PDRP1_ORYSI
ID PDRP1_ORYSI Reviewed; 471 AA.
AC A2YM35;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Probable pyruvate, phosphate dikinase regulatory protein, chloroplastic;
DE EC=2.7.11.32;
DE EC=2.7.4.27;
DE AltName: Full=Bifunctional dikinase regulatory protein;
DE Short=BFRP;
DE AltName: Full=Pyruvate, Pi dikinase regulatory protein;
DE Short=PPDK RP;
DE Short=PPDK regulatory protein;
DE Flags: Precursor;
GN Name=PDRP1; ORFNames=OsI_025378;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC involved in the dark/light-mediated regulation of PPDK by catalyzing
CC its phosphorylation/dephosphorylation. Dark/light-induced changes in
CC stromal concentrations of the competing ADP and Pi substrates govern
CC the direction of the reaction. In the dark, phosphorylates the
CC catalytic intermediate of PPDK (PPDK-HisP), inactivating it. Light
CC exposure induces the phosphorolysis reaction that reactivates PPDK (By
CC similarity). {ECO:0000250}.
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;
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 -!- ACTIVITY REGULATION: Regulated by light/dark exposure. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC regulatory protein family. PDRP subfamily. {ECO:0000305}.
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DR EMBL; CM000132; EAZ04146.1; -; Genomic_DNA.
DR AlphaFoldDB; A2YM35; -.
DR SMR; A2YM35; -.
DR STRING; 39946.A2YM35; -.
DR PRIDE; A2YM35; -.
DR EnsemblPlants; BGIOSGA025853-TA; BGIOSGA025853-PA; BGIOSGA025853.
DR Gramene; BGIOSGA025853-TA; BGIOSGA025853-PA; BGIOSGA025853.
DR HOGENOM; CLU_046206_0_0_1; -.
DR OMA; YAQCEFE; -.
DR Proteomes; UP000007015; Chromosome 7.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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 InterPro; IPR017409; Pyrv_Pi_dikinase_reg_chlpt.
DR PANTHER; PTHR31756; PTHR31756; 1.
DR Pfam; PF03618; Kinase-PPPase; 1.
DR PIRSF; PIRSF038149; Pyruvate_Pi_dikinase_regulator; 1.
PE 3: Inferred from homology;
KW Chloroplast; Kinase; Nucleotide-binding; Plastid; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..471
FT /note="Probable pyruvate, phosphate dikinase regulatory
FT protein, chloroplastic"
FT /id="PRO_0000342601"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171..178
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255"
SQ SEQUENCE 471 AA; 51076 MW; C5B9D37BB49195BE CRC64;
MSSSSSTSPR FGSMISAKLA SPPPSLLLPP SPRLQGRRLT PPSCTPGTPA ALPSPGPDKE
PEREAAGSGS GSATTPRSPA QLGSSQLHRW SRARAHRSGR RLEWPTIRDR GSGGASSPPT
PTRPHPSSDE AASAAAKVAV EEEDGYGVVG RDEAAKSIYM VSDGTGWTAE HSVNAALGQF
EHCLVDRGCA VNTHLFNGID DMDRLIEIVK QAAKEGALVL YTLADPSMAE ATKKACELWG
VPSNDILRPT IEAIASHIGV APSGIPRSSP SRKGQLTEDY FRRIEAIDFT IKQDDGAQPQ
NLNRAHIVLV GVSRTGKTPL SIYLAQKGYK VANVPIVMGV NLPKSLFEID QDKIFGLTIN
PVVLQAIRKA RAKTLGFHGQ KSNYAEMEHV RGELDHANQI FAQHPIWPVI EVTGKAIEET
AAVVVRIFHD RKQKCAMPRI SKRVAPIRIY DYLSEMVNTH VEYQKIFARD F
