GUX1_CRYPA
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 03-AUG-2022, entry version 96.
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 CAZy; GH7; Glycoside Hydrolase Family 7.
DR CLAE; CBH7A_CRYPA; -.
DR OMA; VYSNIKV; -.
DR BioCyc; MetaCyc:MON-17643; -.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase 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; 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
