ID A0A0F4ZI41_9PEZI Unreviewed; 620 AA.
AC A0A0F4ZI41;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glucoamylase {ECO:0000256|PIRNR:PIRNR001031};
DE EC=3.2.1.3 {ECO:0000256|PIRNR:PIRNR001031};
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000256|PIRNR:PIRNR001031};
DE AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|PIRNR:PIRNR001031};
GN ORFNames=TD95_001685 {ECO:0000313|EMBL:KKA29558.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA29558.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA29558.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA29558.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC successively from non-reducing ends of the chains with release of
CC beta-D-glucose.; EC=3.2.1.3; Evidence={ECO:0000256|ARBA:ARBA00001863,
CC ECO:0000256|PIRNR:PIRNR001031};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC {ECO:0000256|ARBA:ARBA00006188, ECO:0000256|PIRNR:PIRNR001031}.
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:KKA29558.1}.
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DR EMBL; LAEV01000782; KKA29558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZI41; -.
DR OrthoDB; 1586242at2759; -.
DR Proteomes; UP000033483; Unassembled WGS sequence.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd05811; CBM20_glucoamylase; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034836; CBM20_glucoamylase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR000165; Glucoamylase.
DR InterPro; IPR046966; Glucoamylase_active_site.
DR InterPro; IPR008291; Glucoamylase_SBD.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR31616:SF12; GLUCOAMYLASE-RELATED; 1.
DR PANTHER; PTHR31616; TREHALASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR PIRSF; PIRSF001031; Glu-a-glcsd_SBD; 1.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS00820; GLUCOAMYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR001031};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001031};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001031};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PIRNR:PIRNR001031};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..620
FT /note="Glucoamylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002482522"
FT DOMAIN 507..613
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-2"
SQ SEQUENCE 620 AA; 65462 MW; ED7CED9885F371E9 CRC64;
MVFLKSAIAA STWLLAATGV VASPVSKRAT LDEFISTERP LALEKLLCNI GSTGCRASGA
SSGVVLASPS TSNPDYYYTW TRDAALVFKE IVDSVETNTT LLLPEIENYV TAQAYLQTVT
NPSGSLSDGA GLAEPKFNAD LTQFTGAWGR PQRDGPALRA TAMIAYYNYL LNNNATTDCG
LWQIIQNDLN YVAQYWNQTG YDLWEEVPGS SFFTVAAQYR ALVEGSTLAA KLGKSHSAYD
TVAPQILCYL QSFWSSSKGY IVANTQTASW VSRSGLDANT PLTAIHLFDP ELGCDDSTFQ
PCSPKQLITT KKLVDSFRSI YAINSGKSAG TALAVGRYAE DVYYNGNPWY LCTLAVAEQL
YDAVYTWKLE GSITVTSVSL PFFTDLLPSL TTGTYASGST TFESIISAVT TYADGFVSIV
QTYTPSDGAL SEQYNKANGQ QLSAQDLTWS YAAFLSATER RDSVVPAGWA GASSVSVPGA
CAATTVVGTY AAASNCGTPG SGSGGNGGSS GNALVTFNEL ATTYYGENIK LVGSTAAFGS
WSPSAGILLS ASSYTASNPL WTTTVSVPQG STVEFKFIRV GSDGSITWES GNNKVLTVGS
SATSVTVSAS WNGAYSVSSS
//
