AMYG_ARTBC
ID AMYG_ARTBC Reviewed; 610 AA.
AC P0DN29; D4B1J8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
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=Allergen sch c 1 homolog {ECO:0000305};
DE AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000250|UniProtKB:P69327};
DE Flags: Precursor;
GN ORFNames=ARB_02327-1;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000312|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
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:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
CC -!- INDUCTION: Expression is up-regulated in presence of human
CC keratinocytes. {ECO:0000269|PubMed:21247460}.
CC -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE30837.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: ARB_02327-1 and ARB_02327-2.; Evidence={ECO:0000305};
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DR EMBL; ABSU01000026; EFE30837.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P0DN29; -.
DR SMR; P0DN29; -.
DR STRING; 663331.P0DN29; -.
DR PRIDE; P0DN29; -.
DR EnsemblFungi; EFE30837; EFE30837; ARB_02327.
DR eggNOG; KOG1198; Eukaryota.
DR Proteomes; UP000008866; 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 CDD; cd05811; CBM20_glucoamylase; 1.
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; IPR034836; CBM20_glucoamylase.
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.
PE 1: Evidence at protein level;
KW Allergen; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250|UniProtKB:P69327"
FT /id="PRO_0000434421"
FT CHAIN 25..610
FT /note="Glucoamylase ARB_02327-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434422"
FT DOMAIN 504..610
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P69327,
FT ECO:0000255|PROSITE-ProRule:PRU10051"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P69327,
FT ECO:0000255|PROSITE-ProRule:PRU10051"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P69327"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 233..236
FT /evidence="ECO:0000250|UniProtKB:P69327"
FT DISULFID 245..472
FT /evidence="ECO:0000250|UniProtKB:P69327"
FT DISULFID 285..293
FT /evidence="ECO:0000250|UniProtKB:P69327"
SQ SEQUENCE 610 AA; 67485 MW; 2B0CBC8F4769E795 CRC64;
MRVTSLLWSS LVIPAAVGFQ VRFKPSEDTA LDTVDDGTLQ SLLDNIGLNG SNAWDTRPGL
VIASPSKKDP NYFFTWTRDS ALVLKCITDA FAAGNTALQE TIHEYISSQA RIQLLNTRSG
GLSSGGLGEP KYRVDETPYN EDWGRPQADG PALRATALIA YARWLLENDY YDVAKSIVWP
VVKNDLSYVS EHWNTTAFDL WEEVNSPSFF TTIVQHRALV EGINIARALD ETCPHCESQA
PQALCYLQSY WTGTAVRSNY GQGRSGLDVA SILGSIHTFD PEGECDDTTF QPCSARALAN
HKAVTDSFRS IYKINGGIKQ GEAVAVGRYP EDVYFNGNPW YLATYAAAEQ LYDAMYQWNK
IGKITVTDVS MPFFKDIYPE VQTGTHESSS PEFGNIIAAV KAYAEGYIEV AKKYTPCTGM
LSEQFSRDNG TPLSVADLTW SYASYLTVMA RRNSVVPASW GEKNARDIPS TCVPSSATGP
YQTATITHWP PNLTPTAQPS PCPTALPTKN NVRFRLLATT QVGEDVFLVG SIPELGSWDV
KKAVPLNADI YADNCHQWYV DIELPTAVAF EYKFIRKRGG EVVWEQDPNR KYTVPQTCGV
SGAIKRDTWR
