ID A0A0A2MSM2_9FLAO Unreviewed; 1272 AA.
AC A0A0A2MSM2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=Q766_00300 {ECO:0000313|EMBL:KGO94601.1};
OS Flavobacterium subsaxonicum WB 4.1-42 = DSM 21790.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121898 {ECO:0000313|EMBL:KGO94601.1, ECO:0000313|Proteomes:UP000030111};
RN [1] {ECO:0000313|EMBL:KGO94601.1, ECO:0000313|Proteomes:UP000030111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 4.1-42 {ECO:0000313|EMBL:KGO94601.1,
RC ECO:0000313|Proteomes:UP000030111};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO94601.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRLY01000001; KGO94601.1; -; Genomic_DNA.
DR RefSeq; WP_026991984.1; NZ_KE383909.1.
DR AlphaFoldDB; A0A0A2MSM2; -.
DR STRING; 1121898.GCA_000422725_00537; -.
DR eggNOG; COG2133; Bacteria.
DR eggNOG; COG5498; Bacteria.
DR OrthoDB; 954626at2; -.
DR Proteomes; UP000030111; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04080; CBM6_cellulase-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 4.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040720; GH81_C.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
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; PF03422; CBM_6; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 4.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50022; FA58C_3; 2.
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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000030111};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1272
FT /note="glucan endo-1,3-beta-D-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001992760"
FT DOMAIN 175..315
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 902..1043
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1057..1176
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
SQ SEQUENCE 1272 AA; 138450 MW; 0AFC5F3E7F328559 CRC64;
MKHIYLCAAA LALGLWQANA QTPVAVGSGS YASAVPAAED IDWNEDGVGD IFPFINTQTI
YVQPGETRPI PTNDWWTSLL VEQYSGLLWA YPLMVDAESY GPRIFFPNSF SADGSNIVYG
GSMMIKATGY TPEKAIAKDW SDWGVVMGIP DAAHNKNIDV TMAHGIPFVW LQTQGVNPEL
SFDAGASYLT AAGTAVQFPT TSSFVVQTDG RYMGVHLPGN ASAEIQNQQY VQIDLGSTQP
ITKVSLNWEA AFAKGYGIQV STNGSTWTSV ATETNGNGGI DDITLNTSGR YVRVVFNERG
TIYAYSLWEV SIFNGATLLS LNKTATAAST EANYFATSLT DGNTGTRWAS DASQFEKLVI
NTGNGGSYFV VSALHNPAEL TTYETYAFNR VTNTQVLYDY TAATGKVATT WNITTANLKG
QANGNTVQGF LPHLYYNAAN TVNFNTPTYV SPRGTLKTAN GKSFTFTYDF NGIIPSYNSP
YSNSADAHPY DADVMFNLLT NFSKKQGYGG DTYWGGKDLV NYAKYMLMAK EVNHQAYESL
KAKTKESLIN WLTYTPGETE KFFARYDRWK AIVGFNESYG SSQFTDNHFH YGYLIQACAM
YGMVDPQFLT DYGPMIKLVA QQYANWNRND TFLPYLRTFD PWIGHSYAGG TSSSTGNNQE
STSEAMQSWT GLFLLGDMLN DESIRDVGAF GYTTESFATL EYWFDWKNRN LPAAYPHDVV
GILSNQGFAY GTYFSASPVH IHGIQYLPVN PGFKYLARDK QWAAGEYADM MTESAAIDGH
QNELDFGDDW AHVALGFRQL YDPEYVAGFM EDNLALAPTS PDYIMDYEAA GMTYYYTHAN
QNLGDFSFNY RTNFPTSSTF EVNGTFSHAV AYNPTATAKT CTIYNSSNGV VGSFTVPAYT
MVTYPSLPTT GQQPTGCYGL APVAATATSG GNSIAAAIDG NLGSRWESAF ADPQTLTVDL
GVSSHVDAIT LSWEAANAKD YTLSGSVDGN TWAPVATKTN MAAGARTDVI TNVNANYRYL
RMIGTARTIP YGYSIYEFEV CGSAASTPTT NFVTLPAQIQ AESYTAQSGV QLETTSDTGA
GQNVGYIDTN DYMDYQVYAP TAGSYPVQFR ISSPYTGTSI QLLSNGNAVG TYTLTNTGGW
QTWQTVNGTV TLPAGNQTLR VKANVGGFNL NWFNVGNVGS GLRFGNLGTG EKETDEVSGS
FTSVTQIYPN PAHNLINVVT DKDADVAIYN VNGALIKQQA VKQGESQINI EGFASGVYFV
RVGQETFKLA VE
//
