ID B6H6W4_PENRW Unreviewed; 631 AA.
AC B6H6W4;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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 / Wisconsin
OS 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., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA 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:
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}.
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DR EMBL; AM920431; CAP92732.1; -; Genomic_DNA.
DR RefSeq; XP_002560481.1; XM_002560435.1.
DR AlphaFoldDB; B6H6W4; -.
DR STRING; 500485.B6H6W4; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR GeneID; 8317640; -.
DR KEGG; pcs:Pc16g00620; -.
DR VEuPathDB; FungiDB:PCH_Pc16g00620; -.
DR eggNOG; ENOG502QPM2; Eukaryota.
DR HOGENOM; CLU_012173_1_0_1; -.
DR OMA; MAPRFWT; -.
DR OrthoDB; 1586242at2759; -.
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; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000000724};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..631
FT /note="Glucoamylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002845424"
FT DOMAIN 524..631
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 502..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR: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
//
