GUX1_TRIKO
ID GUX1_TRIKO Reviewed; 513 AA.
AC P62695; P00725;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Exoglucanase 1;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase;
DE AltName: Full=Exocellobiohydrolase I;
DE Short=CBHI;
DE AltName: Full=Exoglucanase I;
DE Flags: Precursor;
GN Name=cbh1;
OS Trichoderma koningii (Hypocrea koningii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=97093;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G-39;
RX PubMed=7764306; DOI=10.1007/bf01575983;
RA Wey T.T., Hseu T.H., Huang L.;
RT "Molecular cloning and sequence analysis of the cellobiohydrolase I gene
RT from Trichoderma koningii G-39.";
RL Curr. Microbiol. 28:31-39(1994).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR EMBL; X69976; CAA49596.1; -; Genomic_DNA.
DR AlphaFoldDB; P62695; -.
DR BMRB; P62695; -.
DR SMR; P62695; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR BioCyc; MetaCyc:MON-17641; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..513
FT /note="Exoglucanase 1"
FT /id="PRO_0000007926"
FT DOMAIN 477..513
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 18..453
FT /note="Catalytic"
FT REGION 401..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..477
FT /note="Linker"
FT ACT_SITE 143
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..89
FT /evidence="ECO:0000250"
FT DISULFID 36..42
FT /evidence="ECO:0000250"
FT DISULFID 67..88
FT /evidence="ECO:0000250"
FT DISULFID 78..84
FT /evidence="ECO:0000250"
FT DISULFID 155..414
FT /evidence="ECO:0000250"
FT DISULFID 189..227
FT /evidence="ECO:0000250"
FT DISULFID 193..226
FT /evidence="ECO:0000250"
FT DISULFID 247..273
FT /evidence="ECO:0000250"
FT DISULFID 255..260
FT /evidence="ECO:0000250"
FT DISULFID 278..348
FT /evidence="ECO:0000250"
FT DISULFID 485..502
FT /evidence="ECO:0000250"
FT DISULFID 496..512
FT /evidence="ECO:0000250"
SQ SEQUENCE 513 AA; 54073 MW; 9F5C0A8A854F2C12 CRC64;
MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV IDANWRWTHA
TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG VTTSGNSLSI GFVTQSAQKN
VGARLYLMAS DTTYQEFTLL GNEFSFDVDV SQLPCGLNGA LYFVSMDADG GVSKYPTNTA
GAKYGTGYCD SQCPRDLKFI NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE
ALTPHPCTTV GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA EEAEFGGSSF
SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT NETSSTPGAV RGSCSTSSGV
PAQVESQSPN AKVTFSNIKF GPIGSTGNPS GGNPPGGNRG TTTTRRPATT TGSSPGPTQS
HYGQCGGIGY SGPTVCASGT TCQVLNPYYS QCL
