AVTDEVLLAR
     KLSAKYGWSL LDVTRRSIEE TAAAIMKLLA DRQRQRMSE
//

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