ID GUX1_TRIRE STANDARD; PRT; 513 AA. AC P62694; P00725; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 21-MAR-2006, entry version 21. DE Exoglucanase 1 precursor (EC 3.2.1.91) (Exoglucanase I) DE (Exocellobiohydrolase I) (CBHI) (1,4-beta-cellobiohydrolase). GN Name=cbh1; OS Trichoderma reesei (Hypocrea jecorina). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea. OX NCBI_TaxID=51453; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=L27; RA Shoemaker S., Schweickart V., Ladner M., Gelfand D., Kwok S., RA Myambo K., Innis M.; RT "Molecular cloning of exo-cellobiohydrolase I derived from Trichoderma RT reesei strain L27."; RL Biotechnology (N.Y.) 1:691-696(1983). RN [2] RP ACTIVE SITE. RA Tomme P., Clayssens M.; RT "Identification of a functionally important carboxyl group in RT cellobiohydrolase I from Trichoderma reesei."; RL FEBS Lett. 243:239-243(1989). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 18-452. RX MEDLINE=94310436; PubMed=8036495; RA Divne C., Staahlberg J., Reinikainen T., Ruohonen L., Pettersson G., RA Knowles J.K.C., Teeri T.T., Jones T.A.; RT "The three-dimensional crystal structure of the catalytic core of RT cellobiohydrolase I from Trichoderma reesei."; RL Science 265:524-528(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-452. RC STRAIN=QM9414 / Rut C-30; RX MEDLINE=98128795; PubMed=9466911; DOI=10.1006/jmbi.1997.1437; RA Divne C., Staahlberg J., Teeri T.T., Jones T.A.; RT "High-resolution crystal structures reveal how a cellulose chain is RT bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma RT reesei."; RL J. Mol. Biol. 275:309-325(1998). RN [5] RP STRUCTURE BY NMR OF 478-513. RX MEDLINE=90057416; PubMed=2554967; RA Kraulis P.J., Clore G.M., Nilges M., Jones T.A., Pettersson G., RA Knowles J., Gronenborn A.M.; RT "Determination of the three-dimensional solution structure of the RT C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A RT study using nuclear magnetic resonance and hybrid distance geometry- RT dynamical simulated annealing."; RL Biochemistry 28:7241-7257(1989). RN [6] RP STRUCTURE BY NMR OF 478-513. RX MEDLINE=97194052; PubMed=9041630; RA Mattinen M.L., Kontteli M., Kerovuo J., Linder M., Annila A., RA Lindeberg G., Reinikainen T., Drakenberg T.; RT "Three-dimensional structures of three engineered cellulose-binding RT domains of cellobiohydrolase I from Trichoderma reesei."; RL Protein Sci. 6:294-303(1997). 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 -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- MISCELLANEOUS: T.reesei produces two different CC exocellobiohydrolases. They are unique in that they can hydrolyze CC crystalline cellulose in the absence of endoglucanases. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) CC family. CC -!- SIMILARITY: Contains 1 CBM1 (fungal-type carbohydrate-binding) CC 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 PIR; A00902; EUTQI. DR PDB; 1AZ6; NMR; @=478-513. DR PDB; 1AZH; NMR; @=478-513. DR PDB; 1AZJ; NMR; @=478-513. DR PDB; 1AZK; NMR; @=478-513. DR PDB; 1CBH; NMR; @=478-513. DR PDB; 1CEL; X-ray; A/B=18-451. DR PDB; 1DY4; X-ray; A=18-451. DR PDB; 1EGN; X-ray; A=18-451. DR PDB; 1Q2B; X-ray; A=18-451. DR PDB; 1Q2E; X-ray; A/B=18-451. DR PDB; 2CBH; NMR; @=478-513. DR PDB; 2CEL; X-ray; A/B=18-451. DR PDB; 3CEL; X-ray; @=18-451. DR PDB; 4CEL; X-ray; A/B=18-451. DR PDB; 5CEL; X-ray; @=18-451. DR PDB; 6CEL; X-ray; @=18-451. DR PDB; 7CEL; X-ray; @=18-451. DR PDB; 8CEL; Model; @=18-451. DR LinkHub; P62694; -. DR InterPro; IPR000254; CBD_fun. DR InterPro; IPR008985; ConA_like_lec_gl. DR InterPro; IPR001722; Glyco_hydro_7. DR Pfam; PF00734; CBM_1; 1. DR Pfam; PF00840; Glyco_hydro_7; 1. DR PRINTS; PR00734; GLHYDRLASE7. DR ProDom; PD001821; CBD_fungal; 1. DR ProDom; PD186135; Glyco_hydro_7; 1. DR SMART; SM00236; fCBD; 1. DR PROSITE; PS00562; CBM1_1; 1. DR PROSITE; PS51164; CBM1_2; 1. KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; KW Pyrrolidone carboxylic acid; Signal. FT SIGNAL 1 17 FT CHAIN 18 513 Exoglucanase 1. FT /FTId=PRO_0000007927. FT DOMAIN 477 513 CBM1. FT REGION 18 453 Catalytic. FT REGION 454 477 Linker. FT ACT_SITE 143 143 Probable. FT ACT_SITE 229 229 Nucleophile. FT ACT_SITE 234 234 Proton donor. FT MOD_RES 18 18 Pyrrolidone carboxylic acid. FT CARBOHYD 62 62 N-linked (GlcNAc...) (Potential). FT CARBOHYD 81 81 N-linked (GlcNAc...) (Potential). FT CARBOHYD 287 287 N-linked (GlcNAc...) (Potential). FT CARBOHYD 401 401 N-linked (GlcNAc...) (Potential). FT DISULFID 21 89 FT DISULFID 36 42 FT DISULFID 67 88 FT DISULFID 78 84 FT DISULFID 155 414 FT DISULFID 189 227 FT DISULFID 193 226 FT DISULFID 247 273 FT DISULFID 255 260 FT DISULFID 278 348 FT DISULFID 485 502 FT DISULFID 496 512 FT STRAND 19 20 FT STRAND 23 24 FT STRAND 30 36 FT TURN 38 39 FT STRAND 40 40 FT STRAND 42 51 FT HELIX 53 55 FT STRAND 56 56 FT STRAND 58 60 FT TURN 61 62 FT STRAND 63 64 FT STRAND 66 69 FT TURN 70 71 FT STRAND 72 73 FT TURN 75 77 FT STRAND 79 80 FT HELIX 81 87 FT STRAND 88 90 FT TURN 95 99 FT STRAND 101 104 FT TURN 105 106 FT STRAND 107 121 FT STRAND 123 130 FT TURN 131 132 FT STRAND 133 134 FT STRAND 136 137 FT TURN 140 141 FT STRAND 142 149 FT TURN 151 152 FT TURN 155 156 FT STRAND 157 164 FT TURN 168 174 FT TURN 176 177 FT STRAND 180 180 FT HELIX 182 184 FT TURN 185 185 FT STRAND 190 190 FT TURN 191 192 FT STRAND 195 195 FT STRAND 198 200 FT TURN 201 202 FT STRAND 203 204 FT TURN 207 208 FT STRAND 210 211 FT STRAND 213 214 FT TURN 216 217 FT STRAND 219 220 FT STRAND 222 226 FT STRAND 229 235 FT STRAND 237 238 FT STRAND 240 245 FT STRAND 247 249 FT STRAND 251 251 FT STRAND 253 256 FT HELIX 257 260 FT STRAND 262 262 FT TURN 263 264 FT STRAND 265 266 FT TURN 268 269 FT STRAND 270 273 FT STRAND 275 276 FT STRAND 280 280 FT TURN 282 286 FT TURN 288 289 FT STRAND 290 294 FT TURN 295 296 FT STRAND 297 300 FT TURN 301 302 FT STRAND 303 303 FT STRAND 305 311 FT TURN 313 314 FT STRAND 315 315 FT STRAND 317 323 FT TURN 324 325 FT STRAND 326 330 FT STRAND 333 335 FT TURN 336 337 FT STRAND 338 343 FT HELIX 345 355 FT HELIX 359 362 FT TURN 363 364 FT HELIX 365 373 FT TURN 374 374 FT STRAND 375 375 FT STRAND 377 385 FT TURN 387 391 FT HELIX 392 395 FT STRAND 396 399 FT TURN 400 401 FT TURN 404 405 FT STRAND 406 406 FT TURN 407 408 FT STRAND 410 410 FT STRAND 413 414 FT TURN 416 417 FT HELIX 421 427 FT TURN 429 430 FT STRAND 432 442 FT TURN 443 444 FT TURN 446 447 FT STRAND 448 448 FT STRAND 482 483 FT STRAND 485 485 FT TURN 488 489 FT STRAND 491 492 FT STRAND 498 500 FT STRAND 502 506 FT TURN 507 508 FT STRAND 509 512 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 //