ID U3R8K1_9BACT Unreviewed; 499 AA.
AC U3R8K1;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AGW99973.1};
RN [1] {ECO:0000313|EMBL:AGW99973.1}
RP NUCLEOTIDE SEQUENCE.
RA Pandey S., Tiwari R., Nain L., Saxena A.K.;
RT "Diversity of endoglucanase gene in bacillus species.";
RL Submitted (JUN-2013) 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|RuleBase:RU361153}.
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; KF240843; AGW99973.1; -; Genomic_DNA.
DR AlphaFoldDB; U3R8K1; -.
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|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:AGW99973.1};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW 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_5004648110"
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; 55105 MW; B4FAA33FDD9CA11A CRC64;
MKRSISIFIT CLLIAVLTMG GLLPSPASAG GTKTPAAKNG QLSIKGTQLV NRDGKAVQLK
GISSHGLQWY GDFVNKDSLK WLRDDWGITV FRAAMYTADG GYIDNPSVKN KVKEAVEAAK
ELGIYVIIDW HILNDGNPNQ NKEKAKEFFK EMSSLYGNTP NVIYEIANEP NGDVNWKRDI
KPYAEEVISV IRKNDPDNII IVGTGTWSQD VNDAADAQFK DANVLYALHF YAGTHGQFLR
DKANYALSKG APIFVTEWGT SDASGNGGVF LDQSREWLNY LDSKNISWVN WNLSDKQESS
SALKPGASKT GGWPLTDLTA SGTFVRENIR GTKDSTKDGP ETPAQDNPTQ EKGVSVQYKA
GDGRVNSNQI RPQLHIKNNG DAMVDLKDVT ARYWYNAKNK GQNVDCDYAQ MGCGNLTHKF
VTLHKPKQGA DTYLELGFKT GTLSPGASTG NIQLRLHNDD WSNYAQSGDY SFFQSNTFKT
TKKITLYHQG KQIWGTEPN
//