AMYG_AMORE
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 03-AUG-2022, entry version 107.
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 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; -; 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 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; SSF48208; 1.
DR SUPFAM; SSF49452; SSF49452; 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
