ID   GUN1_EVAC2              Reviewed;         488 AA.
AC   P06566;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Endoglucanase A;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase A;
DE   AltName: Full=Endo-1,4-beta-glucanase A;
GN   Name=celA;
OS   Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM
OS   9156 / N-4) (Bacillus cellulosilyticus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Evansella.
OX   NCBI_TaxID=649639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3782013; DOI=10.1128/jb.168.2.479-485.1986;
RA   Fukumori F., Sashihara N., Kudo T., Horikoshi K.;
RT   "Nucleotide sequences of two cellulase genes from alkalophilic Bacillus sp.
RT   strain N-4 and their strong homology.";
RL   J. Bacteriol. 168:479-485(1986).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; M14781; AAA22301.1; -; Genomic_DNA.
DR   PIR; A25156; A25156.
DR   RefSeq; WP_013487061.1; NC_014829.1.
DR   AlphaFoldDB; P06566; -.
DR   SMR; P06566; -.
DR   STRING; 649639.Bcell_0438; -.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   eggNOG; COG2730; Bacteria.
DR   OrthoDB; 154460at2; -.
DR   SABIO-RK; P06566; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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   CDD; cd12215; ChiC_BD; 2.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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   PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00495; ChtBD3; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..488
FT                   /note="Endoglucanase A"
FT                   /id="PRO_0000184044"
FT   REGION          326..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..357
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..420
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..445
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         63..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         258..259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   BINDING         291..293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
SQ   SEQUENCE   488 AA;  54264 MW;  97248E453D28D3B5 CRC64;
     MKKLTTIFIV FTLALLFVGN STSANNGSVV EQNGQLSIQN GQLVNEHGDP VQLKGMSSHG
     LQWYGQFVNY DSIKWLRDDW GITVFRAAMY TSSGGYIEDP SVKEKVKEAV EAAIDLGIYV
     IIDWHILSDN DPNIYKEEAK EFFDEMSALY GDYPNVIYEI ANEPNGHNVR WDSHIKPYAE
     EVIPVIRAND PNNIVIVGTA TWSQDVHEAA DNQLDDPNVM YAFHFYAGTH GQQLRNQVDY
     ALSRGAAIFV SEWGTSAATG DGGVFLDEAQ VWIDFMDERN LSWANWSLTH KDESSAALMP
     GANPTGGWTA AELSPSGAFV REKIRESASI PPSDPTPPSD PDPGEPDPTP PSDPGEYPAW
     DPNQIYTNEI VYHNGQLWQA KWWTQNQEPG ANQYGPWEPL GDAPPSEPSD PPPPSEPEPD
     PGEPDPGEPD PGEPDPTPPS DPGEYPAWDP TQIYTNEIVY HNGQLWQAKW WTQNQEPGYP
     YGPWEPLN
//