※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||
Theoretical PI | 8.45 | ||||||||||||||||||||||||||||||
Molecular Weight | 41760.3 | ||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||
Protein Name | Sedoheptulose-1,7-bisphosphatase, chloroplastic; SED(1,7)P2ase; Sedoheptulose bisphosphatase; SBPase | ||||||||||||||||||||||||||||||
Gene Name | CSBP | ||||||||||||||||||||||||||||||
Created Date | 1995-11-01 | ||||||||||||||||||||||||||||||
Organism | Chlamydomonas reinhardtii(Chlamydomonas smithii) | ||||||||||||||||||||||||||||||
NCBI Taxa ID | 3055 | ||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description Sequence Annotation transit peptide 1 Chloroplast chain 389 Sedoheptulose-1,7-bisphosphatase, chloroplastic region of interest 176 179 Substrate binding metal ion-binding site 126 Magnesium 1 metal ion-binding site 155 Magnesium 1 metal ion-binding site 155 Magnesium 2 metal ion-binding site 173 Magnesium 2 metal ion-binding site 173 Magnesium 3 metal ion-binding site 175 Magnesium 2; via carbonyl oxygen metal ion-binding site 176 Magnesium 3 metal ion-binding site 323 Magnesium 3 binding site 287 Substrate binding site 317 Substrate disulfide bond 115 120 Redox-active (light-modulated) Keyword 3D-structure,Calvin cycle,Carbohydrate metabolism,Chloroplast,Disulfide bond,Hydrolase,Magnesium,Metal-binding,Plastid,Transit peptide Sequence Source UniProt Protein Sequence MAAMMMRQKV AGAIAGERRS AVAPKMGRAA TAPVVVASAN ASAFKGAAVT ARVKASTRAA 60 RVQSRRTAVL TQAKIGDSLA EFLVEATPDP KLRHVMMSMA EATRTIAHKV RTASCAGTAC 120 VNSFGDEQLA VDMVADKLLF EALKYSHVCK LACSEEVPEP VDMGGEGFCV AFDPLDGSSS 180 SDTNFAVGTI FGVWPGDKLT NITGREQVAA GMGIYGPRTV FCIALKDAPG CHEFLLMDDG 240 KWMHVKETTH IGEGKMFAPG NLRATFDNPA YERLINFYLG EKYTLRYTGG IVPDLFQIIV 300 KEKGVFTNLT SPTTKAKLRI LFEVAPLALL IEKAGGASSC DGKAVSALDI PILVCDQRTQ 360 ICYGSIGEVR RFEEYMYGTS PRFSEKVVA 389 Gene Ontology GO:0048046; C: apoplast; IEA: EnsemblPlants/Gramene GO:0009941; C: chloroplast envelope; IEA: EnsemblPlants/Gramene GO:0009570; C: chloroplast stroma; IEA: EnsemblPlants/Gramene GO:0009579; C: thylakoid; IEA: EnsemblPlants/Gramene GO:0042132; F: fructose 1,6-bisphosphate 1-phosphatase activity; IEA: InterPro GO:0046872; F: metal ion binding; IEA: UniProtKB-KW GO:0050278; F: sedoheptulose-bisphosphatase activity; IEA: UniProtKB-EC GO:0042742; P: defense response to bacterium; IEA: EnsemblPlants/Gramene GO:0019253; P: reductive pentose-phosphate cycle; IEA: UniProtKB-UniPathway GO:0019252; P: starch biosynthetic process; IEA: EnsemblPlants/Gramene GO:0005986; P: sucrose biosynthetic process; IEA: EnsemblPlants/Gramene Interpro Pfam Pfam; PF00316; FBPase SMART PROSITE PS00124; FBPASE PRINTS PR01958; S17BPHPHTASE |