ID A0A2L2TSP7_9HYPO Unreviewed; 707 AA.
AC A0A2L2TSP7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI62955.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-2014) 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; LN649230; CEI62955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2TSP7; -.
DR STRING; 56646.A0A2L2TSP7; -.
DR OrthoDB; 96at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000245910; Chromosome ii.
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:UP000245910};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 188..586
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 414
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 707 AA; 80137 MW; AE4A79A0109ED231 CRC64;
MAAIVENSSN SLDPNQTNGA AGDIPNDGTG VVKLDPWLEP FSGALKRRYS KTQDWIKTIN
DTEGSLEKFS RGAEKFGFNV DANNNIVYRE WAPNATAAYL IGDFNGWNRG AHPMKKNDFG
VFEITIPAQN GQTAIPHNSK LKISLDLPGG EHVDRLPAWI KYVTQDLSVS PAYDARFWNP
PASETYKFKN SRPKKPASAR VYEAHVGISS PDQRVATYKE FTKNMLPRIK GLGYNVIQLM
AVMEHAYYAS FGYQINNFFA ASSRYGTPED LKELIDTAHG MGITMLLDVV HSHASKNVLD
GLNEFDGTDH QYFHGGGKGR HDQWDSRLFN YGHHEVMRFL LSNLRFWMDE YQFDGFRFDG
VTSMLYVHHG MGTGFSGGYH EYFGPDVDEE AVVYMMLANE MLHQLYPEII TIAEDVSGMP
ALCLPLSLGG IGFDYRLAMA IPDMWIKILK EVKDDEWDIA SICHTLTNRR HGEKTIAYAE
SHDQALVGDK TLMMHLCDAE MYTNMSTLSP LTPVVDRGMA LHKMIRLVTH GLGGEGYLNF
EGNEFGHPEW LDFPREGNNN SFWYARRQLN LTDDPLLRYK FLDHFDRLMN QTEAKYGWLA
APQAYISLKH EGDKVIVFER AGLVFVFNFH PTNSFSDYRI GIEVPGTYRV VLNTDNGDVG
GHNRIDENTR FFTTPMEWNN RKNWTHIYIP ARTAIVLALE STISQNS
//
