ID B0Y0Q4_ASPFC Unreviewed; 747 AA.
AC B0Y0Q4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=1,4-alpha-glucan-branching enzyme {ECO:0000256|ARBA:ARBA00020932};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
DE AltName: Full=Glycogen-branching enzyme {ECO:0000256|ARBA:ARBA00031979};
GN ORFNames=AFUB_058160 {ECO:0000313|EMBL:EDP51795.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP51795.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP51795.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR EMBL; DS499597; EDP51795.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y0Q4; -.
DR EnsemblFungi; EDP51795; EDP51795; AFUB_058160.
DR HOGENOM; CLU_011131_2_2_1; -.
DR PhylomeDB; B0Y0Q4; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
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:UniProtKB-UniPathway.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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: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 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 201..575
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 348
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 403
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 747 AA; 85711 MW; 1807E05BF49F4CA2 CRC64;
MASTEASNIA QSAPPDGTGV IQLDPWLEPF RDALRHRFGL VENWIKTINE NEGGLDKFSK
GYEKFGFNVN ANGDITYREW APNAVRAYLV GDFNNWDVAA HPMAKDNFGV WEITVPSKDG
MPAIPHDSKV KIAMDIPSGE RIYRIPAWIK RVVQDLEVSP IYESVFWNPP ESERYKFKHS
RPKKPESLRI YEAHVGISSP ETRVATYKEF TKNMLPRIKY LGYNAIQLMA IMEHAYYASF
GYQVNNFFAA SSRYGTPDEL KELIDTAHSM GLTVLLDVVH SHASKNVDDG LNMFDGTDHL
YFHEGGKGRH DLWDSRLFNY GHHEVLRFLL SNLRFWMEEY GFDGFRFDGV TSMLYVHHGI
GTGFSGGYHE YFGPSVDDEG VMYLTLANEM LHTLYPNCIT VAEDVSGMPA LCLPHSLGGI
GFDYRLAMAI PDMYIKLLKE KSDNEWEMGN LAFTLTNRRH GEKTIAYAES HDQALVGDKT
LMMWLCDKEM YTHMSVLTEF TPTIERGMAL HKMIRLVTHG LGGEGYLNFE GNEFGHPEWL
DFPRAGNNNS FWYARRQLNL TEDHLLRYKF LNEFDRSMQL TEEKYGWLHS PQAYVSLKHE
IDKVLAFERA GLLWIFNFHP TESFTDYRVG VEQAGTYRIV LDTDDPEFGG FGRNLKETRF
FTTDMPWNGR SNYLQVYLPT RTALVCTPST FPFVGDLRAN KKLQCRSSPW KKHCSHLNGF
MPRLGRGQCE SLHIDIKYVA LPNNLPQ
//
