ID GUX1_HUMGT Reviewed; 525 AA. AC P15828; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 22-FEB-2023, entry version 114. DE RecName: Full=Exoglucanase 1; DE EC=3.2.1.91; DE AltName: Full=1,4-beta-cellobiohydrolase; DE AltName: Full=Beta-glucancellobiohydrolase; DE AltName: Full=Exocellobiohydrolase I; DE AltName: Full=Exoglucanase I; DE Flags: Precursor; GN Name=CBH-1; OS Humicola grisea var. thermoidea. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Trichocladium; OC Trichocladium griseum. OX NCBI_TaxID=5528; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2308855; DOI=10.1093/nar/18.3.668; RA de Oliviera Alzevedo M., Radford A.; RT "Sequence of cbh-1 gene of Humicola grisea var. thermoidea."; RL Nucleic Acids Res. 18:668-668(1990). 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}. 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; X17258; CAA35159.1; -; Genomic_DNA. DR PIR; S38794; S38794. DR PDB; 4CSI; X-ray; 1.80 A; A/B=20-457. DR PDBsum; 4CSI; -. DR AlphaFoldDB; P15828; -. DR SMR; P15828; -. DR CAZy; CBM1; Carbohydrate-Binding Module Family 1. DR CAZy; GH7; Glycoside Hydrolase Family 7. DR GlyCosmos; P15828; 1 site, No reported glycans. DR BRENDA; 3.2.1.176; 8357. 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; 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 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; KW Polysaccharide degradation; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..525 FT /note="Exoglucanase 1" FT /id="PRO_0000007921" FT DOMAIN 489..525 FT /note="CBM1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597" FT REGION 19..467 FT /note="Catalytic" FT REGION 454..492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 468..489 FT /note="Linker" FT COMPBIAS 465..490 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 231 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 236 FT /note="Proton donor" FT /evidence="ECO:0000250" FT CARBOHYD 289 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 497..514 FT /evidence="ECO:0000250" FT DISULFID 508..524 FT /evidence="ECO:0000250" FT STRAND 31..38 FT /evidence="ECO:0007829|PDB:4CSI" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 42..52 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 59..65 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:4CSI" FT TURN 76..78 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 82..88 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 96..100 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 108..116 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 125..136 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 144..151 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 159..166 FT /evidence="ECO:0007829|PDB:4CSI" FT TURN 170..176 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 224..228 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 231..237 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 242..247 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 249..251 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 255..258 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:4CSI" FT TURN 268..271 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:4CSI" FT TURN 284..288 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 297..300 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 305..313 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 317..328 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 350..360 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 365..368 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 371..380 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 383..391 FT /evidence="ECO:0007829|PDB:4CSI" FT TURN 393..397 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 398..401 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 402..405 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 406..408 FT /evidence="ECO:0007829|PDB:4CSI" FT TURN 412..414 FT /evidence="ECO:0007829|PDB:4CSI" FT HELIX 426..432 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 437..447 FT /evidence="ECO:0007829|PDB:4CSI" FT STRAND 450..452 FT /evidence="ECO:0007829|PDB:4CSI" SQ SEQUENCE 525 AA; 55694 MW; A6684D4CF881E090 CRC64; MRTAKFATLA ALVASAAAQQ ACSLTTERHP SLSWNKCTAG GQCQTVQASI TLDSNWRWTH QVSGSTNCYT GNKWDTSICT DAKSCAQNCC VDGADYTSTY GITTNGDSLS LKFVTKGQHS TNVGSRTYLM DGEDKYQTFE LLGNEFTFDV DVSNIGCGLN GALYFVSMDA DGGLSRYPGN KAGAKYGTGY CDAQCPRDIK FINGEANIEG WTGSTNDPNA GAGRYGTCCS EMDIWEANNM ATAFTPHPCT IIGQSRCEGD SCGGTYSNER YAGVCDPDGC DFNSYRQGNK TFYGKGMTVD TTKKITVVTQ FLKDANGDLG EIKRFYVQDG KIIPNSESTI PGVEGNSITQ DWCDRQKVAF GDIDDFNRKG GMKQMGKALA GPMVLVMSIW DDHASNMLWL DSTFPVDAAG KPGAERGACP TTSGVPAEVE AEAPNSNVVF SNIRFGPIGS TVAGLPGAGN GGNNGGNPPP PTTTTSSAPA TTTTASAGPK AGRWQQCGGI GFTGPTQCEE PYICTKLNDW YSQCL //