ID   EXG1_COCCA              Reviewed;         788 AA.
AC   P49426;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Glucan 1,3-beta-glucosidase;
DE            EC=3.2.1.58;
DE   AltName: Full=1,3-beta-D-glucanohydrolase;
DE   AltName: Full=Exo-beta 1,3 glucanase;
DE   Flags: Precursor;
GN   Name=EXG1;
OS   Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=5017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 90305 / SB111 / 2R15;
RX   PubMed=8135518; DOI=10.1128/aem.60.2.594-598.1994;
RA   Schaeffer H.J., Leykam J., Walton J.D.;
RT   "Cloning and targeted gene disruption of EXG1, encoding exo-beta 1, 3-
RT   glucanase, in the phytopathogenic fungus Cochliobolus carbonum.";
RL   Appl. Environ. Microbiol. 60:594-598(1994).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   AGRICOLA=IND92032302; DOI=10.1016/0885-5765(91)90034-F;
RA   van Hoof A., Leykam J., Schaeffer H.J., Walton J.D.;
RT   "A single beta 1,3-glucanase secreted by the maize pathogen Cochliobolus
RT   carbonum acts by an exolytic mechanism.";
RL   Physiol. Mol. Plant Pathol. 39:259-267(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 55 family. {ECO:0000305}.
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DR   EMBL; L48994; AAC71062.1; -; Genomic_DNA.
DR   AlphaFoldDB; P49426; -.
DR   SMR; P49426; -.
DR   CAZy; GH55; Glycoside Hydrolase Family 55.
DR   CLAE; EXG55A_COCCA; -.
DR   BRENDA; 3.2.1.58; 1551.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 2.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   Pfam; PF12708; Pectate_lyase_3; 2.
DR   SUPFAM; SSF51126; SSF51126; 2.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..42
FT   CHAIN           43..788
FT                   /note="Glucan 1,3-beta-glucosidase"
FT                   /id="PRO_0000012226"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        773
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   788 AA;  84013 MW;  DD202BC4400DE750 CRC64;
     MRFSSLLACL GAVGIQAAAI PFQRRVDNTT DSGSLDAAQA AAAIVDGYWL NDLSGKGRAP
     FNSNPNYKVF RNVKDYGAKG DGVTDDSDAF NRAISDGSRC GPWVCDSSTD SPAVVYVPSG
     TYLINKPIIF YYMTALIGNP RELPVLKAAS SLQALALIDG SPYSNQNGEP GWISTNLFLR
     QIRNLIIDGT AVAPTSGFQA IHWPASQATT IQNVKIRMTQ ASNSVHAGIF VENGSGGHMA
     DLDITGGLYG MNIGNQQFTM RNVKISKAVV GISQIWNWGW LYSGLQISDC GTAFSMVNGG
     SAGKQEVGSA VIIDSEITNC QKFVDSAWSQ TSNPTGSGQL VIENIKLTNV PAAVVSNGAT
     VLAGGSLTIQ TWGQGNKYAP NASGPSKFQG AISGATRPTG LLQNGKFYSK SKPQYETLST
     SSFISARGAG ATGDGVTDDT RAVQAAVTQA ASQNKVLFFE HGVYKVTNTI YVPPGSRMVG
     EIFSAIMGSG STFGDQANPV PIIQIGKPGE SGSIEWSDMI VQTQGATPGA IVIQYNLNTA
     LGSGLWDVHT RIGGAKGTNL QVAQCPAVLG QVKPECFSAH TNVHVTKGAN GAYFENNWFW
     TADHDLDDAD STRINIYTGR GFHVEANNVW IWANGAEHHT MYQYQFNAAQ DIFAGYIQTE
     TPYFQPTPIA PLPYVSSSKY SDPVYSSSQT SAWGLRLLDA KNVLIYGGGL YSFFDNYDVG
     CSSPTAPNGF RDCQTRILSI EGSTSVQAFG FSEVGVEWMV TAAGQDKANW KDNLSVYPTT
     IGYLSYGF