ID GUNW_PECPM Reviewed; 505 AA. AC Q59395; K4FVJ3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2013, sequence version 2. DT 24-JAN-2024, entry version 124. DE RecName: Full=Endoglucanase 6; DE EC=3.2.1.4; DE AltName: Full=Cellulase V1; DE AltName: Full=Endo-1,4-beta-glucanase V1; DE AltName: Full=Endoglucanase V1; DE Flags: Precursor; GN Name=celV1; OrderedLocusNames=W5S_2582; OS Pectobacterium parmentieri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=1905730; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=SCC3193; RX PubMed=7715600; DOI=10.1007/bf00425817; RA Mae A., Heikinheimo R., Palva E.T.; RT "Structure and regulation of the Erwinia carotovora subspecies carotovora RT SCC3193 cellulase gene celV1 and the role of cellulase in RT phytopathogenicity."; RL Mol. Gen. Genet. 247:17-26(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCC3193; RX PubMed=23045508; DOI=10.1128/jb.00681-12; RA Koskinen J.P., Laine P., Niemi O., Nykyri J., Harjunpaa H., Auvinen P., RA Paulin L., Pirhonen M., Palva T., Holm L.; RT "Genome sequence of Pectobacterium sp. strain SCC3193."; RL J. Bacteriol. 194:6004-6004(2012). 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 -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family. CC {ECO:0000305}. 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; X79241; CAA55823.1; -; Genomic_DNA. DR EMBL; CP003415; AFI90670.1; -; Genomic_DNA. DR PIR; S54744; S54744. DR RefSeq; WP_014700240.1; NZ_WABU01000004.1. DR AlphaFoldDB; Q59395; -. DR SMR; Q59395; -. DR STRING; 1905730.W5S_2582; -. DR CAZy; CBM3; Carbohydrate-Binding Module Family 3. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR GeneID; 66802965; -. DR KEGG; pec:W5S_2582; -. DR PATRIC; fig|1166016.3.peg.2610; -. DR eggNOG; COG2730; Bacteria. DR HOGENOM; CLU_012932_1_1_6; -. DR OMA; NVMYALH; -. DR OrthoDB; 9775889at2; -. DR Proteomes; UP000008044; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; Cellulose degradation; Glycosidase; Hydrolase; KW Polysaccharide degradation; Secreted; Signal. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT CHAIN 32..505 FT /note="Endoglucanase 6" FT /id="PRO_0000007859" FT DOMAIN 353..505 FT /note="CBM3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513" FT REGION 32..334 FT /note="Catalytic" FT REGION 333..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 335..352 FT /note="Linker" FT COMPBIAS 340..354 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 168 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O85465" FT ACT_SITE 256 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 68..69 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 130 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 262..263 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 290 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT BINDING 295..297 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:O85465" FT CONFLICT 446 FT /note="Missing (in Ref. 1; CAA55823)" FT /evidence="ECO:0000305" FT CONFLICT 482 FT /note="V -> I (in Ref. 1; CAA55823)" FT /evidence="ECO:0000305" SQ SEQUENCE 505 AA; 55020 MW; 1E714E05E56453D3 CRC64; MWLRRKQIVR KLTLGVVTTM LGMSLSFSAL SATPVETHGQ LSIENGRLVD EQGKRVQLRG ISSNGLQWVG DYVNKDSMKW LRDDWGINVF RVAMYTAENG YIANPSLANK VKEAVAAAQG LGVYIIIDWH TLSDNDPNTY KAQAKIFFAE MAGLYGNSPN VIYEIANEPN GSVTWNGQIR PYALEVTDTI RSKDPDNLII VGSGTWSQDI HDAADNQLPD PNTLYALHFY AGTHGQFLRD RIDYAQSRGA AIFVSEWGTS DASGNGGPFL PESQTWIDFL NNRGISWVNW SLSDKSETSA ALVAGASKSG GWTEQNLSTS GKFVREQIRA GAGLSGGDTP TMPTEPTNPG NGTTGDIVLQ YRNVDNNPSD DAIRMAFNIK NTGSTPIKLS DLQVRYYFHD DGKPGANLFV DWANVGPNNI VTSTGTPAAS TDKANRYVLV TFASGAGSLQ PGAETGEVQV RIHAGDWSNV NETNDYSYGP NVTSYTNWDK ITVHDKGTLV WGTEP //