ID GLGB1_PEA Reviewed; 922 AA. AC Q41058; DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 103. DE RecName: Full=1,4-alpha-glucan-branching enzyme 1, chloroplastic/amyloplastic; DE EC=2.4.1.18; DE AltName: Full=Starch branching enzyme I; DE Flags: Precursor; GN Name=SBEI; OS Pisum sativum (Garden pea) (Lathyrus oleraceus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-65, FUNCTION, CATALYTIC RP ACTIVITY, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RX PubMed=7894509; DOI=10.1046/j.1365-313x.1995.07010003.x; RA Burton R.A., Bewley J.D., Smith A.M., Bhattacharyya M.K., Tatge H., RA Ring S., Bull V., Hamilton W.D., Martin C.; RT "Starch branching enzymes belonging to distinct enzyme families are RT differentially expressed during pea embryo development."; RL Plant J. 7:3-15(1995). RN [2] RP IDENTIFICATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=2153053; DOI=10.1016/0092-8674(90)90721-p; RA Bhattacharyya M.K., Smith A.M., Ellis T.H., Hedley C., Martin C.; RT "The wrinkled-seed character of pea described by Mendel is caused by a RT transposon-like insertion in a gene encoding starch-branching enzyme."; RL Cell 60:115-122(1990). CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages CC in starch by scission of a 1,4-alpha-linked oligosaccharide from CC growing alpha-1,4-glucan chains and the subsequent attachment of the CC oligosaccharide to the alpha-1,6 position. May preferentially transfer CC short chains during branching. Responsible for the synthesis of about CC 75% of the amylopectin found in the starch granules of mature embryos. CC {ECO:0000269|PubMed:7894509}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18; CC Evidence={ECO:0000269|PubMed:7894509}; CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast CC {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stipules, pods and CC flowers. {ECO:0000269|PubMed:7894509}. CC -!- DEVELOPMENTAL STAGE: Highly expressed during early stages of embryo CC development. Decreasing expression during the embryo maturation. CC {ECO:0000269|PubMed:2153053, ECO:0000269|PubMed:7894509}. CC -!- DISRUPTION PHENOTYPE: Wrinkled seeds. {ECO:0000269|PubMed:2153053}. CC -!- MISCELLANEOUS: The wrinkled seeds phenotype (rr) studied by Mendel in CC 1866 is probably caused by an 800 bp insertion in the SBEI gene, CC leading to the loss of the last 61 amino acids of the protein and a CC complete absence of activity. {ECO:0000305|PubMed:2153053}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB CC subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On the garden pea - Issue CC 159 of April 2014; CC URL="https://web.expasy.org/spotlight/back_issues/159/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X80009; CAA56319.1; -; mRNA. DR PIR; T06493; T06493. DR AlphaFoldDB; Q41058; -. DR SMR; Q41058; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblPlants; Psat3g034640.1; Psat3g034640.1.cds; Psat3g034640. DR Gramene; Psat3g034640.1; Psat3g034640.1.cds; Psat3g034640. DR UniPathway; UPA00152; -. DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IMP:UniProtKB. DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB. DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd11321; AmyAc_bac_euk_BE; 1. DR CDD; cd02854; E_set_GBE_euk_N; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR004193; Glyco_hydro_13_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1. DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR Pfam; PF02922; CBM_48; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 1: Evidence at protein level; KW Amyloplast; Chloroplast; Direct protein sequencing; Plastid; Transferase; KW Transit peptide. FT TRANSIT 1..47 FT /note="Chloroplast" FT /evidence="ECO:0000269|PubMed:7894509" FT CHAIN 48..922 FT /note="1,4-alpha-glucan-branching enzyme 1, FT chloroplastic/amyloplastic" FT /id="PRO_5000146301" FT REGION 83..130 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 870..922 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 106..130 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 896..922 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 494 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 549 FT /note="Proton donor" FT /evidence="ECO:0000250" SQ SEQUENCE 922 AA; 105227 MW; 4EDBF9374C6385C8 CRC64; MVYTISGIRF PVLPSLHKST LRCDRRASSH SFFLKNNSSS FSRTSLYAKF SRDSETKSST IAESDKVLIP EDQDNSVSLA DQLENPDITS EDAQNLEDLT MKDGNKYNID ESTSSYREVG DEKGSVTSSS LVDVNTDTQA KKTSVHSDKK VKVDKPKIIP PPGTGQKIYE IDPLLQAHRQ HLDFRYGQYK RIREEIDKYE GGLDAFSRGY EKFGFTRSAT GITYREWAPG AKSAALVGDF NNWNPNADVM TKDAFGVWEI FLPNNADGSP PIPHGSRVKI HMDTPSGIKD SIPAWIKFSV QAPGEIPYNG IYYDPPEEEK YVFKHPQPKR PQSIRIYESH IGMSSPEPKI NTYANFRDDV LPRIKKLGYN AVQIMAIQEH SYYASFGYHV TNFFAPSSRF GTPEDLKSLI DRAHELGLLV LMDIVHSHSS NNTLDGLNMF DGTDGHYFHP GSRGYHWMWD SRLFNYGSWE VLRYLLSNAR WWLDEYKFDG FRFDGVTSMM YTHHGLQVSF TGNYSEYFGL ATDVEAVVYM MLVNDLIHGL FPEAVSIGED VSGMPTFCLP TQDGGIGFNY RLHMAVADKW IELLKKQDED WRMGDIVHTL TNRRWLEKCV VYAESHDQAL VGDKTLAFWL MDKDMYDFMA LDRPSTPLID RGIALHKMIR LITMGLGGEG YLNFMGNEFG HPEWIDFPRG EQHLPNGKIV PGNNNSYDKC RRRFDLGDAD YLRYHGMQEF DRAMQHLEER YGFMTSEHQY ISRKNEGDRV IIFERDNLVF VFNFHWTNSY SDYKVGCLKP GKYKIVLDSD DTLFGGFNRL NHTAEYFTSE GWYDDRPRSF LVYAPSRTAV VYALADGVES EPIELSDGVE SEPIELSVGV ESEPIELSVE EAESEPIERS VEEVESETTQ QSVEVESETT QQSVEVESET TQ //