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Database: UniProt
Entry: A0A061F0Y6_THECC
LinkDB: A0A061F0Y6_THECC
Original site: A0A061F0Y6_THECC 
ID   A0A061F0Y6_THECC        Unreviewed;       882 AA.
AC   A0A061F0Y6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=TCM_022491 {ECO:0000313|EMBL:EOY08149.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY08149.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY08149.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
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   EMBL; CM001883; EOY08149.1; -; Genomic_DNA.
DR   EMBL; CM001883; EOY08150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061F0Y6; -.
DR   STRING; 3641.A0A061F0Y6; -.
DR   EnsemblPlants; EOY08149; EOY08149; TCM_022491.
DR   EnsemblPlants; EOY08150; EOY08150; TCM_022491.
DR   Gramene; EOY08149; EOY08149; TCM_022491.
DR   Gramene; EOY08150; EOY08150; TCM_022491.
DR   eggNOG; KOG0470; Eukaryota.
DR   InParanoid; A0A061F0Y6; -.
DR   OMA; IPDYWIK; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000026915; Chromosome 5.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005982; P:starch metabolic process; IBA:GO_Central.
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; 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   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:UP000026915};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          348..720
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          68..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   882 AA;  100638 MW;  84164684FEF28928 CRC64;
     MVYGVSAIRL SCVPSVYRFS QSSFNGARRS SSFSLLLKKD QFSRKIFAQK SSYDSDSSSL
     TVTASEKVLA PGGQGDGSSS LTGQLESPST ISDDPQVTHD VDGNEMEDDE KVEVEEQESV
     PSALANNDEE ACNEEPSVPL HMKVSTEKSE AKPRSIPPPG AGQKIYEIDP TLLGFREHLD
     YRYAQYKRMR EAIDKYEGGL EVFSRGYEKL GFTRSETGIT YREWAPGAKS AALIGDFNNW
     NPNADIMSQN EFGVWEIFLP NNADGSPPIP HGSRVKIHME TPSGIKDSIP AWIKFSVQAP
     GEIPYSGIYY DPQEEEKYVF KHPQPKRPKS LRIYESHVGM SSTEPIINTY ANFRDDVLPR
     IKRLGYNAVQ IMAIQEHSYY ASFGYHVTNF FAPSSRFGTP DDLKSLIDRA HELGLLVLMD
     IVHSHASNNV LDGLNMFDGT DGHYFHLGSR GHHWMWDSRL FNYESWEVLR FLLSNARWWL
     EEYKFDGFRF DGVTSMMYTH HGLEVAFTGN YNEYFGFATD VDAVVYLMLV NDMIHGLYPE
     AVTIGEDVSG MPTFCLPVQD GGVGFDYRLQ MAIADKWIEI LKKRDEDWKM GNIIHTLTNR
     RWLEKCVAYA ESHDQALVGD KTLAFWLMDK DMYDFMALDR PSTPRIDRGI ALHKMIRLIT
     MGLGGEGYLN FMGNEFGHPE WIDFPRGEQH LPNGSVIPGN NCSYDKCRRR FDLGDADYLR
     YRGMQEFDQA MQHLEAKYGF MTSEHQYISR KNEGDRMIVF ERGNLVFVFN FHWINSYFDY
     RVGCLKPGKY KIVLDSDDPL FGGFNRLDHN AEYFSTEGWY DDRPRSFLVY APSRTAVVYA
     LVEDEPEAVG KPEPVQKIET VEEEAEAVEE LEPRKESEPL EG
//
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