ID B8PLI6_POSPM Unreviewed; 491 AA. AC B8PLI6; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 66. DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595}; DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595}; GN ORFNames=POSPLDRAFT_92881 {ECO:0000313|EMBL:EED78264.1}; 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:EED78264.1, 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=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in CC polysaccharides containing three or more (1->4)-alpha-linked D- CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|ARBA:ARBA00008061}. 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; EQ966456; EED78264.1; -; Genomic_DNA. DR RefSeq; XP_002476539.1; XM_002476494.1. DR AlphaFoldDB; B8PLI6; -. DR STRING; 561896.B8PLI6; -. DR KEGG; ppl:POSPLDRAFT_92881; -. DR HOGENOM; CLU_006462_7_2_1; -. DR InParanoid; B8PLI6; -. DR OMA; YMDGVLN; -. DR OrthoDB; 3249969at2759; -. DR Proteomes; UP000001743; Unassembled WGS sequence. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro. DR CDD; cd11319; AmyAc_euk_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR013777; A-amylase-like. DR InterPro; IPR015340; A_amylase_C_dom. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1. DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR Pfam; PF09260; A_amylase_dom_C; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR PIRSF; PIRSF001024; Alph-amyl_fung; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR001024-3}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001024-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000001743}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..491 FT /note="alpha-amylase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002878912" FT DOMAIN 30..384 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 220 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1" FT ACT_SITE 244 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 137 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 138 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 176 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 218 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 220 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 244 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 248 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 312 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 359 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT SITE 312 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2" FT DISULFID 46..54 FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4" FT DISULFID 164..178 FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4" SQ SEQUENCE 491 AA; 54403 MW; B92DE50675516937 CRC64; MLRQLLPALL TALPAFSASA ADWQQRSIYQ LVTDRFATTN GSYPSCDTED RVYCGGTWQG VIRQLDYIQN MGFDAIWISP IVANLEGSTG DGESYHGYWT VDQNSLNSHF GNESDLLELS SQLHSRGMYL MLDVVVNHMA ADTLPPDYVL FTPFNTESDF HTFCWITDYS NQTNVEQCWL GDDNVPLADC DTESDYVIDF FYRWIGDLVA NYSADGLRID TVKHVRSDFW PGFAEAAGVF TIGEVLDGDV DYVSTYTEVL DAVLDYPTYY QLFYAFESTS GSLSNLVSWV QQSQSTYKNG EFMTGSFLEN QDNPRFQSVQ TDQALVSNAI SWPFIQDGIP ILYYGQEQGY TGSDDPYNRE ALWLSGYVED KPLVKLVRTL NAARKAAIAA SSDYLSTVLT FPSVTSSTLA VYKQPMLALL TNGGSSSTPS WSVSSTDYSN GEELINVLTC DTLTAGSNGA VSVTGSEGMP QILLPTSVFN VTYCNELLST Y //