CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014819
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate, phosphate dikinase 1, chloroplastic 
Protein Synonyms/Alias
 OsPPDKB; Pyruvate, orthophosphate dikinase 1 
Gene Name
 PPDK1 
Gene Synonyms/Alias
 CPDK1; PPDKB; Os05g0405000; LOC_Os05g33570; OJ1174_H11.5; OsJ_017742 
Created Date
 July 27, 2013 
Organism
 Oryza sativa subsp. japonica (Rice) 
NCBI Taxa ID
 39947 
Lysine Modification
Position
Peptide
Type
References
664SSLELRQKALDRLLPubiquitination[1]
Reference
 [1] Proteomic analysis of salt-responsive ubiquitin-related proteins in rice roots.
 Liu CW, Hsu YK, Cheng YH, Yen HC, Wu YP, Wang CS, Lai CC.
 Rapid Commun Mass Spectrom. 2012 Aug 15;26(15):1649-60. [PMID: 22730086
Functional Description
 Formation of phosphoenolpyruvate. The cytoplasmic isoform supports the biosynthetic processes in the nascent endosperm and provides an efficient mechanism for glycolytic ATP synthesis in oxygen depleted tissues. May be involved in regulating the flux of carbon into starch and fatty acids of seeds and in the remobilization of nitrogen reserves in senescing leaves. 
Sequence Annotation
 ACT_SITE 529 529 Tele-phosphohistidine intermediate (By
 ACT_SITE 907 907 Proton donor (By similarity).
 METAL 821 821 Magnesium (By similarity).
 METAL 845 845 Magnesium (By similarity).
 BINDING 635 635 Substrate (By similarity).
 BINDING 692 692 Substrate (By similarity).
 BINDING 821 821 Substrate (By similarity).
 BINDING 842 842 Substrate; via carbonyl oxygen (By
 BINDING 843 843 Substrate; via amide nitrogen (By
 BINDING 844 844 Substrate (By similarity).
 BINDING 845 845 Substrate; via amide nitrogen (By
 MOD_RES 527 527 Phosphothreonine; by PDRP1.  
Keyword
 Alternative promoter usage; ATP-binding; Chloroplast; Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Photosynthesis; Plastid; Pyruvate; Reference proteome; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 947 AA 
Protein Sequence
MPSVSRAVCV QRASGNNGRR CRDGAAAAGR RSVVAQRARH GKPEVAIRSG SGGSARGGHC 60
SPLRAVAAPI PTTKKRVFHF GKGKSEGNKA MKDLLGGKGA NLAEMASIGL SVPPGFTVST 120
EACQQYQAAG KTLPAGLWEE IVEGLQWVEE YMAARLGDPA RPLLLSVRSG AAVSMPGMMD 180
TVLNLGLNDE VAAGLAAKSG DRFAYDSYRR FLDMFGNVVM DIPHALFEEK LEAMKAVKGL 240
HNDTDLTATD LKELVAQYKD VYVEAKGEPF PSDPKKQLQL AVLAVFNSWD SPRAIKYRSI 300
NKITGLKGTA VNVQTMVFGN MGNTSGTGVL FTRNPSTGEK KLYGEFLVNA QGEDVVAGIR 360
TPEDLDAMRD HMPEPYEELV ENCKILESHY KEMMDIEFTV QENRLWMLQC RTGKRTGKGA 420
VKIAVDMVNE GLVERRTALK MVEPGHLDQL LHPQFENPSG YKDKVIATGL PASPGAAVGQ 480
IVFTAEDAEA WHAQGKDVIL VRTETSPEDV GGMHAAVGIL TARGGMTSHA AVVARGWGKC 540
CVSGCSSVRV NDASKIVVIE DKALHEGEWL SLNGSTGEVI IGKQPLCPPA LSGDLETFMS 600
WVDEVRKLKV MANADTPEDA TTARQNGAEG IGLCRTEHMF FASDERIKAV RQMIMASSLE 660
LRQKALDRLL PYQRSDFEGI FRAMDGLPVT IRLLDPPLHE FLPEGHVEDM VRELCSETGA 720
AQDDVLARVE KLSEVNPMLG FRGCRLGISY PELTEMQARA IFEAAITMTN QGIQVFPEIM 780
VPLVGTPQEL GHQVDVIRQI ANKVFTDMGK TIGYKVGTMI EIPRAALVAD EIAEQAEFFS 840
FGTNDLTQMT FGYSRDDVGK FLPIYLSQGI LQHDPFEVLD QRGVGELVKL ATERGRKARP 900
NLKVGICGEH GGEPLSVAFF AKAGLDYVSC SPFRVPIARL AAAQVLL 947 
Gene Ontology
 GO:0009570; C:chloroplast stroma; IEA:EnsemblPlants/Gramene.
 GO:0005634; C:nucleus; IEA:EnsemblPlants/Gramene.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:EC.
 GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
 GO:0006090; P:pyruvate metabolic process; IEA:InterPro. 
Interpro
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR008279; PEP-util_enz_mobile_dom.
 IPR018274; PEP_util_AS.
 IPR000121; PEP_util_C.
 IPR023151; PEP_util_CS.
 IPR002192; PPDK_PEP-bd.
 IPR010121; Pyruvate_phosphate_dikinase.
 IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. 
Pfam
 PF00391; PEP-utilizers
 PF02896; PEP-utilizers_C
 PF01326; PPDK_N 
SMART
  
PROSITE
 PS00742; PEP_ENZYMES_2
 PS00370; PEP_ENZYMES_PHOS_SITE 
PRINTS