ID A0A072P4X0_9EURO Unreviewed; 718 AA.
AC A0A072P4X0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=A1O9_09339 {ECO:0000313|EMBL:KEF54896.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF54896.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF54896.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF54896.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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; 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:KEF54896.1}.
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DR EMBL; AMGV01000009; KEF54896.1; -; Genomic_DNA.
DR RefSeq; XP_013257486.1; XM_013402032.1.
DR AlphaFoldDB; A0A072P4X0; -.
DR STRING; 1182545.A0A072P4X0; -.
DR GeneID; 25284248; -.
DR VEuPathDB; FungiDB:A1O9_09339; -.
DR HOGENOM; CLU_011131_2_2_1; -.
DR OrthoDB; 96at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000027920; 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:UP000027920};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 234..582
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 426
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 718 AA; 81929 MW; D372B00DF63A217A CRC64;
MALNQASANS LAAAPAGQDS APDGTGQTPK RRTQSITDKN TGVIQLDPWL DPFRDSLKSR
FAKAQKWIKT IEETEGGLEK FSRGYETFGF TFGSDGSITY REWAPNAEQA FLIGDFNNWN
RDATPLKKNH FGVWEITLPA RDGVAPISHN SKIKVSFIIP GGERIERLPA WITRVTQDLN
VSPVYDAVLW NPPHHERYQF KNPRPPYPKS ARIYEAHVGI SSPELKVATY KEFTKNMLPR
IQYLGYNVIQ LMAIMEHAYY ASFGYQVNSF FAASSRYGTP DDLKELIDAA HGMGITVLLD
VVHSHASKNT LDGLNMFDGS DHLYFHEGAK GRHELWDSRL FNYGHHEVLR FLLSNLRFWM
EEYQFDGFRF DGVTSMLYTH HGIGTGFSGG YHEYFGPSVD EDGIVYLMLA NEMLHNLYPN
AITIAEDVSG MPALCLKLSL GGVGFDYRLA MAVPDMYIKM LKEKSDDEWD IGNIAFTLTN
RRHGEKTIAY AESHDQALVG DKSLMMWLAD AEMYTHMSTL TEFTPTIERA LSLHKLIRLV
THSLGGEGYL NFEGNEFGHP EWLDFPRAGN DNSFWYARRQ FNLTEDGLLR YKFLNDFDRA
MNWTEEKYGW LHSPQAYISL KNETDKVLVF ERAGLLWIFN FHPTKSYTDY RVGVEQGGVY
RIVLDTDSPE FGGLSRNAKD TRFFTNDLPW NGRKNFTQVY IPTRTALVSL HIILLVCY
//
