GLGB1_PEA
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 03-AUG-2022, entry version 100.
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).
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/";
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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:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
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; PTHR43651; 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; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 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
