ID GUX_CELFI STANDARD; PRT; 484 AA. AC P07986; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 21-MAR-2006, entry version 62. DE Exoglucanase/xylanase precursor [Includes: Exoglucanase (EC 3.2.1.91) DE (Exocellobiohydrolase) (1,4-beta-cellobiohydrolase) DE (Beta-1,4-glycanase CEX); Endo-1,4-beta-xylanase B (EC 3.2.1.8) DE (Xylanase B)]. GN Name=cex; Synonyms=xynB; OS Cellulomonas fimi. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Cellulomonadaceae; Cellulomonas. OX NCBI_TaxID=1708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87055250; 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 RT fimi."; RL Gene 44:325-330(1986). RN [2] RP ACTIVE SITE GLU-274. RX MEDLINE=91340691; PubMed=1678739; 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 RT 'retaining' exoglucanase from Cellulomonas fimi."; RL J. Biol. Chem. 266:15621-15625(1991). RN [3] RP DISULFIDE BONDS. RX MEDLINE=92104156; PubMed=1761039; 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 RT beta-1,4-glycanases."; RL Eur. J. Biochem. 202:367-377(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=95001978; PubMed=7918478; 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 RT cex from Cellulomonas fimi."; RL Biochemistry 33:12546-12552(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=96163434; PubMed=8564541; RA White A., Tull D., Johns K., Withers S.G., Rose D.R.; RT "Crystallographic observation of a covalent catalytic intermediate in RT a beta-glycosidase."; RL Nat. Struct. Biol. 3:149-154(1996). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-353. RX MEDLINE=98206890; 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 RT cex 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; RX MEDLINE=98400502; PubMed=9731776; RA Notenboom V., Birsan C., Nitz M., Rose D.R., Warren R.A., RA Withers S.G.; RT "Insights into transition state stabilization of the RT beta-1,4-glycosidase Cex by covalent intermediate accumulation in RT active site mutants."; RL Nat. Struct. Biol. 5:812-818(1998). RN [8] RP STRUCTURE BY NMR OF 377-484. RX MEDLINE=95284032; PubMed=7766609; 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 RT fimi by nuclear magnetic resonance spectroscopy."; RL Biochemistry 34:6993-7009(1995). RN [9] RP MUTAGENESIS OF GLU-168. RX MEDLINE=94250681; PubMed=7910761; RA Macleod A.M., Lindhorst T., Withers S.G., Warren R.A.J.; RT "The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas RT fimi is glutamic acid 127: evidence from detailed kinetic studies of RT mutants."; RL Biochemistry 33:6371-6376(1994). CC -!- FUNCTION: Hydrolyzes both cellulose and xylan. Has also weak CC endoglucanase activity. CC -!- FUNCTION: The biological conversion of cellulose to glucose CC generally requires three types of hydrolytic enzymes: (1) CC Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) CC Exocellobiohydrolases that cut the dissaccharide cellobiose from CC the nonreducing end of the cellulose polymer chain; (3) CC Beta-1,4-glucosidases which hydrolyze the cellobiose and other CC short cello-oligosaccharides to glucose. CC -!- CATALYTIC ACTIVITY: Hydrolysis of 1,4-beta-D-glucosidic linkages CC in cellulose and cellotetraose, releasing cellobiose from the non- CC reducing ends of the chains. CC -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-xylosidic CC linkages in xylans. 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) CC family. CC -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M15824; AAA56791.1; -; Genomic_DNA. DR PIR; A24994; A24994. DR PDB; 1EXG; NMR; @=377-484. DR PDB; 1EXH; NMR; @=377-484. DR PDB; 1EXP; X-ray; @=42-353. DR PDB; 1J01; X-ray; A=42-353. DR PDB; 2EXO; X-ray; @=42-353. DR PDB; 2HIS; X-ray; @=42-353. DR PDB; 2XYL; X-ray; @=42-353. DR LinkHub; P07986; -. DR InterPro; IPR008965; Carb_bd. DR InterPro; IPR001919; CBD_bac. DR InterPro; IPR012291; CBD_carb_bd. DR InterPro; IPR001000; Glyco_hydro_10. 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 PROSITE; PS51173; CBM2; 1. DR PROSITE; PS00561; CBM2_A; 1. DR PROSITE; PS00591; GLYCOSYL_HYDROL_F10; 1. KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Glycosidase; Hydrolase; Multifunctional enzyme; KW Polysaccharide degradation; Repeat; Signal; Xylan degradation. FT SIGNAL 1 41 FT CHAIN 42 484 Exoglucanase/xylanase. FT /FTId=PRO_0000007960. FT DOMAIN 375 484 CBM2. FT REGION 42 356 Catalytic. FT REGION 357 376 Linker ("hinge") (Pro-Thr box). FT ACT_SITE 168 168 Proton donor. FT ACT_SITE 274 274 Nucleophile. FT DISULFID 208 240 FT DISULFID 302 308 FT DISULFID 382 481 FT MUTAGEN 168 168 E->A,D,G: Reduced activity. FT STRAND 44 44 FT HELIX 45 51 FT TURN 52 53 FT STRAND 55 60 FT HELIX 62 66 FT STRAND 67 67 FT HELIX 68 77 FT STRAND 79 85 FT TURN 86 87 FT STRAND 88 88 FT HELIX 89 92 FT STRAND 94 95 FT TURN 96 97 FT STRAND 98 98 FT HELIX 102 114 FT TURN 115 115 FT STRAND 117 120 FT STRAND 123 124 FT STRAND 126 128 FT HELIX 131 134 FT TURN 135 135 FT HELIX 138 156 FT TURN 157 159 FT STRAND 161 167 FT STRAND 170 170 FT TURN 172 173 FT STRAND 174 176 FT STRAND 178 179 FT HELIX 181 201 FT STRAND 203 213 FT STRAND 215 218 FT HELIX 219 233 FT TURN 234 235 FT STRAND 240 243 FT STRAND 246 248 FT TURN 249 250 FT TURN 254 255 FT HELIX 256 264 FT TURN 265 267 FT STRAND 269 282 FT HELIX 285 303 FT TURN 304 304 FT STRAND 305 305 FT TURN 306 307 FT STRAND 308 314 FT STRAND 316 317 FT HELIX 318 320 FT STRAND 322 322 FT HELIX 323 326 FT STRAND 327 327 FT TURN 328 329 FT STRAND 330 331 FT STRAND 334 336 FT TURN 338 339 FT STRAND 340 340 FT STRAND 342 342 FT HELIX 344 352 FT STRAND 377 377 FT STRAND 382 385 FT STRAND 388 403 FT STRAND 405 407 FT STRAND 409 417 FT STRAND 419 421 FT STRAND 423 435 FT TURN 436 437 FT STRAND 438 443 FT STRAND 445 445 FT HELIX 446 448 FT STRAND 449 450 FT STRAND 452 463 FT STRAND 465 467 FT STRAND 472 472 FT STRAND 474 476 FT TURN 477 478 FT STRAND 479 483 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 //