ID A0A0E0DDT1_9ORYZ Unreviewed; 839 AA.
AC A0A0E0DDT1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-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 meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI04G10300.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI04G10300.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI04G10300.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI04G10300.1}
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; A0A0E0DDT1; -.
DR STRING; 40149.A0A0E0DDT1; -.
DR EnsemblPlants; OMERI04G10300.1; OMERI04G10300.1; OMERI04G10300.
DR Gramene; OMERI04G10300.1; OMERI04G10300.1; OMERI04G10300.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011131_2_1_1; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000008021; Chromosome 4.
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:UP000008021};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 343..703
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 55..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 486
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 541
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 839 AA; 94679 MW; F113D26CB028C60C CRC64;
MASFAVSGAR LGVVRAGGGG GGGPAARSGG LDLPSVLFRR KDSFSRGVVS CAGAPGKVLL
PGGGSDDLLS SAEPDVETQE QPEESQIPDD DKVKPFEEEE EIPAVAEASI KVVAEDKLES
SEVIQDIEEN VTEGVIKDAD EPTVEDKPRV IPPPGDGQKI YQIDPMLEGF RNHLDYRYSE
YKRMRAAIDQ HEGGLDAFSR GYEKLGFTRS TEGITYREWA PGAQSAALVG DFNNWNPNAD
TMTRNEYGVW EISLPNNADG SPAIPHGSRV KIRMDTPSGV KDSIPAWIKF AVQAPGEIPY
NGIYYDPPEE EKYVFQHPQP KRPNSLRIYE SHIGMSSPEP KINTYANFRD EVLPRIKKLG
YNAVQIMAIQ EHSYYASFGY HVTNFFAPSS RFGTPEDLKS LIDKAHELGL LVLMDIVHSH
ASNNTLDGLN GFDGTDTHYF HGGPRGHHWM WDSRLFNYGS WEVLRYLLSN ARWWLEEYKF
DGFRFDGVTS MMYTHHGLQV AFTGNYGEYF GFATDVDAVV YLMLVNDLIH GLYPEAVAIG
EDVSGMPTFC IPVQDGGVGF DYRLHMAVPD KWIELLKQSD EYWKMGDIVH TLTNRRWSEK
CVTYAESHDQ ALVGDKTIAF WLMDKDMYDF MALDRPSTPR IDRGIALHKM IRLVTMGLGG
EGYLNFMGNE FGHPEWIDFP RGPQSLPNGS VLPGNNYSFD KCRRRFDLGD ADYLRYHGMQ
EFDQAMQHLE EKYGFMTSEH QYISRKHEED KVIIFERGDL VFVFNFHWSN SYFDYRVGGL
KPGKYKIVLD SDDGLFGGFS RLDHDAEYFT ADWPHDNRPC SFSVYTPSRT AVVYALTED
//
