ID K9GNI5_PEND1 Unreviewed; 640 AA.
AC K9GNI5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=PDIP_42500 {ECO:0000313|EMBL:EKV14741.1};
OS Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV14741.1, ECO:0000313|Proteomes:UP000009886};
RN [1] {ECO:0000313|Proteomes:UP000009886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKV14741.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKCU01000298; EKV14741.1; -; Genomic_DNA.
DR RefSeq; XP_014535241.1; XM_014679755.1.
DR AlphaFoldDB; K9GNI5; -.
DR GeneID; 26232568; -.
DR KEGG; pdp:PDIP_42500; -.
DR HOGENOM; CLU_012173_1_0_1; -.
DR OrthoDB; 1586242at2759; -.
DR Proteomes; UP000009886; Unassembled WGS sequence.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..640
FT /note="Glucoamylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003929314"
FT DOMAIN 533..640
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 499..528
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 640 AA; 68129 MW; C2E28DC539EDF273 CRC64;
MVRFFWAALW ALTLGQVVMA VQQILAPRAT GSLDIWLATE RVVARQGILN NIGSAGAYAA
NAKPGIVVAS PSTSNPNYYY TWTRDSALVF KTLIDLFKNG DSALLDVIEE YINAQAYIQT
VSNPSGDLSG GGGLGEPKFN TDETAFTGSW GRPQRDGPAL RATALISFGQ WLMDNGYTTY
ATNIVWPIVR NDLSYVAQYW NQTGFDLWEE VSGSSFFTIA AQHRALVEGS TFARQVGVSC
SSCDSQAPQV LCFLQSFWTG SYILANFGGG RSGKDANTLL GSIQTFDPEA GCDDTTFQPC
SARALANHKV VTDSFRSVYS LNSGIAAGKA VSVGRYPEDS YYNGNPWYLC TLAAAEQLYD
AIYTWNQIGS LTITSVSLSF FKDLYSSAAP GTYSSSSDTY ASIVSAVKTY ADGYVRVVET
YAPSSGSLSE QFSRSDGSQL SARDLTWSYA ALLTANERRN AIVPAPWGET SASSVPGQCQ
YTSAVGTFSS ATNTAWPSTL TSGSGSGTTT GSGGATTTKT TPATKTTSTI TSCTTPTAVA
VTFNVIATTL YGQNIKLAGS ISELGSWSPS SAIALSASSY TTSNHLWFVT VTLPAGISFT
YKFIRVVSDG TITWESDPNL SYTVPATCGA TAVTVNNTWR
//
