Detail Information for IndEnz0001000635
IED ID IndEnz0001000635
Enzyme Type ID amylase000635
Protein Name 1,4-alpha-glucan-branching enzyme 1, chloroplastic/amyloplastic
EC 2.4.1.18
Starch branching enzyme I
Fragment
Gene Name SBEII
Organism Pisum sativum (Garden pea)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade Hologalegina IRL clade Fabeae Pisum Pisum sativum (Garden pea)
Enzyme Sequence ATTTTTTHNSKNKQYLAKQKPVELTLGYQNPNGCKVCSFGSKGSIYQKVSSGFKGVSVMTDDKSTMPSVEEDFENIGILNVDSSLEPFKDHFKYRLKRYLHQKKLIEEYEGGLQEFAKGYLKFGFNREEDGISYREWAPAAQEAQIIGDFNGWNGSNLHMEKDQFGVWSIQIPDADGNPAIPHNSRVKFRFKHSDGVWVDRIPAWIKYATVDPTRFAAPYDGVYWDPPLSERYQFKHPRPPKPKAPRIYEAHVGMSSSEPRINSYREFADDVLPRIRENNYNTVQLMAVMEHSYYASFWYHVTKPFFAVSSRSGSPEDLKYLIDKAHSLGLNVLMDVIHSHASNNVTDGLNGFDVGQSSQQSYFHAGDRGYHKLWDSRLFNYANWKSSFLLSNLRWWLEEYKFDGFRFDGVTSMLYHHHGINMAFTGDYNEYFSEETDVDAVVYLMLANSLVHDILPDATDIAEDVSGMPGLGRPVSEVGIGFDYRLAMAIPDKWIDYLKNKKDSEWSMKEISLNLTNRRYTEKCVSYAESHDQSIVGDKTIAFLLMDEEMYSSMSCLTMLSPTIERGISLHKMIHFITLALGGEGYLNFMGNEFGHPEWIDFPREGNGWSYEKCRLTQWNLVDTNHLRYKFMNAFDRAMNLLDDKFSILASTKQIVSSTNNEDKVIVFERGDLVFVFNFHPENTYEGYKVGCDLPGKYRVALDSDATEFGGHGRVGHDADQFTSPEGIPGIPETNFNNRPNSFKVLSPPHTCVVYYRVDERQEESNNPNLGSVEETFAAADTDVARIPDVSMESEDSNLDRIEDNSEDAVDAGILKVEREVVGDN
Enzyme Length 826
Uniprot Accession Number Q41059
Absorption
Active Site ACT_SITE 409; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 464; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
DNA Binding
EC Number 2.4.1.18
Enzyme Function FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. May preferentially transfer long chains during branching. {ECO:0000269|PubMed:7894509}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan biosynthesis; starch biosynthesis.
nucleotide Binding
Features Active site (2); Chain (1); Compositional bias (1); Non-terminal residue (1); Region (1); Transit peptide (1)
Keywords Amyloplast;Chloroplast;Direct protein sequencing;Plastid;Transferase;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 94,191
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda