ID A0A251V7V9_HELAN Unreviewed; 852 AA.
AC A0A251V7V9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=HannXRQ_Chr03g0076721 {ECO:0000313|EMBL:OTG31534.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG31534.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
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; CM007892; OTG31534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251V7V9; -.
DR STRING; 4232.A0A251V7V9; -.
DR InParanoid; A0A251V7V9; -.
DR OMA; HWDPPPE; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000215914; Chromosome 3.
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 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:UP000215914};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 335..732
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 39..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 98096 MW; D0BAA3A4AFB6636C CRC64;
MTSSLSLLTQ IPLPPTTDGS VGIRSITYRR SVVFPTKKWR CSVSPGQSPP PKHRQRQSKN
PESGEKGIDP VGFLSKSGIT HKGFALYLRE RYKSLKDLKD EILTRHIDFR DMASGFELLG
MHRNVQHRVD FMEWAPGARY CAIVGDFNDW SPTENCAREG HYGHDDYGYW FVILEDKLRD
GEEPDELYFQ QYNYVDDYDK GDSGVTADEV FQKANDEYWE PGEDRFVKSR FEIIAKLYEQ
IGKEYDIFNV IDDPVSKAKF RAKKPPIAYW FETRKGRKAW LKKYAPAIPH GSKYRVYFNT
PNGPLERIPA WATYVNPEAD GNQGYAIHWE PPPEHAYKWK HNSPKVPKSL RIYEAHIGIS
GSEPKIASFS EFTEKVLPYV KDAGYNAIQL IGVVEHKDYF TVGYRVTNMF AVSSRYGTPE
DFKRLVDVAH GLGLLVFMDI VHSYSAADEM VGLSLFDGSN DCYFHTGKRG QHKFWGTRMF
KYEDLDVLHY LLSNLNWWVV EYHVDGFNFH SLASMMYTHN GFASFTGDME EFYNQYVDRS
AILYLILANE ILHTLHPNII TIAEDATLYP GLCEPTSQGG LGFDYFVNPH ASEMWLWFLE
NAQDSSWSMS KIVDTLAGIN RNSNKMLLYT ENHNQSISGG RSFAEILYGQ TLEQSPVMND
LLLRGCSLHK MIRLITYSIS GRAYLNFMGN EFGHPKRVEF PMSSNGFSFS LANRDWDLLA
KEGVHQNLLS FDKDMMDLEK TEKVISRWLP NIHHVNDTNM VISYLRGPFL FIFNFHPTNS
YERYSVGVEE AGEYQVILNS DEKKYSGQGS IGQDQYFRKT ISRRVDGMRN CIEVPLPSRS
AQVYKLTRIL RV
//
