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Database: UniProt
Entry: A0A0D9ZKE9_9ORYZ
LinkDB: A0A0D9ZKE9_9ORYZ
Original site: A0A0D9ZKE9_9ORYZ 
ID   A0A0D9ZKE9_9ORYZ        Unreviewed;       841 AA.
AC   A0A0D9ZKE9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM04G11360.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM04G11360.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM04G11360.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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:0000256|ARBA:ARBA00000826};
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC       {ECO:0000256|ARBA:ARBA00004602}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR   AlphaFoldDB; A0A0D9ZKE9; -.
DR   STRING; 40148.A0A0D9ZKE9; -.
DR   EnsemblPlants; OGLUM04G11360.1; OGLUM04G11360.1; OGLUM04G11360.
DR   Gramene; OGLUM04G11360.1; OGLUM04G11360.1; OGLUM04G11360.
DR   eggNOG; KOG0470; Eukaryota.
DR   HOGENOM; CLU_011131_2_1_1; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
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:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005983; P:starch catabolic process; IEA:UniProt.
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; 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; 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   PIRSF; PIRSF000463; GlgB; 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   3: Inferred from homology;
KW   Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          345..705
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          57..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        488
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        543
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   841 AA;  94810 MW;  95AF673127CD7406 CRC64;
     MASFAVSGAR LGVVRAGGGG GGGGGPAARS SGVDLPSVLF RRKDSFSRGV VSCAGAPGKV
     LVPGGGSDDL LSSAEPDVET QEQPEESQIP DDNKVKPFEE EEEIPAVAEA SIKVVAEDKL
     ESSEVIQDIE ENVTEGVIKD ADEPTVEDKP RVIPPPGDGQ KIYQIDPMLE GFRNHLDYRY
     SEYKRMRAAI DQHEGGLDAF SRGYEKLGFT RSAEGITYRE WAPGAQSAAL VGDFNNWNPN
     ADTMTRNEYG VWEISLPNNA DGSPAIPHGS RVKIRMDTPS GVKDSIPAWI KFAVQAPGEI
     PYNGIYYDPP EEEKYVFQHP QPKRPNSLRI YESHIGMSSP EPKINTYANF RDEVLPRIKK
     LGYNAVQIMA IQEHSYYASF GYHVTNFFAP SSRFGTPEDL KSLIDKAHEL GLLVLMDIVH
     SHASNNTLDG LNGFDGTDTH YFHGGPRGHH WMWDSRLFNY GSWEVLRYLL SNARWWLEEY
     KFDGFRFDGV TSMMYTHHGL QVAFTGNYGE YFGFATDVDA VVYLMLVNDL IHGLYPEAVA
     IGEDVSGMPT FCIPVQDGGV GFDYRLHMAV PDKWIELLKQ SDEYWKMGDI VHTLTNRRWS
     EKCVTYAESH DQALVGDKTI AFWLMDKDMY DFMALDRPST PRIDRGIALH KMIRLVTMGL
     GGEGYLNFMG NEFGHPEWID FPRGPQSLPN GSVLPGNNYS FDKCRRRFDL GDADYLRYHG
     MQEFDQAMQH LEEKYGFMTS EHQYISRKHE EDKVIIFERG DLVFVFNFHW SNSYFDYRVG
     CLKPGKYKIV LDSDDGLFGG FSRLDHDAEY FTADWPHDNR PCSFSVYTPS RTAVVYALTE
     D
//
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