ID GUX_CELFI Reviewed; 484 AA. AC P07986; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 28-JUN-2023, entry version 145. DE RecName: Full=Exoglucanase/xylanase; DE Includes: DE RecName: Full=Exoglucanase; DE EC=3.2.1.91; DE AltName: Full=1,4-beta-cellobiohydrolase; DE AltName: Full=Beta-1,4-glycanase CEX; DE AltName: Full=Exocellobiohydrolase; DE Includes: DE RecName: Full=Endo-1,4-beta-xylanase B; DE Short=Xylanase B; DE EC=3.2.1.8; DE Flags: Precursor; GN Name=cex; Synonyms=xynB; OS Cellulomonas fimi. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=1708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3096818; DOI=10.1016/0378-1119(86)90197-6; RA O'Neill G., Goh S.H., Warren R.A.J., Kilburn D.G., Miller R.C. Jr.; RT "Structure of the gene encoding the exoglucanase of Cellulomonas fimi."; RL Gene 44:325-330(1986). RN [2] RP ACTIVE SITE GLU-274. RX PubMed=1678739; DOI=10.1016/s0021-9258(18)98451-6; RA Tull D., Withers S.G., Gilkes N.R., Kilburn D.G., Warren R.A.J., RA Aebersold R.; RT "Glutamic acid 274 is the nucleophile in the active site of a 'retaining' RT exoglucanase from Cellulomonas fimi."; RL J. Biol. Chem. 266:15621-15625(1991). RN [3] RP DISULFIDE BONDS. RX PubMed=1761039; DOI=10.1111/j.1432-1033.1991.tb16384.x; RA Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A., RA Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.; RT "Structural and functional relationships in two families of beta-1,4- RT glycanases."; RL Eur. J. Biochem. 202:367-377(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=7918478; DOI=10.1021/bi00208a003; RA White A., Withers S.G., Gilkes N.R., Rose D.R.; RT "Crystal structure of the catalytic domain of the beta-1,4-glycanase cex RT from Cellulomonas fimi."; RL Biochemistry 33:12546-12552(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=8564541; DOI=10.1038/nsb0296-149; RA White A., Tull D., Johns K., Withers S.G., Rose D.R.; RT "Crystallographic observation of a covalent catalytic intermediate in a RT beta-glycosidase."; RL Nat. Struct. Biol. 3:149-154(1996). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-353. RX PubMed=9537990; DOI=10.1021/bi9729211; RA Notenboom V., Birsan C., Warren R.A.J., Withers S.G., Rose D.R.; RT "Exploring the cellulose/xylan specificity of the beta-1,4-glycanase cex RT from Cellulomonas fimi through crystallography and mutation."; RL Biochemistry 37:4751-4758(1998). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 42-353. RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / RC NCTC 7547; RX PubMed=9731776; DOI=10.1038/1852; RA Notenboom V., Birsan C., Nitz M., Rose D.R., Warren R.A., Withers S.G.; RT "Insights into transition state stabilization of the beta-1,4-glycosidase RT Cex by covalent intermediate accumulation in active site mutants."; RL Nat. Struct. Biol. 5:812-818(1998). RN [8] RP STRUCTURE BY NMR OF 377-484. RX PubMed=7766609; DOI=10.1021/bi00021a011; RA Xu G.-Y., Ong E., Gilkes N.R., Kilburn D.G., Muhandiram D.R., RA Harris-Brandts M., Carver J.P., Kay L.E., Harvey T.S.; RT "Solution structure of a cellulose-binding domain from Cellulomonas fimi by RT nuclear magnetic resonance spectroscopy."; RL Biochemistry 34:6993-7009(1995). RN [9] RP MUTAGENESIS OF GLU-168. RX PubMed=7910761; DOI=10.1021/bi00186a042; RA Macleod A.M., Lindhorst T., Withers S.G., Warren R.A.J.; RT "The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi RT is glutamic acid 127: evidence from detailed kinetic studies of mutants."; RL Biochemistry 33:6371-6376(1994). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 43-354. RX PubMed=10995222; DOI=10.1021/bi0010625; RA Notenboom V., Williams S.J., Hoos R., Withers S.G., Rose D.R.; RT "Detailed structural analysis of glycosidase/inhibitor interactions: RT complexes of Cex from Cellulomonas fimi with xylobiose-derived aza- RT sugars."; RL Biochemistry 39:11553-11563(2000). CC -!- FUNCTION: Hydrolyzes both cellulose and xylan. Has also weak CC endoglucanase activity. 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 -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; CC -!- MISCELLANEOUS: The linker region (also termed 'hinge') may be a CC potential site for proteolysis. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) 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; M15824; AAA56791.1; -; Genomic_DNA. DR PIR; A24994; A24994. DR PDB; 1EXG; NMR; -; A=377-484. DR PDB; 1EXH; NMR; -; A=377-484. DR PDB; 1EXP; X-ray; 1.80 A; A=42-353. DR PDB; 1FH7; X-ray; 1.82 A; A=42-353. DR PDB; 1FH8; X-ray; 1.95 A; A=42-353. DR PDB; 1FH9; X-ray; 1.72 A; A=42-353. DR PDB; 1FHD; X-ray; 1.90 A; A=42-353. DR PDB; 1J01; X-ray; 2.00 A; A=42-353. DR PDB; 2EXO; X-ray; 1.80 A; A=42-353. DR PDB; 2HIS; X-ray; 1.84 A; A=42-353. DR PDB; 2XYL; X-ray; 1.90 A; A=42-353. DR PDB; 3CUF; X-ray; 1.67 A; A=42-356. DR PDB; 3CUG; X-ray; 1.68 A; A=42-356. DR PDB; 3CUH; X-ray; 1.89 A; A=42-356. DR PDB; 3CUI; X-ray; 1.50 A; A=42-356. DR PDB; 3CUJ; X-ray; 1.70 A; A=42-356. DR PDB; 6QFS; X-ray; 2.20 A; A/B/C/D/E/F/G/H=380-484. DR PDBsum; 1EXG; -. DR PDBsum; 1EXH; -. DR PDBsum; 1EXP; -. DR PDBsum; 1FH7; -. DR PDBsum; 1FH8; -. DR PDBsum; 1FH9; -. DR PDBsum; 1FHD; -. DR PDBsum; 1J01; -. DR PDBsum; 2EXO; -. DR PDBsum; 2HIS; -. DR PDBsum; 2XYL; -. DR PDBsum; 3CUF; -. DR PDBsum; 3CUG; -. DR PDBsum; 3CUH; -. DR PDBsum; 3CUI; -. DR PDBsum; 3CUJ; -. DR PDBsum; 6QFS; -. DR AlphaFoldDB; P07986; -. DR BMRB; P07986; -. DR SMR; P07986; -. DR DrugBank; DB04282; 2-deoxy-2-fluoro-Alpha-D-glucose. DR DrugBank; DB03717; 3-Hydroxy-4-(3,4,5-trihydroxy-tetrahydro-pyran-2-yloxy)-piperidin-2-one. DR DrugBank; DB03389; alpha-D-Xylopyranose. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB02374; Xylose-Derived Imidazole. DR DrugBank; DB01921; Xylose-derived lactam oxime. DR CAZy; CBM2; Carbohydrate-Binding Module Family 2. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR BRENDA; 3.2.1.91; 1233. DR EvolutionaryTrace; P07986; -. DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC. DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW. DR DisProt; DP01933; -. DR Gene3D; 2.60.40.290; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001919; CBD2. DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR012291; CBM2_carb-bd_dom_sf. DR InterPro; IPR018366; CBM2_CS. DR InterPro; IPR044846; GH10. DR InterPro; IPR031158; GH10_AS. DR InterPro; IPR001000; GH10_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1. DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1. DR Pfam; PF00553; CBM_2; 1. DR Pfam; PF00331; Glyco_hydro_10; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00637; CBD_II; 1. DR SMART; SM00633; Glyco_10; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1. DR PROSITE; PS51173; CBM2; 1. DR PROSITE; PS00561; CBM2_A; 1. DR PROSITE; PS00591; GH10_1; 1. DR PROSITE; PS51760; GH10_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Disulfide bond; Glycosidase; Hydrolase; Multifunctional enzyme; KW Polysaccharide degradation; Repeat; Signal; Xylan degradation. FT SIGNAL 1..41 FT CHAIN 42..484 FT /note="Exoglucanase/xylanase" FT /id="PRO_0000007960" FT DOMAIN 42..352 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT DOMAIN 375..484 FT /note="CBM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135" FT REGION 357..377 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..376 FT /note="Linker ('hinge') (Pro-Thr box)" FT COMPBIAS 359..375 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 168 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:7918478" FT ACT_SITE 274 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061, FT ECO:0000269|PubMed:1678739" FT DISULFID 208..240 FT /evidence="ECO:0000269|PubMed:1761039" FT DISULFID 302..308 FT /evidence="ECO:0000269|PubMed:1761039" FT DISULFID 382..481 FT /evidence="ECO:0000269|PubMed:1761039" FT MUTAGEN 168 FT /note="E->A,D,G: Reduced activity." FT /evidence="ECO:0000269|PubMed:7910761" FT HELIX 45..52 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 62..66 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 68..77 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 79..85 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 89..92 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 102..114 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 117..128 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 138..156 FT /evidence="ECO:0007829|PDB:3CUI" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 162..167 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 181..186 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:1EXP" FT HELIX 190..201 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 203..213 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 219..234 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 256..264 FT /evidence="ECO:0007829|PDB:3CUI" FT TURN 265..267 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 269..282 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 285..303 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 308..314 FT /evidence="ECO:0007829|PDB:3CUI" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 323..326 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:3CUI" FT HELIX 344..353 FT /evidence="ECO:0007829|PDB:3CUI" FT STRAND 383..390 FT /evidence="ECO:0007829|PDB:6QFS" FT STRAND 392..402 FT /evidence="ECO:0007829|PDB:6QFS" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:6QFS" FT STRAND 409..411 FT /evidence="ECO:0007829|PDB:6QFS" FT STRAND 413..417 FT /evidence="ECO:0007829|PDB:6QFS" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:1EXG" FT STRAND 423..435 FT /evidence="ECO:0007829|PDB:6QFS" FT STRAND 438..443 FT /evidence="ECO:0007829|PDB:6QFS" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:1EXG" FT STRAND 455..463 FT /evidence="ECO:0007829|PDB:6QFS" FT STRAND 465..467 FT /evidence="ECO:0007829|PDB:1EXG" FT STRAND 474..476 FT /evidence="ECO:0007829|PDB:6QFS" FT STRAND 479..483 FT /evidence="ECO:0007829|PDB:6QFS" SQ SEQUENCE 484 AA; 51291 MW; 6EE5486BC0E9B02F CRC64; MPRTTPAPGH PARGARTALR TTRRRAATLV VGATVVLPAQ AATTLKEAAD GAGRDFGFAL DPNRLSEAQY KAIADSEFNL VVAENAMKWD ATEPSQNSFS FGAGDRVASY AADTGKELYG HTLVWHSQLP DWAKNLNGSA FESAMVNHVT KVADHFEGKV ASWDVVNEAF ADGDGPPQDS AFQQKLGNGY IETAFRAARA ADPTAKLCIN DYNVEGINAK SNSLYDLVKD FKARGVPLDC VGFQSHLIVG QVPGDFRQNL QRFADLGVDV RITELDIRMR TPSDATKLAT QAADYKKVVQ ACMQVTRCQG VTVWGITDKY SWVPDVFPGE GAALVWDASY AKKPAYAAVM EAFGASPTPT PTTPTPTPTT PTPTPTSGPA GCQVLWGVNQ WNTGFTANVT VKNTSSAPVD GWTLTFSFPS GQQVTQAWSS TVTQSGSAVT VRNAPWNGSI PAGGTAQFGF NGSHTGTNAA PTAFSLNGTP CTVG //