ID   GUX1_COCCA              Reviewed;         456 AA.
AC   Q00328;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=CEL1;
OS   Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=5017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Race 1;
RX   PubMed=8589415; DOI=10.1094/mpmi-8-0602;
RA   Sposato P., Ahn J., Walton J.D.;
RT   "Characterization and disruption of a gene in the maize pathogen
RT   Cochliobolus carbonum encoding a cellulase lacking a cellulose binding
RT   domain and hinge region.";
RL   Mol. Plant Microbe Interact. 8:602-609(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; U25129; AAC49089.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00328; -.
DR   SMR; Q00328; -.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
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..456
FT                   /note="Exoglucanase 1"
FT                   /id="PRO_0000007919"
FT   REGION          407..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        237
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   456 AA;  48304 MW;  8014094907DEEA52 CRC64;
     MYRTLAFASL SLYGAARAQQ VGTSTAENHP KLTWQTCTGT GGTNCSNKSG SVVLDSNWRW
     AHNVGGYTNC YTGNSWSTQY CPDGDSCTKN CAIDGADYSG TYGITTSNNA LSLKFVTKGS
     FSSNIGSRTY LMETDTKYQM FNLINKEFTF DVDVSKLPCG LNGALYFVEM AADGGIGKGN
     NKAGAKYGTG YCDSQCPHDI KFINGKANVE GWNPSDADPN GGAGKIGACC PEMDIWEANS
     ISTAYTPHPC RGVGLQECSD AASCGDGSNR YDGQCDKDGC DFNSYRMGVK DFYGPGATLD
     TTKKMTVITQ FLGSGSSLSE IKRFYVQNGK VYKNSQSAVA GVTGNSITES FCTAQKKAFG
     DTSSFAALGG LNEMGASLAR GHVLIMSLWG DHAVNMLWLD STYPTDADPS KPGAARGTCP
     TTSGKPEDVE KNSPDATVVF SNIKFGPIGS TFAQPA