ID   GUX2_AGABI              Reviewed;         506 AA.
AC   Q92400;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Exoglucanase;
DE            EC=3.2.1.91;
DE   AltName: Full=1,4-beta-cellobiohydrolase;
DE   AltName: Full=Beta-glucancellobiohydrolase;
DE   AltName: Full=Exocellobiohydrolase;
DE   Flags: Precursor;
GN   Name=cel2;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=D649;
RX   PubMed=9025297; DOI=10.1099/00221287-143-1-239;
RA   Yague E., Mehak-Zunic M., Morgan L., Wood D.A., Thurston C.F.;
RT   "Expression of CEL2 and CEL4, two proteins from Agaricus bisporus with
RT   similarity to fungal cellobiohydrolase I and beta-mannanase, respectively,
RT   is regulated by the carbon source.";
RL   Microbiology 143:239-244(1997).
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=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC         and cellotetraose, releasing cellobiose from the non-reducing ends of
CC         the chains.; EC=3.2.1.91;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; Z50094; CAA90422.1; -; mRNA.
DR   AlphaFoldDB; Q92400; -.
DR   SMR; Q92400; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase 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   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; -; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..506
FT                   /note="Exoglucanase"
FT                   /id="PRO_0000007917"
FT   DOMAIN          470..506
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          19..450
FT                   /note="Catalytic"
FT   REGION          405..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..473
FT                   /note="Linker"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        478..495
FT                   /evidence="ECO:0000250"
FT   DISULFID        489..505
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   506 AA;  54320 MW;  0D0390CA4E71BC55 CRC64;
     MFPRSILLAL SLTAVALGQQ VGTNMAENHP SLTWQRCTSS GCQNVNGKVT LDANWRWTHR
     INDFTNCYTG NEWDTSICPD GVTCAENCAL DGADYAGTYG VTSSGTALTL KFVTESQQKN
     IGSRLYLMAD DSNYEIFNLL NKEFTFDVDV SKLPCGLNGA LYFSEMAADG GMSSTNTAGA
     KYGTGYCDSQ CPRDIKFIDG EANSEGWEGS PNDVNAGTGN FGACCGEMDI WEANSISSAY
     TPHPCREPGL QRCEGNTCSV NDRYATECDP DGCDFNSFRM GDKSFYGPGM TVDTNQPITV
     VTQFITDNGS DNGNLQEIRR IYVQNGQVIQ NSNVNIPGID SGNSISAEFC DQAKEAFGDE
     RSFQDRGGLS GMGSALDRGM VLVLSIWDDH AVNMLWLDSD YPLDASPSQP GISRGTCSRD
     SGKPEDVEAN AGGVQVVYSN IKFGDINSTF NNNGGGGGNP SPTTTRPNSP AQTMWGQCGG
     QGWTGPTACQ SPSTCHVIND FYSQCF