GUNW_PECPM
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 03-AUG-2022, entry version 119.
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; Proteobacteria; 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}.
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DR EMBL; X79241; CAA55823.1; -; Genomic_DNA.
DR EMBL; CP003415; AFI90670.1; -; Genomic_DNA.
DR PIR; S54744; S54744.
DR RefSeq; WP_014700240.1; NZ_QESW01000035.1.
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 EnsemblBacteria; AFI90670; AFI90670; W5S_2582.
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; 1395441at2; -.
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; -; 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; 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
