GLGB_SOLTU
ID GLGB_SOLTU Reviewed; 861 AA.
AC P30924;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=1,4-alpha-glucan-branching enzyme;
DE EC=2.4.1.18;
DE AltName: Full=Q-enzyme;
DE AltName: Full=Starch-branching enzyme;
GN Name=SBE1; Synonyms=SBE;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Dianella;
RX PubMed=8278528; DOI=10.1104/pp.102.3.1053;
RA Poulsen P., Kreiberg J.D.;
RT "Starch branching enzyme cDNA from Solanum tuberosum.";
RL Plant Physiol. 102:1053-1054(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 279-527.
RC STRAIN=cv. Desiree; TISSUE=Tuber;
RX PubMed=1745241; DOI=10.1007/bf00290648;
RA Kossmann J., Visser R.G.F., Mueller-Roeber B., Willmitzer L., Sonnewald U.;
RT "Cloning and expression analysis of a potato cDNA that encodes branching
RT enzyme: evidence for co-expression of starch biosynthetic genes.";
RL Mol. Gen. Genet. 230:39-44(1991).
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.
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 -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; X69805; CAA49463.1; -; mRNA.
DR PIR; S34730; S34730.
DR RefSeq; NP_001275183.1; NM_001288254.1.
DR AlphaFoldDB; P30924; -.
DR SMR; P30924; -.
DR STRING; 4113.PGSC0003DMT400025846; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P30924; -.
DR GeneID; 102596498; -.
DR KEGG; sot:102596498; -.
DR InParanoid; P30924; -.
DR OrthoDB; 165238at2759; -.
DR BioCyc; MetaCyc:MON-1885; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P30924; baseline and differential.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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 PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Amyloplast; Chloroplast; Glycosyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase.
FT CHAIN 1..861
FT /note="1,4-alpha-glucan-branching enzyme"
FT /id="PRO_0000188787"
FT ACT_SITE 429
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 484
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 861 AA; 99084 MW; F3D519AC7CF1BEF2 CRC64;
MEINFKVLSK PIRGSFPSFS PKVSSGASRN KICFPSQHST GLKFGSQERS WDISSTPKSR
VRKDERMKHS SAISAVLTDD NSTMAPLEED VKTENIGLLN LDPTLEPYLD HFRHRMKRYV
DQKMLIEKYE GPLEEFAQGY LKFGFNREDG CIVYREWAPA AQEDEVIGDF NGWNGSNHMM
EKDQFGVWSI RIPDVDSKPV IPHNSRVKFR FKHGNGVWVD RIPAWIKYAT ADATKFAAPY
DGVYWDPPPS ERYHFKYPRP PKPRAPRIYE AHVGMSSSEP RVNSYREFAD DVLPRIKANN
YNTVQLMAIM EHSYYGSFGY HVTNFFAVSS RYGNPEDLKY LIDKAHSLGL QVLVDVVHSH
ASNNVTDGLN GFDIGQGSQE SYFHAGERGY HKLWDSRLFN YANWEVLRFL LSNLRWWLEE
YNFDGFRFDG ITSMLYVHHG INMGFTGNYN EYFSEATDVD AVVYLMLANN LIHKIFPDAT
VIAEDVSGMP GLGRPVSEGG IGFDYRLAMA IPDKWIDYLK NKNDEDWSMK EVTSSLTNRR
YTEKCIAYAE SHDQSIVGDK TIAFLLMDKE MYSGMSCLTD ASPVVDRGIA LHKMIHFFTM
ALGGEGYLNF MGNEFGHPEW IDFPREGNNW SYDKCRRQWN LADSEHLRYK FMNAFDRAMN
SLDEKFSFLA SGKQIVSSMD DDNKVVVFER GDLVFVFNFH PKNTYEGYKV GCDLPGKYRV
ALDSDAWEFG GHGRTGHDVD HFTSPEGIPG VPETNFNGRQ IPSKCCLLRE HVWLITELMN
ACQKLKITRQ TFVVSYYQQP ISRRVTRNLK IRYLQISVTL TNACQKLKFT RQTFLVSYYQ
QPILRRVTRK LKDSLSTNIS T