PDRP_AFIC5
ID PDRP_AFIC5 Reviewed; 283 AA.
AC B6JAK6; F8BS11;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=OCA5_c01460, OCAR_4385;
OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS (Oligotropha carboxidovorans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Afipia.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=18539730; DOI=10.1128/jb.00614-08;
RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT carboxidovorans OM5T.";
RL J. Bacteriol. 190:5531-5532(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=21742883; DOI=10.1128/jb.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT carboxidovorans strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI91531.1; -; Genomic_DNA.
DR EMBL; CP002826; AEI04878.1; -; Genomic_DNA.
DR RefSeq; WP_012561562.1; NC_015684.1.
DR AlphaFoldDB; B6JAK6; -.
DR SMR; B6JAK6; -.
DR STRING; 504832.OCAR_4385; -.
DR EnsemblBacteria; AEI04878; AEI04878; OCA5_c01460.
DR KEGG; oca:OCAR_4385; -.
DR KEGG; ocg:OCA5_c01460; -.
DR PATRIC; fig|504832.7.peg.153; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_2_0_5; -.
DR OMA; YAQCEFE; -.
DR OrthoDB; 980472at2; -.
DR Proteomes; UP000007730; 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 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..283
FT /note="Putative pyruvate, phosphate dikinase regulatory
FT protein"
FT /id="PRO_1000149712"
FT BINDING 154..161
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ SEQUENCE 283 AA; 31320 MW; D7C5813BCA791EBB CRC64;
MAGTNKSYFH LHMISDSTGE TLIMVARAVA AQYANVTPVE HVYPLVRSQK QLDRVLAEIE
EAPGIVLFTL LEKDLVERVE ATCKDMNIPS LSIIGPVMEL FRAYLGRETS PRVGAQHTLN
AEYFNRIDAL NYTMMHDDGQ HVEGLEEADV VLVGVSRTSK TPTSIYLANR GIRTANVPLV
PGIPIPPQLE TLKKPLVVSL HATPERLVQV RQNRLLGIGA GAPLPGRGED SYIDSRSVAE
EVAFARKLSA KYDWPLLDVT RRSIEETAAA VMKLYADRQR QHG
