AMYG_SCHCM
ID AMYG_SCHCM Reviewed; 576 AA.
AC D8Q9M3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Glucoamylase ARB_02327-1 {ECO:0000305};
DE EC=3.2.1.3 {ECO:0000250|UniProtKB:P69327};
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000250|UniProtKB:P69327};
DE AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000250|UniProtKB:P69327};
DE AltName: Allergen=Sch c 1 {ECO:0000303|PubMed:24372664};
DE Flags: Precursor;
GN ORFNames=SCHCODRAFT_57589;
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000312|Proteomes:UP000007431};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000312|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX PubMed=24372664; DOI=10.1111/cea.12260;
RA Toyotome T., Satoh M., Yahiro M., Watanabe A., Nomura F., Kamei K.;
RT "Glucoamylase is a major allergen of Schizophyllum commune.";
RL Clin. Exp. Allergy 44:450-457(2014).
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:0000250|UniProtKB:P69327};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DN29}.
CC -!- ALLERGEN: Major allergen that causes an allergic reaction in human.
CC Binds to IgE and IgG. {ECO:0000269|PubMed:24372664}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR EMBL; GL377308; EFI95688.1; -; Genomic_DNA.
DR RefSeq; XP_003030591.1; XM_003030545.1.
DR AlphaFoldDB; D8Q9M3; -.
DR SMR; D8Q9M3; -.
DR STRING; 578458.D8Q9M3; -.
DR Allergome; 10126; Sch c 1.
DR Allergome; 10127; Sch c 1.0101.
DR EnsemblFungi; EFI95688; EFI95688; SCHCODRAFT_57589.
DR GeneID; 9591574; -.
DR KEGG; scm:SCHCODRAFT_57589; -.
DR eggNOG; ENOG502QPM2; Eukaryota.
DR HOGENOM; CLU_012173_2_1_1; -.
DR InParanoid; D8Q9M3; -.
DR OMA; SSNNLWY; -.
DR OrthoDB; 589046at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 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 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; SSF48208; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS00820; GLUCOAMYLASE; 1.
PE 1: Evidence at protein level;
KW Allergen; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..576
FT /note="Glucoamylase ARB_02327-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434423"
FT DOMAIN 477..576
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 552..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR001031-2"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 243..470
FT /evidence="ECO:0000250|UniProtKB:P69327"
FT DISULFID 285..293
FT /evidence="ECO:0000250|UniProtKB:P69327"
SQ SEQUENCE 576 AA; 60941 MW; 909BFED225AD7A9F CRC64;
MGLASTVSLA LLGLCSLARA QTSAADAYVS AESPIAQAGI LANIGPSGSK SHGAASGVII
ASPSTSNPDY LYTWTRDAAL VSRALVDEFI EGESSLQSVI DSYVSSQQKL QRVDNPSGSY
TSGGLGEPKF NIDLTAFTGA WGRPQRDGPA LRAITLITYG NHLLSSGNTS YVTDTIWPVV
KADLDYVVSY WNQTGFDLWE EVSSSSFFTT AEQHTALRLG ATFATAVGAS ASTYLTQADN
VLCFLQSYWN SNGGYATANT GGGRSGIDAN TVLTSIHTFD IEAGCDSVTF QPCSDRALSN
LKVYVDSFRG LYSINPTGAT DPILTGRYKE DVYYNGNPWY LTTFAVAEQL YDALNTWDKL
GSLDVTSTSL AFFKQFDSSI TAGTYASSTS EYATLTSAIR NWADGFLEVL ADFTPADGGL
TEQIDKSSGN PTSAADLTWS YASAITAFKA RGGAIPASWG AAGLTVPATC STGGGGGSGG
DTVAVTLNVQ ATTVYGENIY VTGSVNQLAN WSPDNAIALN ADNYPTWSVT VNLPANTQIE
YKYIRKNNGQ VTWESDPNRS ITTSASGSFT QNDTWR
