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Database: UniProt
Entry: B8P7A3_POSPM
LinkDB: B8P7A3_POSPM
Original site: B8P7A3_POSPM 
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
//
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