ID   PDRP2_SYNWW             Reviewed;         273 AA.
AC   Q0AWT8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   18-JUN-2025, entry version 85.
DE   RecName: Full=Putative pyruvate, phosphate dikinase regulatory protein 2 {ECO:0000255|HAMAP-Rule:MF_00921};
DE            Short=PPDK regulatory protein 2 {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=Swol_1513;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC   Syntrophomonadaceae; Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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=N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate
CC         dikinase] + ADP = N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-
CC         [pyruvate, phosphate dikinase] + AMP + H(+); Xref=Rhea:RHEA:43692,
CC         Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:61977, ChEBI:CHEBI:83586,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.11.32;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00921};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate,
CC         phosphate dikinase] + phosphate + H(+) = N(tele)-phospho-L-
CC         histidyl/L-threonyl-[pyruvate, phosphate dikinase] + diphosphate;
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; CP000448; ABI68816.1; -; Genomic_DNA.
DR   RefSeq; WP_011640915.1; NC_008346.1.
DR   AlphaFoldDB; Q0AWT8; -.
DR   SMR; Q0AWT8; -.
DR   STRING; 335541.Swol_1513; -.
DR   KEGG; swo:Swol_1513; -.
DR   eggNOG; COG1806; Bacteria.
DR   HOGENOM; CLU_046206_2_1_9; -.
DR   OrthoDB; 9782201at2; -.
DR   Proteomes; UP000001968; 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   HAMAP; MF_00921; PDRP; 1.
DR   InterPro; IPR005177; Kinase-pyrophosphorylase.
DR   InterPro; IPR026565; PPDK_reg.
DR   NCBIfam; NF003742; PRK05339.1; 1.
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; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..273
FT                   /note="Putative pyruvate, phosphate dikinase regulatory
FT                   protein 2"
FT                   /id="PRO_0000316752"
FT   BINDING         151..158
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ   SEQUENCE   273 AA;  30691 MW;  7DB0833725F8EC34 CRC64;
     MSNHLPGVFI VSDSIGETAE MVVRAAASQF NSGNMEIRQV PNISDTETLE EIINQAAASN
     FIIAYTLVIN ELADFLKMEA RKKGVICVDV LGPVIEAFKS VSDIEPRREP GLLRKVDEMY
     YRRVEAVEFA VRYDDGKDPR GVMQSDIVLV GVSRTSKTPL SMYLAHKRIK VANVPLVPEV
     EPPEEIFQVE KGKVIGLVIN PEQLNQIRTE RLKTLGLKGQ ASYANLERIL EEMEYAQEIM
     KRLGCPVIDV TNRAVEETAS KILEIYYRRL SHV
//