ID A0A0E0AEL8_9ORYZ Unreviewed; 818 AA.
AC A0A0E0AEL8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:OGLUM06G29370.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G29370.1}
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:OGLUM06G29370.1}
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; A0A0E0AEL8; -.
DR STRING; 40148.A0A0E0AEL8; -.
DR EnsemblPlants; OGLUM06G29370.1; OGLUM06G29370.1; OGLUM06G29370.
DR Gramene; OGLUM06G29370.1; OGLUM06G29370.1; OGLUM06G29370.
DR eggNOG; KOG0470; Eukaryota.
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 261..628
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 464
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 818 AA; 92995 MW; F2B55DA0EAD639B1 CRC64;
MLCLTSSSSS APAPLLPSLA DRPSPGIAGG GGNVRLSVVS SPRRSWPGKV KTNFSVPATA
RKNKTMVTVV EEVDHLPIYD LDPKLEEFKD HFNYRIKRYL DQKCLIEKHE GGLEEFSKGY
LKFGINTVDG ATIYREWAPA AQEAQLIGEF NNWNGAKHKM EKDKFGIWSI KISHVNGKPA
IPHNSKVKFR FRHGGGAWVD RIPAWIRYAT FDASKFGAPY DGVHWDPPAC ERYVFKHPRP
PKPDAPRIYE AHVGMSGEEP EVRTYREFAD NVLPRIRANN YNTVQLMAIM EHSYYASFGY
HVTNFFAVSS RSGTPEDLKY LVDKAHSLGL RVLMDVVHSH ASNNVTDGLN GYDVGQNTHE
SYFHTGDRGY HKLWDSRLFN YANWEVLRFL LSNLRYWMDE FMFDGFRFDG VTSMLYHHHG
INKGFTGNYK EYFSLDTDVD AIVYMMLANH LMHKLLPEAT IVAEDVSGMP VLCRPVDEGG
VGFDFRLAMA IPDRWIDYLK NKEDRKWSMS EIVQTLTNRR YTEKCIAYAE SHDQSIVGDK
TIAFLLMDKE MYTGMSDLQP ASPTINRGIA LQKMIHFITM ALGGDGYLNF MGNEFGHPEW
IDFPREGNNW SYDKCRRQWS LVDTDHLRYK VVPKYINYMN AFDQAMNALE EEFSFLSSSK
QIVSDMNEKD KVIVFERGDL VFVFNFHPNK TYKGYKVGCD LPGKYRVALD SDALVFGGHG
RVGHDVDHFT SPEGMPGVPE TNFNNRPNSF KVLSPPRTCV AYYRVDEDRE ELRRGGAVAS
GKIVTGYIDV EATSGETISG GWKGSEKDDC GKKGMKFD
//
