GUX1_HYPRU
ID GUX1_HYPRU Reviewed; 514 AA.
AC P19355; O93832;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Exoglucanase 1;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase;
DE AltName: Full=Exocellobiohydrolase;
DE AltName: Full=Exoglucanase I;
DE Flags: Precursor;
GN Name=cbh1;
OS Hypocrea rufa (Trichoderma viride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5547;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2216737; DOI=10.1093/nar/18.18.5559;
RA Cheng C., Tsukagoshi N., Udaka S.;
RT "Nucleotide sequence of the cellobiohydrolase gene from Trichoderma
RT viride.";
RL Nucleic Acids Res. 18:5559-5559(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MC300-1;
RA Watanabe M.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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; X53931; CAA37878.1; -; Genomic_DNA.
DR EMBL; AB021656; BAA36215.1; -; Genomic_DNA.
DR PIR; S11439; S11439.
DR AlphaFoldDB; P19355; -.
DR SMR; P19355; -.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..17
FT CHAIN 18..514
FT /note="Exoglucanase 1"
FT /id="PRO_0000007928"
FT DOMAIN 478..514
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 18..453
FT /note="Catalytic"
FT REGION 401..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..478
FT /note="Linker"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /note="Proton donor"
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 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 486..503
FT /evidence="ECO:0000250"
FT DISULFID 497..513
FT /evidence="ECO:0000250"
FT CONFLICT 173
FT /note="S -> T (in Ref. 1; CAA37878)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="D -> E (in Ref. 1; CAA37878)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="N -> D (in Ref. 1; CAA37878)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="C -> S (in Ref. 1; CAA37878)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="S -> P (in Ref. 1; CAA37878)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="R -> P (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="S -> I (in Ref. 1; CAA37878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 54002 MW; C5B1FB734C9CDAF5 CRC64;
MYQKLALISA FLATARAQSA CTLQAETHPP LTWQKCSSGG TCTQQTGSVV IDANWRWTHA
TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG VTTSADSLSI GFVTQSAQKN
VGARLYLMAS DTTYQEFTLL GNEFSFDVDV SQLPCGLNGA LYFVSMDADG GVSKYPTNTA
GAKYGTGYCD SQCPRDLKFI NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE
ALTPHPCTTV GQEICDGDSC GGTYSGDRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGDYSG NSLDDDYCAA EEAEFGGSSF
SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT NETSSTPGAV RGSCSTSSGV
PAQLESNSPN AKVVYSNIKF GPIGSTGNSS GGNPPGGNPP GTTTTRRPAT STGSSPGPTQ
THYGQCGGIG YSGPTVCASG STCQVLNPYY SQCL
