ID AMYG_SCHPO Reviewed; 450 AA. AC O60087; Q96WS5; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 142. DE RecName: Full=Probable glucoamylase; DE EC=3.2.1.3; DE AltName: Full=1,4-alpha-D-glucan glucohydrolase; DE AltName: Full=Glucan 1,4-alpha-glucosidase; DE AltName: Full=Meiotic expression up-regulated protein 17; DE Flags: Precursor; GN Name=meu17; ORFNames=SPBC14C8.05c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 210-450. RC STRAIN=CD16-1; RX PubMed=11376151; DOI=10.1093/nar/29.11.2327; RA Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y., RA Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.; RT "Comprehensive isolation of meiosis-specific genes identifies novel RT proteins and unusual non-coding transcripts in Schizosaccharomyces pombe."; RL Nucleic Acids Res. 29:2327-2337(2001). 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}. 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; CU329671; CAA18423.1; -; Genomic_DNA. DR EMBL; AB054301; BAB60870.1; -; mRNA. DR PIR; T39433; T39433. DR RefSeq; NP_595908.1; NM_001021816.2. DR AlphaFoldDB; O60087; -. DR SMR; O60087; -. DR BioGRID; 276237; 1. DR STRING; 284812.O60087; -. DR CAZy; GH15; Glycoside Hydrolase Family 15. DR GlyCosmos; O60087; 2 sites, No reported glycans. DR PaxDb; 4896-SPBC14C8-05c-1; -. DR EnsemblFungi; SPBC14C8.05c.1; SPBC14C8.05c.1:pep; SPBC14C8.05c. DR GeneID; 2539682; -. DR KEGG; spo:SPBC14C8.05c; -. DR PomBase; SPBC14C8.05c; meu17. DR VEuPathDB; FungiDB:SPBC14C8.05c; -. DR eggNOG; ENOG502QPM2; Eukaryota. DR HOGENOM; CLU_012173_2_2_1; -. DR InParanoid; O60087; -. DR OMA; SHFWNQS; -. DR PhylomeDB; O60087; -. DR PRO; PR:O60087; -. DR Proteomes; UP000002485; Chromosome II. DR GO; GO:0009986; C:cell surface; NAS:PomBase. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase. DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase. DR GO; GO:0005628; C:prospore membrane; HDA:PomBase. DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; ISO:PomBase. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central. DR GO; GO:0005980; P:glycogen catabolic process; ISO:PomBase. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR012341; 6hp_glycosidase-like_sf. DR InterPro; IPR011613; GH15-like. DR InterPro; IPR000165; Glucoamylase. DR PANTHER; PTHR31616:SF12; GLUCOAMYLASE-RELATED; 1. DR PANTHER; PTHR31616; TREHALASE; 1. DR Pfam; PF00723; Glyco_hydro_15; 1. DR PRINTS; PR00736; GLHYDRLASE15. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Meiosis; KW Polysaccharide degradation; Reference proteome; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT PROPEP 17..28 FT /evidence="ECO:0000250" FT /id="PRO_0000001479" FT CHAIN 29..450 FT /note="Probable glucoamylase" FT /id="PRO_0000001480" FT ACT_SITE 203 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 206 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 147 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 383 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 409 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 450 AA; 51164 MW; 31C5BF2A8E4785FE CRC64; MRTYWLFLLL GGVVSAESLL SPNKRSKEAS MDEWTDQQKG IAMGHMLNNI GDSGMHAKDI NPGCIIASPS TDSPDYYYQW VRDSALTIMT ILDRFFEGDK GLEPIIVKYM DEMVRLQKVP NPSGDFYAGG LGEPKFNVDG TSYDGDWGRP QNDSPALRAI AFIKYMNYLF ENGKEVHEVT VWIEAVLADL DYTANHWTEA SFDLWEEIKD VHYFTLAVQK RAMQDGTAFA KRIGAPDQAA LYQRTIEPID LKLGEFWDPG MGVIKGYKGR VDRSGLDCST LLASLYSNEF DMHILPTLLK LQETMTRDYP VNQGWKQAMG RYPEDVYDGV SKSIGNPWFI CTSSAAEIIY KAIAYYDNKG LPELTEYNIH FFMKFAEFGD PYNWSVIRKN MHTYADNFLK AVAEFQHPNG SMSEQFSRDD GHQKGARDLT WSYSSLLNAI YRREAIKGSV //