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Database: UniProt
Entry: A0A443HJ33_BYSSP
LinkDB: A0A443HJ33_BYSSP
Original site: A0A443HJ33_BYSSP 
ID   A0A443HJ33_BYSSP        Unreviewed;       683 AA.
AC   A0A443HJ33;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
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=C8Q69DRAFT_481337 {ECO:0000313|EMBL:RWQ91860.1};
OS   Byssochlamys spectabilis (Paecilomyces variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ91860.1, ECO:0000313|Proteomes:UP000283841};
RN   [1] {ECO:0000313|EMBL:RWQ91860.1, ECO:0000313|Proteomes:UP000283841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ91860.1,
RC   ECO:0000313|Proteomes:UP000283841};
RX   PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA   Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA   Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA   Grigoriev I.V., Idnurm A.;
RT   "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT   variotii (Eurotiales).";
RL   Front. Microbiol. 9:3058-3058(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RWQ91860.1}.
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DR   EMBL; RCNU01000016; RWQ91860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443HJ33; -.
DR   STRING; 264951.A0A443HJ33; -.
DR   OrthoDB; 96at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000283841; 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   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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283841};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          192..553
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        394
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   683 AA;  78521 MW;  92D3564D3F93A83A CRC64;
     MMPQAPDGTG VVQLDPWLEP YKEALRTRFS YAQKWIKAIE ESEGGLEKFS KGYEKFGLNV
     SANGDITYRE WAPNVIQAHL IGDFNNWDRT ATPMKKNDFG VWEVTLPAKD GMPAIPHNSK
     LKITMEIPGG ERIDRLPAWI KRVVQDLSVS PVYEAVFWNP PAEERYTFKQ QRPKRPESLR
     IYEAHVGISS PETRVATYKE FTKNMLPRIK YLGYNAIQLM AIMEHAYYAS FGYQVNNFFA
     ASSRYGTPED LKELIDTAHS LGLVVLLDVV HSHASKNVLD GLNMFDGTDH LYFHGGGKGQ
     HELWDSRLFN YGHHEVLRFL LSNLRFWMEE YRFDGFRFDG VTSMLYTHHG IGTGFSGGYH
     EYFGPSVDED GVMYLQIANE MLHQLYPEVI TVAEDVSGMP ALCLPLSLGG VGFDYRLAMA
     VPDLYIKWLK EKADDEWDMG NLSFTLTNRR HGEKTIAYAE SHDQALVGDK TLMMWLCDKE
     MYDHMSVLSP LTPIIERGMS LHKLIRLVTH GLGGEGYLNF EGNEFGHPEW LDFPREGNGN
     SFWYARRQLN LTEDPLLRYR FLNEFDRAMQ LTEEKYGWLH SPQAYVSLKN ETDKVLVFER
     AGLLWIFNFH PTNSFTDYRV GVETAGTYRI VLDSDDTEFG GFGRNQKETR FFTTDLPWNG
     RKNFVQVYIP TRTALVLALE ETL
//
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