ID   GUX1_CRYPA              Reviewed;         452 AA.
AC   Q00548;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-SEP-2026, entry version 106.
DE   RecName: Full=Exoglucanase 1;
DE            EC=3.2.1.91;
DE   AltName: Full=1,4-beta-cellobiohydrolase I;
DE   AltName: Full=Beta-glucancellobiohydrolase I;
DE   AltName: Full=Exocellobiohydrolase I;
DE   AltName: Full=Exoglucanase I;
DE   Flags: Precursor;
GN   Name=CBH-1;
OS   Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC   Cryphonectria-Endothia species complex; Cryphonectria.
OX   NCBI_TaxID=5116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8524797; DOI=10.1073/pnas.92.25.11529;
RA   Wang P., Nuss D.L.;
RT   "Induction of a Cryphonectria parasitica cellobiohydrolase I gene is
RT   suppressed by hypovirus infection and regulated by a GTP-binding-protein-
RT   linked signaling pathway involved in fungal pathogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:11529-11533(1995).
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; L43048; AAB00479.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00548; -.
DR   SMR; Q00548; -.
DR   GlyCosmos; Q00548; 3 sites, No reported glycans.
DR   OMA; MADTTHY; -.
DR   BioCyc; MetaCyc:MONOMER-17643; -.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009251; P:glucan catabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   FunFam; 2.70.100.10:FF:000001; Glucanase; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF2; GLYCOSIDE HYDROLASE FAMILY 7 PROTEIN; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..452
FT                   /note="Exoglucanase 1"
FT                   /id="PRO_0000007920"
FT   ACT_SITE        230
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        235
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  48358 MW;  5802FD112C2CA864 CRC64;
     MFSKFALTGS LLAGAVNAQG VGTQQTETHP QMTWQSCTSP SSCTTNQGEV VIDSNWRWVH
     DKDGYVNCYT GNTWNTTLCP DDKTCAANCV LDGADYSSTY GITTSGNALS LQFVTQSSGK
     NIGSRTYLME SSTKYHLFDL IGNEFAFDVD LSKLPCGLNG ALYFVTMDAD GGMAKYSTNT
     AGAEYGTGYC DSQCPRDLKF INGQGNVEGW TPSTNDANAG VGGLGSCCSE MDVWEANSMD
     MAYTPHPCET AAQHSCNADE CGGTYSSSRY AGDCDPDGCD WNPFRMGNKD FYGSGDTVDT
     SQKFTVVTQF HGSGSSLTEI SQYYIQGGTK IQQPNSTWPT LTGYNSITDD FCKAQKVEFN
     DTDVFSEKGG LAQMGAGMAD GMVLVMSLWD DHYANMLWLD STYPVDADAS SPGKQRGTCA
     TTSGVPADVE SSDASATVIY SNIKFGPIGA TY
//