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 13-SEP-2023, entry version 76. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P62695; 4 sites, No reported glycans. DR BioCyc; MetaCyc:MONOMER-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; Glycoside hydrolase, family 7, domain; 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; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1. DR PANTHER; PTHR33753:SF2; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 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; SSF57180; Cellulose-binding domain; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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 //