ID A0A2G5DTQ4_AQUCA Unreviewed; 795 AA.
AC A0A2G5DTQ4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN ORFNames=AQUCO_01500400v1 {ECO:0000313|EMBL:PIA46826.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA46826.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA46826.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KZ305032; PIA46826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5DTQ4; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000230069; 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 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; 2.
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:UP000230069};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 285..651
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 762..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 481
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 795 AA; 89976 MW; D086AA88CE66489D CRC64;
MMYCFSSSSS SFNLSLSLLP SNKINTKACR DHRCITRRTR AAHGSMEFFG KLSFLSSQTL
TVHGKVERNV AFATLLDNEN PTMTSSQDET ENIAIMGLDP GLEGFKDHLK YRTQKYVEQK
NLIENFEGSL EDFAQGYLKF GFNRGQDCIV YREWAPAAQE AQLIGDFNGW DGFKHQMEKD
QFGVWTLKIP NSGGTPAIPH NSRVKFRFRH GDGTWVDRIP AWIKYATVDP TKFAAAYDGV
YWDPTPPERY EFKYPRPPKP MSPRIYEAHV GMSSSEPCIN SYREFADNVL PRIQANNYNT
VQLMAVMEHS YYASFGYHVT NFFAVSSRSG TPEDLKYLID KAHSLGLRVL MDVVHSHASN
NVTDGLNGFD VGQSAQESYF HAGDRGYHKL WDSRLFNYAN WEVLRFLLSN LRWWLEEFKF
DGFRFDGVTS MLYHHHGINM AFTGDYNEYF SESTDVDAVV YLMLANLVIH KILPDATVIA
EDVSGMPALG RLVSEGGIGF DYRLAMAIPD KWIDYVMNKK DEEWSMNDIV LTLTNRRYTE
KCISYAESHD QSIVGDKTIA FSLMDKEMYS GMSCLTDASP TVERGVALHK MIHFITMALG
GDGYLIFMGN EFLNAFNRAI NSLDDRFSFL SSTKQIVSSS NEEEKIIVFE RGDLVFVFNF
HPENSYDGYK IGCDLPGKYR VALDSDAWEF GGHGRVAHDV DHFTSPEGIP GVPETNFNGR
PNSFKVLSPP RTCVVYYKVE EDLDDGYGED FTGILDPVTG AVALEENSDK SASSQEDVGP
TPEDMEFQMG DESDD
//
