ID   AMYG_HORRE     STANDARD;      PRT;   616 AA.
AC   Q03045;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   21-MAR-2006, entry version 48.
DE   Glucoamylase P precursor (EC 3.2.1.3) (Glucan 1,4-alpha-glucosidase)
DE   (1,4-alpha-D-glucan glucohydrolase).
GN   Name=GAMP;
OS   Hormoconis resinae (Creosote fungus) (Amorphotheca resinae).
OC   Eukaryota; Fungi; Ascomycota; Ascomycota incertae sedis;
OC   Amorphothecaceae; Amorphotheca.
OX   NCBI_TaxID=5101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 20495;
RX   MEDLINE=93146382; 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,
RT   sequencing and introduction into Trichoderma reesei.";
RL   FEMS Microbiol. Lett. 78:237-243(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 20495;
RX   MEDLINE=93365035; 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   MEDLINE=90338987; PubMed=2116499;
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: Hydrolysis of terminal 1,4-linked alpha-D-
CC       glucose residues successively from non-reducing ends of the chains
CC       with release of beta-D-glucose.
CC   -!- SUBCELLULAR LOCATION: Secreted protein.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC   -!- SIMILARITY: Contains 1 CBM20 (carbohydrate binding type-20)
CC       domain.
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DR   EMBL; X68143; CAA48243.1; -; Genomic_DNA.
DR   EMBL; X67708; CAA47945.1; -; mRNA.
DR   PIR; S33908; S33908.
DR   HSSP; P04064; 1GAI.
DR   InterPro; IPR008928; 6hp_glycosidase.
DR   InterPro; IPR008291; Glucamylse_SBD.
DR   InterPro; IPR011613; Glyco_hydro15rel.
DR   InterPro; IPR000165; Glyco_hydro_15.
DR   InterPro; IPR002044; Glyco_hydro_s_bd.
DR   InterPro; IPR012343; Glyco_trans_sub.
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   ProDom; PD001568; Glyco_hydro_CBD; 1.
DR   PROSITE; PS51166; CBM20; 1.
DR   PROSITE; PS00820; GLUCOAMYLASE; FALSE_NEG.
KW   Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL        1     29
FT   CHAIN        30    616       Glucoamylase P.
FT                                /FTId=PRO_0000001471.
FT   DOMAIN      501    608       CBM20.
FT   ACT_SITE    205    205       Proton acceptor (By similarity).
FT   ACT_SITE    208    208       Proton donor (By similarity).
FT   BINDING     149    149       Substrate (By similarity).
FT   CARBOHYD    200    200       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    427    427       N-linked (GlcNAc...) (Potential).
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
//
 
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