ID A0A0E0AEM2_9ORYZ Unreviewed; 762 AA.
AC A0A0E0AEM2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:OGLUM06G29370.5};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G29370.5}
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:OGLUM06G29370.5}
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}.
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 AlphaFoldDB; A0A0E0AEM2; -.
DR EnsemblPlants; OGLUM06G29370.5; OGLUM06G29370.5; OGLUM06G29370.
DR Gramene; OGLUM06G29370.5; OGLUM06G29370.5; OGLUM06G29370.
DR HOGENOM; CLU_011131_2_2_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:SF2; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME, CHLOROPLASTIC_AMYLOPLASTIC; 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 Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 196..563
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 399
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 762 AA; 87446 MW; 4691C382A70B664E CRC64;
MVTVVEEVDH LPIYDLDPKL EEFKDHFNYR IKRYLDQKCL IEKHEGGLEE FSKGYLKFGI
NTVDGATIYR EWAPAAQEAQ LIGEFNNWNG AKHKMEKDKF GIWSIKISHV NGKPAIPHNS
KVKFRFRHGG GAWVDRIPAW IRYATFDASK FGAPYDGVHW DPPACERYVF KHPRPPKPDA
PRIYEAHVGM SGEEPEVRTY REFADNVLPR IRANNYNTVQ LMAIMEHSYY ASFGYHVTNF
FAVSSRSGTP EDLKYLVDKA HSLGLRVLMD VVHSHASNNV TDGLNGYDVG QNTHESYFHT
GDRGYHKLWD SRLFNYANWE VLRFLLSNLR YWMDEFMFDG FRFDGVTSML YHHHGINKGF
TGNYKEYFSL DTDVDAIVYM MLANHLMHKL LPEATIVAED VSGMPVLCRP VDEGGVGFDF
RLAMAIPDRW IDYLKNKEDR KWSMSEIVQT LTNRRYTEKC IAYAESHDQS IVGDKTIAFL
LMDKEMYTGM SDLQPASPTI NRGIALQKMI HFITMALGGD GYLNFMGNEF GHPEWIDFPR
EGNNWSYDKC RRQWSLVDTD HLRYKVVPKY INYMNAFDQA MNALEEEFSF LSSSKQIVSD
MNEKDKVIVF ERGDLVFVFN FHPNKTYKGY KVGCDLPGKY RVALDSDALV FGGHGRVGHD
VDHFTSPEGM PGVPETNFNN RPNSFKVLSP PRTCVAYYRV DEDREELRRG GAVASGKIVT
GYIDVEATSG ETISGGWKGS EKDDCGKKGM KFVFRSSDED CK
//
