GUNZ_DICD3
ID GUNZ_DICD3 Reviewed; 426 AA.
AC P07103; E0SIP0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Endoglucanase Z;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase Z;
DE AltName: Full=Endo-1,4-beta-glucanase Z;
DE Short=EGZ;
DE Flags: Precursor;
GN Name=celZ; Synonyms=cel5, cel5Z; OrderedLocusNames=Dda3937_02793;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=2835589; DOI=10.1111/j.1365-2958.1988.tb00017.x;
RA Guiseppi A., Cami B., Aymeric J.-L., Ball G., Creuzet N.;
RT "Homology between endoglucanase Z of Erwinia chrysanthemi and
RT endoglucanases of Bacillus subtilis and alkalophilic Bacillus.";
RL Mol. Microbiol. 2:159-164(1988).
RN [2]
RP SEQUENCE REVISION, AND DISULFIDE BOND.
RX PubMed=8152378; DOI=10.1111/j.1365-2958.1994.tb00335.x;
RA Bortoli-German I., Brun E., Py B., Chippaux M., Barras F.;
RT "Periplasmic disulphide bond formation is essential for cellulase secretion
RT by the plant pathogen Erwinia chrysanthemi.";
RL Mol. Microbiol. 11:545-553(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [4]
RP MUTAGENESIS, AND DOMAINS.
RX PubMed=1677466; DOI=10.1093/protein/4.3.325;
RA Py B., Bortoli-German I., Haiech J., Chippaux M., Barras F.;
RT "Cellulase EGZ of Erwinia chrysanthemi: structural organization and
RT importance of His98 and Glu133 residues for catalysis.";
RL Protein Eng. 4:325-333(1991).
RN [5]
RP STEREOCHEMISTRY OF THE REACTION.
RC STRAIN=3937;
RX PubMed=1563515; DOI=10.1016/0014-5793(92)80183-h;
RA Barras F., Bortoli-German I., Bauzan M., Rouvier J., Gey C., Heyraud A.,
RA Henrissat B.;
RT "Stereochemistry of the hydrolysis reaction catalyzed by endoglucanase Z
RT from Erwinia chrysanthemi.";
RL FEBS Lett. 300:145-148(1992).
RN [6]
RP STRUCTURE BY NMR OF 365-426.
RX PubMed=9405041; DOI=10.1021/bi9718494;
RA Brun E., Moriaud F., Gans P., Blackledge M.J., Barras F., Marion D.;
RT "Solution structure of the cellulose-binding domain of the endoglucanase Z
RT secreted by Erwinia chrysanthemi.";
RL Biochemistry 36:16074-16086(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 44-335.
RX PubMed=11501995; DOI=10.1006/jmbi.2001.4787;
RA Chapon V., Czjzek M., El Hassouni M., Py B., Juy M., Barras F.;
RT "Type II protein secretion in Gram-negative pathogenic bacteria: the study
RT of the structure/secretion relationships of the cellulase Cel5 (formerly
RT EGZ) from Erwinia chrysanthemi.";
RL J. Mol. Biol. 310:1055-1066(2001).
CC -!- FUNCTION: Represents 97% of the global cellulase activity.
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; Y00540; CAA68604.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM99099.1; -; Genomic_DNA.
DR PIR; S03767; S03767.
DR RefSeq; WP_013318538.1; NC_014500.1.
DR PDB; 1AIW; NMR; -; A=367-426.
DR PDB; 1EGZ; X-ray; 2.30 A; A/B/C=44-334.
DR PDBsum; 1AIW; -.
DR PDBsum; 1EGZ; -.
DR AlphaFoldDB; P07103; -.
DR SMR; P07103; -.
DR STRING; 198628.Dda3937_02793; -.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblBacteria; ADM99099; ADM99099; Dda3937_02793.
DR GeneID; 9734341; -.
DR KEGG; ddd:Dda3937_02793; -.
DR PATRIC; fig|198628.6.peg.2889; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_012932_1_2_6; -.
DR OMA; NDKNEGA; -.
DR OrthoDB; 1395441at2; -.
DR BioCyc; DDAD198628:DDA3937_RS13605-MON; -.
DR EvolutionaryTrace; P07103; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR032798; CBM_5_12_2.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF14600; CBM_5_12_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51055; SSF51055; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..43
FT CHAIN 44..426
FT /note="Endoglucanase Z"
FT /id="PRO_0000007860"
FT REGION 44..332
FT /note="Catalytic"
FT REGION 333..366
FT /note="Linker"
FT REGION 336..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..426
FT /note="Cellulose-binding"
FT ACT_SITE 176
FT /note="Proton donor"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT DISULFID 368..425
FT /evidence="ECO:0000269|PubMed:8152378"
FT MUTAGEN 141
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1677466"
FT MUTAGEN 176
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1677466"
FT CONFLICT 293..295
FT /note="SNA -> QLTQ (in Ref. 1; CAA68604)"
FT /evidence="ECO:0000305"
FT CONFLICT 350..364
FT /note="TDTTVDEPTTTDTPA -> MTPPLTNRPQPTHRQ (in Ref. 1;
FT CAA68604)"
FT /evidence="ECO:0000305"
FT CONFLICT 388..426
FT /note="THNEAGQSIVYKGNLYTANWYTASVPGSDSSWTQVGSCN -> LITKQANRS
FT STKATCIPQTGTPHPFRAAIPPGRRLVAVTN (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1EGZ"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1EGZ"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:1EGZ"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1EGZ"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:1EGZ"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:1AIW"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:1AIW"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:1AIW"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:1AIW"
FT STRAND 401..409
FT /evidence="ECO:0007829|PDB:1AIW"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:1AIW"
SQ SEQUENCE 426 AA; 46418 MW; E78F2EE021FCA5DA CRC64;
MPLSYLDKNP VIDSKKHALR KKLFLSCAYF GLSLACLSSN AWASVEPLSV NGNKIYAGEK
AKSFAGNSLF WSNNGWGGEK FYTADTVASL KKDWKSSIVR AAMGVQESGG YLQDPAGNKA
KVERVVDAAI ANDMYAIIGW HSHSAENNRS EAIRFFQEMA RKYGNKPNVI YEIYNEPLQV
SWSNTIKPYA EAVISAIRAI DPDNLIIVGT PSWSQNVDEA SRDPINAKNI AYTLHFYAGT
HGESLRNKAR QALNNGIALF VTEWGTVNAD GNGGVNQTET DAWVTFMRDN NISNANWALN
DKNEGASTYY PDSKNLTESG KKVKSIIQSW PYKAGSAASA TTDPSTDTTT DTTVDEPTTT
DTPATADCAN ANVYPNWVSK DWAGGQPTHN EAGQSIVYKG NLYTANWYTA SVPGSDSSWT
QVGSCN
