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
//