ID B8P7A3_POSPM Unreviewed; 568 AA.
AC B8P7A3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00012593};
DE EC=3.2.1.3 {ECO:0000256|ARBA:ARBA00012593};
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000256|ARBA:ARBA00033473};
DE AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00033442};
GN ORFNames=POSPLDRAFT_117345 {ECO:0000313|EMBL:EED83206.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED83206.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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 Evidence={ECO:0000256|ARBA:ARBA00001863};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC {ECO:0000256|ARBA:ARBA00006188}.
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DR EMBL; EQ966271; EED83206.1; -; Genomic_DNA.
DR RefSeq; XP_002471558.1; XM_002471513.1.
DR AlphaFoldDB; B8P7A3; -.
DR SMR; B8P7A3; -.
DR STRING; 561896.B8P7A3; -.
DR KEGG; ppl:POSPLDRAFT_117345; -.
DR HOGENOM; CLU_012173_1_0_1; -.
DR InParanoid; B8P7A3; -.
DR OMA; MAPRFWT; -.
DR OrthoDB; 1586242at2759; -.
DR Proteomes; UP000001743; 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; cd05808; CBM20_alpha_amylase; 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; IPR002044; CBM_fam20.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR000165; Glucoamylase.
DR InterPro; IPR008291; Glucoamylase_SBD.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR31616:SF11; GLUCOAMYLASE, INTRACELLULAR SPORULATION-SPECIFIC; 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; 2.
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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..568
FT /note="glucan 1,4-alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002878679"
FT DOMAIN 469..568
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 547..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-2"
SQ SEQUENCE 568 AA; 60941 MW; 5724D99B7A697EC9 CRC64;
MRLTVVSGLA YACGALAASS SVSSYIASES PVAKAGVLAN IGAGGAAQSR LSGVVIASPS
TSNPDYLYTW TRDSSLTFKA LIDQYTSGED TSLRTLIDEF VSAEATLQQV TNPSGSVSTG
GLGEPKFNIN ETAFTGAWGR PQRDGPALRA TAVMSYATYL YNSGNTTYVT DTLWPIIELD
LNYVAGNWNQ STFDLWEEVD SSSFFTTAVQ HRSLRQGVIF ANLIGQTSVV SNYETQAQAL
LCFLQSYWNP TDNYVTANTG GGRSGKDANT ILASIHTFDL DAGCDATTFQ PCSDKALSNL
KVYVDSFRSI YTINDDISSD AAVATGRYPE DTYYNGNPWY LCTLAVAEQL YDALIVWDAQ
DYLEVTSTSL AFFQQFDSSV AAGTYDSSTS TYSTLTSAVK SFADGFTLIV ASYTPSDGEL
SEQYSKSDGS QTSAVDLTWS YASALTAFAA EAGTSYGSWG AANLSTSSCP STSGVSVTFE
VEYDTEYGEN LYITGSVSEL EDWSADDALI MSSANYPTWS ITVTLPASTA IQYKYLTKYN
GDVTWEDDPN NEITTPASGS VTQSDSWH
//