ID A0A0E0K0K5_ORYPU Unreviewed; 804 AA.
AC A0A0E0K0K5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G16910.2};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC02G16910.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC02G16910.2}
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; A0A0E0K0K5; -.
DR EnsemblPlants; OPUNC02G16910.2; OPUNC02G16910.2; OPUNC02G16910.
DR Gramene; OPUNC02G16910.2; OPUNC02G16910.2; OPUNC02G16910.
DR HOGENOM; CLU_011131_2_1_1; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000026962; Chromosome 2.
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; 2.
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:SF13; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME 2, CHLOROPLASTIC_AMYLOPLASTIC; 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:UP000026962};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 329..681
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 452
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 507
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 804 AA; 90455 MW; 6BC7877387108F66 CRC64;
MAAPASAVPG SAAGLRAGAV RFPVPAGARR RGAAELPTSR SLLTGRRFPG AVRVGGYGGR
VAVHAAGASG EVMIPEGESD GMPASAGSDD LQVPALDDEL STEVGAQVEI ESSGASDVEG
VKRVVEELAA EQKPRVVPPT GDGQKIFQMD SMLNGYKYHL EYRYSLYRRL RSDIDQYEGG
LETFSRGYEK FGFNHSAEGV TYREWAPGAH SAALVGDFNN WNPNADRMSK NEFGVWEIFL
PNNADGSSPI PHGSRVKVRM ETPSGIKDSI PAWIKYSVQA AGEIPYNGIY YDPPEEEKYV
FKHPQPKRPK SLRIYETHVG MSSTEPKINT YANFRDEVLP RIKKLGYNAV QIMAIQEHAY
YGSFGYHVTN FFAPSSRFGT PEELNHASNN TLDGLNGFDG TDTHYFHSGS RGHHWMWDSR
LFNYGNWEVL RFLLSNARWW LEEYKFDGFR FDGVTSMMYT HHGLQVAFTG NYSEYFGFAT
DADAVVYLML VNDLIHGLYP EAITIGEDVS GMPTFAVPVQ DGGVGFDYRL HMAVPDKWIE
LLKQSDESWK MGDIVHTLTN RRWSEKCVTY AESHDQALVG DKTIAFWLMD KDMYDFMALD
RPATPSIDRG IALHKMIRLI TMGLGGEGYL NFMGNEFGHP EWIDFPRAPQ VLPNGKFIPG
NNNSYDKCRR RFDLGDADYL RYRGMQEFDR AMQSLEEKYG FMTSDHQYIS RKHEEDKMII
FEKGDLVFVF NFHWSNSYFD YRVGCLKPGK YKVVLDSDAG LFGGFGRIHH SADHFTADCS
HDNRPYSFSV YSPSRTCVVY APAE
//
