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Database: UniProt
Entry: A0A1G5UI27_9SPHN
LinkDB: A0A1G5UI27_9SPHN
Original site: A0A1G5UI27_9SPHN 
ID   A0A1G5UI27_9SPHN        Unreviewed;       269 AA.
AC   A0A1G5UI27;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Putative pyruvate, phosphate dikinase regulatory protein {ECO:0000256|HAMAP-Rule:MF_00921};
DE            Short=PPDK regulatory protein {ECO:0000256|HAMAP-Rule:MF_00921};
DE            EC=2.7.11.32 {ECO:0000256|HAMAP-Rule:MF_00921};
DE            EC=2.7.4.27 {ECO:0000256|HAMAP-Rule:MF_00921};
GN   ORFNames=SAMN03159340_02857 {ECO:0000313|EMBL:SDA33169.1};
OS   Sphingomonas sp. NFR15.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1566282 {ECO:0000313|EMBL:SDA33169.1, ECO:0000313|Proteomes:UP000199327};
RN   [1] {ECO:0000313|Proteomes:UP000199327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR15 {ECO:0000313|Proteomes:UP000199327};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00921};
CC   -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC       regulatory protein family. PDRP subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00921}.
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DR   EMBL; FMWX01000006; SDA33169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5UI27; -.
DR   STRING; 1566282.SAMN03159340_02857; -.
DR   OrthoDB; 9782201at2; -.
DR   Proteomes; UP000199327; Unassembled WGS sequence.
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_00921; PDRP; 1.
DR   InterPro; IPR005177; Kinase-pyrophosphorylase.
DR   InterPro; IPR026565; PPDK_reg.
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_00921};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00921}; Reference proteome {ECO:0000313|Proteomes:UP000199327};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|HAMAP-Rule:MF_00921};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00921}.
FT   BINDING         148..155
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00921"
SQ   SEQUENCE   269 AA;  29688 MW;  3178815FF4B4A983 CRC64;
     MRLHLHLLSD STGETLENIA KAALAQYDDV ETIRHFWPMV RTEGHLERIL QEISQNPGLV
     LFTLVNSETR RNLEMRCRAL GLPAVAPLDA VTGALSSLLG QQAKARPGRQ HMLDAAYFAR
     VDAIQFTIAH DDGLGSEDWE EADIVLAGVS RSSKTPTSIY LANRGYKTAN IPIVVESPPP
     PVLFALKRPL VVGLTTSADR LIQVRRNRLL SLNQAPETAY VDHEAVSREV AWARRMFADN
     GWPVIDVTRR SIEETAAAII ALVAERGEA
//
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