(data stored in SCRATCH zone)

SWISSPROT: B6H6W4_PENRW

ID   B6H6W4_PENRW            Unreviewed;       631 AA.
AC   B6H6W4;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 52.
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=Pc16g00620 {ECO:0000313|EMBL:CAP92732.1}, PCH_Pc16g00620
GN   {ECO:0000313|EMBL:CAP92732.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92732.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92732.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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. {ECO:0000256|PIRNR:PIRNR001031}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC       {ECO:0000256|PIRNR:PIRNR001031}.
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DR   EMBL; AM920431; CAP92732.1; -; Genomic_DNA.
DR   RefSeq; XP_002560481.1; XM_002560435.1.
DR   ProteinModelPortal; B6H6W4; -.
DR   STRING; 500485.XP_002560481.1; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   EnsemblFungi; CAP92732; CAP92732; PCH_Pc16g00620.
DR   GeneID; 8317640; -.
DR   KEGG; pcs:Pc16g00620; -.
DR   eggNOG; ENOG410IGG8; Eukaryota.
DR   eggNOG; COG3387; LUCA.
DR   HOGENOM; HOG000182646; -.
DR   KO; K01178; -.
DR   OMA; EDSYYNG; -.
DR   OrthoDB; EOG092C1YYH; -.
DR   BioCyc; PCHR:PC16G00620-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
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; 2.60.40.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034836; CBM20_glucoamylase.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR000165; Glucoamylase.
DR   InterPro; IPR008291; Glucoamylase_SBD.
DR   InterPro; IPR011613; Glyco_hydro_15/PHK.
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.
DR   PROSITE; PS00820; GLUCOAMYLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H6W4.
DR   SWISS-2DPAGE; B6H6W4.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001031};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001031};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001031};
KW   Polysaccharide degradation {ECO:0000256|PIRNR:PIRNR001031};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    631       Glucoamylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002845424.
FT   DOMAIN      524    631       CBM20 (carbohydrate binding type-20).
FT                                {ECO:0000259|PROSITE:PS51166}.
FT   ACT_SITE    206    206       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR001031-1}.
FT   ACT_SITE    209    209       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001031-1}.
FT   BINDING     150    150       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001031-2}.
SQ   SEQUENCE   631 AA;  67258 MW;  48FA108E59A6C0A0 CRC64;
     MAPRFWTALW ALTLGHAVVA TPQILAPRAT GSLDTWLASE TVVARQGILD NIGSAGAHAA
     NAKPGVVLAS PSTSDPDYYY TWTRDSALVF KNLVDMFRSG DSALLEVIEE YISSQAYIQT
     VSNPSGGLSG GGGLGEPKFN ADETAFTGSW GRPQRDGPAL RATALISFGQ WLIDNGYTTY
     ATDIVWPVVR NDLSYVSQYW NQTGFDLWEE VSGSSFFTVA AQHRALVEGS TFASQVGSSC
     LYCDSQAPQV LCFLQSFWTG SYILANFGGG RSGKDANTLL GSIHTFDPEA GCDDTTFQPC
     SARALANHKV VTDSFRSIYS VNSGIAAGKA VSVGRYPEDS YYNGNPWYLC TLAAAEQLYD
     AIYTWNRIGS LTITSVSLSF FKDLYSSAAT GTYSSSSDTY SSIVAAVKEY ADGYVSIVEK
     YAASSGSLSE QFSKSDGSQL SARDLTWSYA ALLTANERRN AIVPAPWGET SASSVPGQCQ
     YTSAIGTYSS ATNTAWPTTL TSGSGSVTTT KTTTTTSKPT TTSCTTPTTV AVTFNVIATT
     EYGQNIKLAG SISQLGSWSP SSAVALSASK YTTSNHLWFV TVTLPVGTSF SYKYIQVASD
     GTIKWESDPN QSYTVPATCG TTAVTVSDTW R
//

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