※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||
Theoretical PI | 4.61 | ||||||||||||||||||||||||||||||
Molecular Weight | 37480.1 | ||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||
Protein Name | 3'(2'),5'-bisphosphate nucleotidase; 3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase; DPNPase | ||||||||||||||||||||||||||||||
Gene Name | Os12g0183300; LOC_Os12g08280 | ||||||||||||||||||||||||||||||
Created Date | 2007-07-24 | ||||||||||||||||||||||||||||||
Organism | Oryza sativa subsp. japonica(Rice) | ||||||||||||||||||||||||||||||
NCBI Taxa ID | 39947 | ||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Sequence Annotation chain 1 358 3'(2'),5'-bisphosphate nucleotidase region of interest 142 145 Substrate binding metal ion-binding site 78 Magnesium 1 metal ion-binding site 140 Magnesium 1 metal ion-binding site 140 Magnesium 2 metal ion-binding site 142 Magnesium 1; via carbonyl oxygen metal ion-binding site 143 Magnesium 2 metal ion-binding site 292 Magnesium 2 binding site 78 Substrate binding site 292 Substrate Keyword Complete proteome,Hydrolase,Magnesium,Metal-binding,Reference proteome Sequence Source UniProt Protein Sequence MSQAAGNPYA AELAAAKKAV TLAARLCQAV QKDILQSGVQ SKADQSPVTV ADYGSQILVS 60 LVLKMEAPAS SSFSMVAEED SEELRKEGAE EILENITELV NETIVDDGTY SIYFSKEGIL 120 SAIDDGKSEG GPSGRHWVLD PIDGTKGFLR GDQYAIALAL LDEGKVVLGV LACPNLSLGS 180 IGNLNGGSSG DQVGALFSAT IGCGAEVESL QGSPAQKISV CSIDNPVEAS FFESYEGAHS 240 LRDLTGSIAE KLGVQAPPVR IDSQAKYGAL ARGDGAIYLR FPHKGYREKI WDHAAGSIVV 300 TEAGGLVTDA SGNDLDFSKG RFLDLDTGII ATNKQLMPSL LKAVQDAIKE QNQAASPL 358 Gene Ontology GO:0008441; F: 3'(2'),5'-bisphosphate nucleotidase activity; IEA: UniProtKB-EC GO:0046872; F: metal ion binding; IEA: UniProtKB-KW GO:0046854; P: phosphatidylinositol phosphorylation; IEA: InterPro GO:0006790; P: sulfur compound metabolic process; IEA: InterPro Interpro Pfam Pfam; PF00459; Inositol_P SMART PROSITE PRINTS PR00377; IMPHPHTASES |