ID E3VRS9_9BACI Unreviewed; 499 AA.
AC E3VRS9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
OS Bacillus sp. NK-2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=696710 {ECO:0000313|EMBL:ADO85705.1};
RN [1] {ECO:0000313|EMBL:ADO85705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NK-2 {ECO:0000313|EMBL:ADO85705.1};
RA Shen Y., Cai J., Chen Y.;
RT "The Study of Antifungal Substances From Bacillus sp. Strain: NK-2.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966,
CC ECO:0000256|RuleBase:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; HQ214668; ADO85705.1; -; Genomic_DNA.
DR AlphaFoldDB; E3VRS9; -.
DR SMR; E3VRS9; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361153}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..499
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003181998"
FT DOMAIN 350..499
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT REGION 326..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 55148 MW; F532AFEC43F11859 CRC64;
MKRSISVFIT CLLIAVLTMG GLLPSPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK
GISSHGLQWY GDFVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK
ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI
KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQFLR
DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLNY LDSKKISWVN WNLSDKQESS
SALKPGASKT GGWPLSDLTA SGTFVRENIR GTKDSTKDGP ETPAQDNPTQ EKGVSVQYKA
GDGLVNSNQI RPQLHIKNNG NATVDLKDVT ARYWYNVKNK GQNFDCDYAQ MGCGNLTHKF
VTLHKPKQGA DTYLELGFKT GTLSPGASTG NIQLRLHNDD WSNYAQSGDY SFFQSNTFKT
TKKITLYHQG KLIWGTEPN
//
