ID   GUN1_HUMGT              Reviewed;         435 AA.
AC   Q12622;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Endoglucanase EG-1;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=EG-1;
OS   Humicola grisea var. thermoidea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Trichocladium;
OC   Trichocladium griseum.
OX   NCBI_TaxID=5528;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IFO 9854;
RA   Takashima S., Nakamura A., Hidaka M., Masaki H., Uozumi T.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC       requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC       cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC       cut the disaccharide cellobiose from the non-reducing end of the
CC       cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC       cellobiose and other short cello-oligosaccharides to glucose.
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 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; D63516; BAA09786.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12622; -.
DR   SMR; Q12622; -.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   CLAE; EGL7A_HUMGT; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; PTHR33753; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..435
FT                   /note="Endoglucanase EG-1"
FT                   /id="PRO_0000007916"
FT   ACT_SITE        217
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        38..44
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        83..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        160..385
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..215
FT                   /evidence="ECO:0000250"
FT   DISULFID        196..214
FT                   /evidence="ECO:0000250"
FT   DISULFID        235..254
FT                   /evidence="ECO:0000250"
FT   DISULFID        243..248
FT                   /evidence="ECO:0000250"
FT   DISULFID        259..335
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   435 AA;  47890 MW;  25EB3D62D96B65FA CRC64;
     MARGTALLGL TSLLLGLVNG QKPGETKEVH PQLTTFRCTK KGGCKPATNY IVLDSLSHPI
     HRAEGLGWGN CGDWGNPPPK DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP
     DGRVPSPRVY LLDKTERRYE MLHLTGFEFT FDVDATKLPC GMNSALYLSE MHPTGAKSKH
     NPGGAYYGTG YCDAQCFVTP FINGLGNIEG KGSCCNEMDI WEANSRASHV APHVCNKKGL
     YLCEGEECAF EGVCDKNGCG WNPYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRKGKL
     EKIHRFYVQD GKIIESFYTN KEGIPYTNMI EDEFCAATGS RKYMELGATQ GMGEALTRGM
     VLAMSIWWDQ GGNMEWLDHG EAGPCAKGEG APSNVVQVEP FPEVTYTNLR WGEIGSTYQE
     VQKPKPKPGP GPRSD