ID   GUN1_STRHA              Reviewed;         321 AA.
AC   P33682;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Endoglucanase 1;
DE            EC=3.2.1.4;
DE   AltName: Full=CEL1;
DE   AltName: Full=CMCase I;
DE   AltName: Full=Cellulase I;
DE   AltName: Full=Endo-1,4-beta-glucanase 1;
DE   Flags: Precursor;
GN   Name=celA1;
OS   Streptomyces halstedii.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-33.
RC   STRAIN=JM8 / CECT3310;
RX   PubMed=1400190; DOI=10.1128/jb.174.20.6368-6376.1992;
RA   Fernandez-Abalos J.M., Sanchez P., Coll-Fresno P.M., Villanueva J.R.,
RA   Perez P., Santamaria R.I.;
RT   "Cloning and nucleotide sequence of celA1, and endo-beta-1,4-glucanase-
RT   encoding gene from Streptomyces halstedii JM8.";
RL   J. Bacteriol. 174:6368-6376(1992).
CC   -!- FUNCTION: Implicated in the mechanism of induction exerted by
CC       cellobiose.
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 6 (cellulase B) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; Z12157; CAA78145.1; -; Genomic_DNA.
DR   AlphaFoldDB; P33682; -.
DR   SMR; P33682; -.
DR   CAZy; GH6; Glycoside Hydrolase Family 6.
DR   PRIDE; P33682; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.40; -; 1.
DR   InterPro; IPR016288; Beta_cellobiohydrolase.
DR   InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR   InterPro; IPR001524; Glyco_hydro_6_CS.
DR   PANTHER; PTHR34876; PTHR34876; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   SUPFAM; SSF51989; SSF51989; 1.
DR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:1400190"
FT   CHAIN           28..321
FT                   /note="Endoglucanase 1"
FT                   /id="PRO_0000007906"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        149
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT   ACT_SITE        295
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        112..156
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  33695 MW;  DC5E39EF3CCD114C CRC64;
     MSRKLRTLMA ALCALPLAFA AAPPAHAADP TTMTNGFYAD PDSSASRWAA ANPGDGRAAA
     INASIANTPM ARWFGSWSGA IGTAAGAYAG AADGRDKLPI LVAYNIYNRD YCGGHSAGGA
     ASPSAYADWI ARFAGGIAAR PAVVILEPDS LGDYGCMNPA QIDEREAMLT NALVQFNRQA
     PNTWVYMDAG NPRWADAATM ARRLHEAGLR QAHGFSLNVS NYITTAENTA YGNAVNNELA
     ARYGYTKPFV VDTSRNGNGS NGEWCNPSGR RIGTPTRTGG GAEMLLWIKT PGESDGNCGV
     GSGSTAGQFL PEVAYKMIYG Y