ID A0A3B6TLV6_WHEAT Unreviewed; 914 AA.
AC A0A3B6TLV6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CFC21_109914 {ECO:0000313|EMBL:KAF7109699.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7D02G344000.1};
RN [1] {ECO:0000313|EMBL:KAF7109699.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7109699.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS7D02G344000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7D02G344000.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS7D02G344000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7109699.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7109699.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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}.
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DR EMBL; CM022231; KAF7109699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6TLV6; -.
DR STRING; 4565.A0A3B6TLV6; -.
DR PaxDb; 4565-Traes_7DL_E638906EF-1; -.
DR EnsemblPlants; TraesCS7D02G344000.1; TraesCS7D02G344000.1; TraesCS7D02G344000.
DR Gramene; TraesCS7D02G344000.1; TraesCS7D02G344000.1; TraesCS7D02G344000.
DR Gramene; TraesCS7D03G0811600.1; TraesCS7D03G0811600.1.CDS; TraesCS7D03G0811600.
DR Gramene; TraesKAR7D01G0318800.1; cds.TraesKAR7D01G0318800.1; TraesKAR7D01G0318800.
DR Gramene; TraesROB_scaffold_029117_01G000200.1; TraesROB_scaffold_029117_01G000200.1; TraesROB_scaffold_029117_01G000200.
DR OMA; HWDPPPE; -.
DR OrthoDB; 349883at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000019116; Chromosome 7D.
DR Proteomes; UP000815260; Chromosome 7D.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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 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; 2.
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:SF4; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME 3, 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:UP000019116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 400..741
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 45..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 104889 MW; 4D92BA9CFA24A72B CRC64;
MASCPLFLLA PQPPPPLVAA RHCRSPLAGS AHPLTSCRAP RLRRRQSCRC SSSPSSSSSS
SSGPRERSPR PRQRKQRTEQ RPGSGSAVDP VGFLVKTGVS DRAFAQFLRD RHKALKDRRW
ELYSRFIDLK EGSSGYELLG MHRHRQHRVD FMDWAPGARY CSLIGDFNQW SATENCAREG
HLGHDDFGYW FVILEDKLRE GQEPDEYFFQ EYNYVDDYDK GDNGVDAKDL IRRMNEEYWE
PGEVTSRKSR WETVAKLYEQ MFGPNGPQTE EELGEIPDAE TRYKNWKATQ KDESSSSSPS
YDIIDTGQEF DIFNVVTDRA SFEKFQAKAT PLAYWVEMRK GRKAWIEKYV PAISHKDKYR
IYFNTPDGAL ERVPAWATYV LPDAEGMQSY AVHWEPPPEE IYKWRFGRPK VKGSLRIYEC
HVGISGSEQK ISSFQEFTSN VLPHIKNAGY NAVQIIGVLE HKDYSSVGYK VTNYFAVSSR
FGTPDDFKKL VDEAHGLGLL VLIDIVHSYA SADEMVGLSL FDGSNDCYFH SGKRGHHKYW
GTRMFKYDDV DVLHFLLSNL SWWVTEYKID GFQFHSLSSM LYTHNGFSTF TGAIEEYCNQ
YVDKDALIYL ILANEMLHEL HPDIITIAED ATYYPGLCEP TTQGGLGFDY WANLSIPEMW
LWHLENVPER EWSMNKIMKV LISSNHHMLS YVENHNQSIS GRKSFAEIIL NTGMCSSGSV
DDDLIFKASS LLKIIKLITF TTSGGAYLNF MGNEFAHPKR VEFPMSSNEY SFHLACRQWE
LLDKGVHKHI FNFDKDIMSL DENERVTSRG SLNVHHCDDT NMVISFTRGP FLFVFNFNPE
VPYQLYRVGV DEAGEYQLIL NTDETKYGGR GELKSSQYMK KTSDRRADGC RNSLELALAS
RSAQVYKLVR ILRI
//
