ID   GUN3_HUMIN              Reviewed;         388 AA.
AC   Q12624; Q12620;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Endoglucanase 3;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase 3;
DE   AltName: Full=Endo-1,4-beta-glucanase 3;
DE   Flags: Precursor;
GN   Name=CMC3;
OS   Humicola insolens (Soft-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Humicola.
OX   NCBI_TaxID=34413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8190078; DOI=10.1007/bf00301060;
RA   Dalboege H., Hansen H.P.H.;
RT   "A novel method for efficient expression cloning of fungal enzyme genes.";
RL   Mol. Gen. Genet. 243:253-260(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=IFO 9854;
RX   PubMed=9058960; DOI=10.1271/bbb.61.245;
RA   Takashima S., Nakamura A., Masaki H., Uozumi T.;
RT   "Cloning, sequencing, and expression of a thermostable cellulase gene of
RT   Humicola grisea.";
RL   Biosci. Biotechnol. Biochem. 61:245-250(1997).
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   -!- BIOTECHNOLOGY: Used as a detergent cellulase. Sold under the name
CC       Celluzyme by Novozymes. This special enzyme has three effects: colour
CC       brightening, softening and removal of particulate soil. The overall
CC       effect is that it helps to preserve the nice appearance of new fabric
CC       and restores old fabric so that it looks new again.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X76046; CAA53631.1; -; Genomic_DNA.
DR   EMBL; D84470; BAA12676.1; -; Genomic_DNA.
DR   PIR; JC5461; JC5461.
DR   PIR; S43920; S43920.
DR   AlphaFoldDB; Q12624; -.
DR   SMR; Q12624; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EGL5C_HUMGT; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..388
FT                   /note="Endoglucanase 3"
FT                   /id="PRO_0000007863"
FT   DOMAIN          17..52
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          53..91
FT                   /note="Linker"
FT   REGION          56..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..388
FT                   /note="Catalytic"
FT   COMPBIAS        56..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        322
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..51
FT                   /evidence="ECO:0000250"
FT   CONFLICT        8
FT                   /note="G -> S (in Ref. 2; BAA12676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340
FT                   /note="T -> N (in Ref. 2; BAA12676)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   388 AA;  42564 MW;  C7CF349DACC10690 CRC64;
     MKHSVLAGLF ATGALAQGGA WQQCGGVGFS GSTSCVSGYT CVYLNDWYSQ CQPQPTTLRT
     TTTPGATSTT RSAPAATSTT PAKGKFKWFG INQSCAEFGK GEYPGLWGKH FTFPSTSSIQ
     THINDGFNMF RVAFSMERLA PNQLNAAFDA NYLRNLTETV NFITGKGKYA MLDPHNFGRY
     YERIITDKAA FASFFTKLAT HFASNPLVVF DTNNEYHDMD QQLVFDLNQA AIDAIRAAGA
     TSQYIMVEGN SWTGAWTWNV TNNNLAALRD PENKLVYQMH QYLDSDGSGT STACVSTQVG
     LQRVIGATNW LRQNGKVGLL GEFAGGANSV CQQAIEGMLT HLQENSDVWT GALWWAGGPW
     WGDYIYSFEP PSGIGYTYYN SLLKKYVP