ID   GUNN_PECAT              Reviewed;         444 AA.
AC   Q59394;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Endoglucanase N;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase N;
DE   AltName: Full=Endo-1,4-beta-glucanase N;
DE   Flags: Precursor;
GN   Name=celN;
OS   Pectobacterium atrosepticum (Erwinia carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=29471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9636315; DOI=10.1038/nbt0196-71;
RA   Olsen O., Thomsen K.K., Weber J., Duus J.O., Svendsen I., Wegener C.,
RA   von Wettstein D.;
RT   "Transplanting two unique beta-glucanase catalytic activities into one
RT   multienzyme, which forms glucose.";
RL   Biotechnology (N.Y.) 14:71-76(1996).
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; L39788; AAC37033.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59394; -.
DR   SMR; Q59394; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
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..444
FT                   /note="Endoglucanase N"
FT                   /id="PRO_0000007857"
FT   DOMAIN          356..444
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   REGION          332..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..358
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         64
FT                   /ligand="substrate"
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"
SQ   SEQUENCE   444 AA;  48301 MW;  FA7E4179004CBB43 CRC64;
     MWMRRNQIVR KLTLGVVTTV LGMSLSFSAL SATPVETHGQ LSIENGRLVD EQGKRVQLRG
     VSSHGLQWFG DYVNKDSMKW LRDDWGINVF RVAMYTAADG YISNPSLANK VKEAVAAAQS
     LGVYIIIDWH ILSDNDPNIY KAQAKTFFAE MAGLYGSSPN VIYEIANEPN GGVTWNGQIR
     PYALEVTDTI RSKDPDNLII VGTGTWSQDI HDAADNQLPD PNTLYALHFY AGTHGQFLRD
     RIDYAQSRGA AIFVSEWGTS DASGNGGPFL PESQTWIDFL NNRGVSWVNW SLTDKSEASA
     ALAPGASKSG GWTEQNLSTS GKFVREQIRA GANLGGGDTP TTPTTPTEPT NPGNGTTGDV
     VLQYRNVDNN PSDDAIRMAV NIKNTGSTPI KLSDLQVRYY FHDDGKPGAN LFVDWANVGP
     NNIVTSTGTP AASTDKANRY VLVT