ID C7T4H7_PECCA Unreviewed; 441 AA. AC C7T4H7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 11-DEC-2019, entry version 38. DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153}; DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153}; OS Pectobacterium carotovorum (Erwinia carotovora). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=554 {ECO:0000313|EMBL:ACO59153.1}; RN [1] {ECO:0000313|EMBL:ACO59153.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 15713 {ECO:0000313|EMBL:ACO59153.1}; RA Choi S.-G., Kim S.-D.; RT "Cloning and expression of cellulase genes from Erwinia carotovora in E. RT coli."; RL Submitted (APR-2009) 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|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; FJ890934; ACO59153.1; -; Genomic_DNA. DR CAZy; CBM3; Carbohydrate-Binding Module Family 3. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR eggNOG; ENOG4107QWR; Bacteria. DR eggNOG; COG2730; LUCA. 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; -; 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 Pfam; PF00942; CBM_3; 1. DR Pfam; PF00150; Cellulase; 1. DR SMART; SM01067; CBM_3; 1. DR SUPFAM; SSF49384; SSF49384; 1. DR SUPFAM; SSF51445; SSF51445; 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|RuleBase:RU361153}; KW Hydrolase {ECO:0000256|RuleBase:RU361153}; KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..31 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 32..441 FT /note="Endoglucanase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002984728" FT DOMAIN 353..441 FT /note="CBM3" FT /evidence="ECO:0000259|PROSITE:PS51172" FT REGION 332..356 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 334..356 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 441 AA; 48107 MW; FD2B13412A45FD9F CRC64; MWMRRNQIVR KLTLGVVTTV LGMSLSFSAL SATPVETHGQ LSIENGRLVD EQGKRVQLRG VSSHGLQWFG DYVNKDSMKW LRDDWGINVF RVAMYTAADG YISNPSLANK VKEAVAAAQS LGVYIIIDWH ILSDNDPNIY KAQAKTFFAE MAGLYGSSPN VIYEIANEPN GGVTWNGQIR PYALEVTDTI RSKDPDNLII VGTGTWSQDI HDAADNQLPD PNTMYALHFY AGTHGQFLRD RIDYAQSRGA AIFVSEWGTS DASGNGGPFL PESQTWIDFL NNRGVSWVNW SLTDKSEASA ALAPGASKSG GWTEQNLSTS GKFVREQIRA GADLSNGDTP TTPTEPTNPG NGTTGDVVLQ YRNVDNNPSD DAIRMAVNIK NTGSTPIKLS DLQVRYYFHD DGKPGANLFV DWANVGPNNI VTSTGTPAAS TDKANRYVLV T //