ID   W0V8Y5_9BURK            Unreviewed;      1243 AA.
AC   W0V8Y5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=glucan endo-1,3-beta-D-glucosidase {ECO:0000256|ARBA:ARBA00012780};
DE            EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780};
GN   ORFNames=GJA_3726 {ECO:0000313|EMBL:CDG84341.1};
OS   Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG84341.1, ECO:0000313|Proteomes:UP000027604};
RN   [1] {ECO:0000313|EMBL:CDG84341.1, ECO:0000313|Proteomes:UP000027604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX   PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA   Graupner K., Lackner G., Hertweck C.;
RT   "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT   agaricidamnosum.";
RL   Genome Announc. 3:e00277-e00277(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00000382};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family.
CC       {ECO:0000256|ARBA:ARBA00010730}.
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DR   EMBL; HG322949; CDG84341.1; -; Genomic_DNA.
DR   RefSeq; WP_051781025.1; NZ_HG322949.1.
DR   AlphaFoldDB; W0V8Y5; -.
DR   STRING; 1349767.GJA_3726; -.
DR   KEGG; jag:GJA_3726; -.
DR   PATRIC; fig|1349767.4.peg.314; -.
DR   eggNOG; COG5498; Bacteria.
DR   HOGENOM; CLU_003268_0_0_4; -.
DR   Proteomes; UP000027604; Chromosome I.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProt.
DR   GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR   GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR   InterPro; IPR005200; Endo-beta-glucanase.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040720; GH81_C.
DR   InterPro; IPR040451; GH81_N.
DR   PANTHER; PTHR31983; ENDO-1,3(4)-BETA-GLUCANASE 1; 1.
DR   PANTHER; PTHR31983:SF0; ENDO-1,3(4)-BETA-GLUCANASE 2; 1.
DR   Pfam; PF00754; F5_F8_type_C; 3.
DR   Pfam; PF17652; Glyco_hydro81C; 1.
DR   Pfam; PF03639; Glyco_hydro_81; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR   PROSITE; PS50022; FA58C_3; 3.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDG84341.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027604}.
FT   DOMAIN          34..179
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          188..328
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          1098..1240
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
SQ   SEQUENCE   1243 AA;  136099 MW;  C5D3CD7D27880D51 CRC64;
     MHSALPSRKV HRLYHASRLS ALRPALKRIA AVGLALQLAG IVSAYAQTTP YLMSVNKPVY
     GSSVSGANTP DLAVDGSLGS RWESAHGKDP QWVYVDLGAH ASITRVVVNW EGAFASQYQI
     EVSDDEIHWN PVWSTTNNNS TLNDIALPAG TAGRFVRLLG TKRNTAYGYS IYEFSVYGTG
     ASGGPATAPA PDIALHTPVT ASSDEAQQPG HPAELTPKDY LASNITDDDA TSRWSSRYSD
     NEWIQVDLGS SKVIGAVELN WQNAYGRAYD IQVSDNGSNW TTVYRQLAGA GGNDKVALYA
     SGRYVRMQGI ARGTPFGYSL FGFKVYPYRD GDPKPAYPLP AVTTPQVVQV GKGSYEIGDL
     SQPEPPPPLF KTANISGPIP SNDWWQSLLI ANLGNGNSLV TLPLRSKYTK SGLALTTIDA
     GYVAADGGAI DTDSEPDLYI RPSNLVPANL KTKVSGYGDY SVNVIMSDDD SAKMTSTLVQ
     GSPFVYNTFV NPDKVQLTSY NIKRLFDDAG NTILANDFES YQGDHIGIEL ETTNKAPQPQ
     TATRWYGVFA PAGSTFLRIG STIKVTLANG QNFMSLATLT APGDLPGYYQ RAYAFVSDTK
     VDYHYDPATS LVTTNFNTST DVKRNGFSGE TLMGLMPHQW KLSGAALNGR EYASVRGQIK
     LHEGNSFTTT DRFYGVIPQF VEPKNPEYSR ARLSGYLDQL DQSLAGGLMN DDPYWQGKAL
     HPLAMATLIA DQIGDASRRQ RYLSQLKTIL SDWLTYSPTE RKHGTYFHYV PSWGSLVAYN
     TGFGLNTGLT DHHFTYGYFT FAAAVLATYD SQFVSDYGPM VEMLIRDYAN PSRTDPLFPQ
     LRNFNPYEGH SWAGGFGDNT SGNNQEAAGE ALFSWVGQYL WGLATNNTAY RDTGIYGFTT
     EEKATEQYWF NYDRDNWTPA YQHGGVGQVY GSSYRYGTYF EGRPPFIYGI HWVPTAEWLT
     YYGRDVSRAN DLYNSMVADN GGTEQVWQHI IWPFQSLSDA PAVLRKFDAS VMQQNEVFNS
     YWFINSMATL GQRSNDIWSV NWPAATVYRN ASGYTAQVWN PGDTARTVQF SNAGGGIIGS
     AVVPARATIA VDPTKTVTTP PVVTPPLDPY LSRDGWSAST SAPNGEPAAN MLDGKLTTRW
     STAQSQQPGQ WVQIDMKQQK SFDTLFVNAG SAGDQMKGYQ VFVSNDGVNW GAAVASGADA
     NQNALIVLPR QNARYIKLVQ TGTASNWWSI VELRVANFGS ATQ
//