ID B7UAM4_BACIU Unreviewed; 499 AA.
AC B7UAM4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
OS Bacillus subtilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423 {ECO:0000313|EMBL:ACK38261.1};
RN [1] {ECO:0000313|EMBL:ACK38261.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I15 {ECO:0000313|EMBL:ACK38261.1};
RX PubMed=19669599; DOI=10.1007/s11033-009-9635-y;
RA Yang D., Weng H., Wang M., Xu W., Li Y., Yang H.;
RT "Cloning and expression of a novel thermostable cellulase from newly
RT isolated Bacillus subtilis strain I15.";
RL Mol. Biol. Rep. 37:1923-1929(2010).
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; FJ464332; ACK38261.1; -; Genomic_DNA.
DR AlphaFoldDB; B7UAM4; -.
DR SMR; B7UAM4; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR BRENDA; 3.2.1.4; 658.
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_5002864650"
FT DOMAIN 350..499
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
SQ SEQUENCE 499 AA; 55375 MW; 28AAB0F69D9B272A CRC64;
MKRSISIFIT CLLITLLTMG GMMASPASAA GTKTPVAKNG QLSIKGTQLV NRDGKAVQLK
GISSHGLQWY GEYVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK
ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI
KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADDQLK DANVMYALHF YAGTHGQFLR
DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLKY LDSKTISWVN WNLSDKQESS
SALKPGASKT GGWRLSDLSA SGTFVRENIL GTKDSTRDIP ETPAKDKPTQ ENGISVQYRA
GDGSMNSNQI RPQLQIKNNG NTTVDLKDVT ARYWYKAKNK GQNFDCDYAQ IGCGNVTHKF
VTLHKPKQGA DTYLELGFKN GTLAPGASTG NIQLRLHNDD WSNYEQSGDY SFFKSNTFKT
TKKITLYDQG KLIWGTEPN
//
