ID   AMYG_AMORE              Reviewed;         616 AA.
AC   Q03045;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Glucoamylase P;
DE            EC=3.2.1.3;
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE   AltName: Full=Glucan 1,4-alpha-glucosidase;
DE   Flags: Precursor;
GN   Name=GAMP;
OS   Amorphotheca resinae (Creosote fungus) (Hormoconis resinae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Amorphothecaceae; Amorphotheca.
OX   NCBI_TaxID=5101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20495 / CBS 174.61 / NRRL 6437;
RX   PubMed=1490604; DOI=10.1016/0378-1097(92)90033-k;
RA   Joutsjoki V.V., Torkkeli T.K.;
RT   "Glucoamylase P gene of Hormoconis resinae: molecular cloning, sequencing
RT   and introduction into Trichoderma reesei.";
RL   FEMS Microbiol. Lett. 78:237-243(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 20495 / CBS 174.61 / NRRL 6437;
RX   PubMed=8358830; DOI=10.1007/bf00324663;
RA   Vainio A.E.I., Torkkeli H.T., Tuusa T., Aho S.A., Fagerstroem B.R.,
RA   Korhola M.P.;
RT   "Cloning and expression of Hormoconis resinae glucoamylase P cDNA in
RT   Saccharomyces cerevisiae.";
RL   Curr. Genet. 24:38-44(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 72-76, AND CHARACTERIZATION.
RX   PubMed=2116499; DOI=10.1099/00221287-136-5-913;
RA   Fagerstroem R., Vainio A.E.I., Suoranta K., Pakula T., Kalkkinen N.,
RA   Torkkeli H.T.;
RT   "Comparison of two glucoamylases from Hormoconis resinae.";
RL   J. Gen. Microbiol. 136:913-920(1990).
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;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR   EMBL; X68143; CAA48243.1; -; Genomic_DNA.
DR   EMBL; X67708; CAA47945.1; -; mRNA.
DR   PIR; S33908; S33908.
DR   PDB; 6FHW; X-ray; 3.60 A; A/B=1-616.
DR   PDBsum; 6FHW; -.
DR   AlphaFoldDB; Q03045; -.
DR   SMR; Q03045; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   CLAE; GLA15P_AMORE; -.
DR   GlyCosmos; Q03045; 2 sites, No reported glycans.
DR   BRENDA; 3.2.1.3; 1433.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..29
FT   CHAIN           30..616
FT                   /note="Glucoamylase P"
FT                   /id="PRO_0000001471"
FT   DOMAIN          501..608
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   616 AA;  66432 MW;  B5F4DC8EEBB152FB CRC64;
     MRLLPSSCAG ALSLLCSLAI AAPTELKARD LSSFIASERA IALQGALNNI GPDGSAVPGA
     GAGFVVASPS KANPDYFYTW SRDSALTLKM IIDEFILGNT TLQTIIEQYI HAQAVLQTVS
     NPSGTFLPDG VGLGEPKFMV DGTRFNGPWG RPQRDGPALR AIALMTYSNW LIKNGQFAEA
     KTKIWPIIAN DLSYVGQYWN QSGFDLWEET YASSFFTIQN QHRALVEGAQ LAHDLGVTCT
     GCDQAPEVLC FLQSFWNGKY IVSNINVNNG RTGLDGNSIL GAISTFDIDA YCDSPTLQPC
     HSQSLANFKV LTDTFRNLYT INAGIPEGQG VAVGRYAEDV YMGGNPWYLI TTAAAEFLYD
     AVAQWKARHV LTVDETSLAF FKDIYPEVTV REYKSGNANS PFAQIMDAVT AYADSYVAIA
     EKYIPSNGSL SEQFNRDTGT PLSAIDLTWS YAAFITMSQR RAGQYPSSWG SRNALPPPTT
     CSASSTPGIY TPATAAGAPN VTSSCQVSIT FNINATTYYG ENLYVIGNSS DLGAWNIADA
     YPLSASAYTQ DRPLWSAAIP LNAGEVISYQ YVRQEDCDQP YIYETVNRTL TVPACGGAAV
     TTDDAWMGPV GSSGNC
//