ID A0A137QFU0_9AGAR Unreviewed; 681 AA.
AC A0A137QFU0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=AN958_10488 {ECO:0000313|EMBL:KXN86121.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN86121.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN86121.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN86121.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) 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}.
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DR EMBL; KQ962390; KXN86121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QFU0; -.
DR STRING; 1714833.A0A137QFU0; -.
DR OrthoDB; 96at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000070249; 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:UP000070249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 164..567
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 340
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 395
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 681 AA; 78430 MW; EC3DD67686418FB4 CRC64;
MPTPPLDPKV VLKIDGYLRP HIPAIIQRYN SFRRWKDAFE LHEGGWDKFT RGYERFGFNV
GPNNEVVYRE WAPNAKEAYL IGDFNEWNRQ SHPMTVNDFG IWEITVPPLP SGHCAIPHDS
KIKISMILPN GERIERLPTW IKRVTQDLDV SPVYDARFWN PPEPERYKLK NPRPPKPTNI
RIYEAHVGIS TAELRVGTYK EFTQNILPRI KSLGYNAIQI MAIMEHAYYA SFGYQVTSFF
APSSRYGTPE DLKELIDTAH GLGLTVLLDI VHSHACKNVL DGLNEFDGTD HLYFHEGGKG
RHDLWDSRLF NYGSHEVLRF LLSNLRYWIE TYGFDGFRFD GVTSMMYKHH GIGAGFSGGY
HEYFGDSTDE EGIVYLMLAN EAMHTLHPSI ITIAEDVSGM PFLCLPVSKG GVGFDYRLSM
AIPDTWIKLL KHKADDEWDM GNIVFTLTNR RHGEKSITYC ESHDQALVGD KTIAFWLMDK
EMYTHMSDLT PMTPIIARGL SLHKLIRFIT HTLGGEGYLN FEGNEFGHPE WLDFPREGNG
NSFKHARRQW NVVDDHLLRY KYLNNFDSAM NHVAAKYGWL EAPQAYVSLK HESDKVIVFE
RAGLLFIFNF HPTNSYTDYR VGVDVAGEYK VVLNSDEKQF GGFDNVKSDS TYFTTPTEWN
NRKNWLQVYI PSRTCLVLGR K
//
