ID GUX2_TRIRE STANDARD; PRT; 471 AA. AC P07987; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 07-FEB-2006, entry version 68. DE Exoglucanase 2 precursor (EC 3.2.1.91) (Exoglucanase II) DE (Exocellobiohydrolase II) (CBHII) (1,4-beta-cellobiohydrolase). GN Name=cbh2; 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 [GENOMIC DNA]. RC STRAIN=VTT-D-80133; RX MEDLINE=87248061; PubMed=3596237; RA Teeri T.T., Lehtovaara P., Kauppinen S., Salovuori I., Knowles J.; RT "Homologous domains in Trichoderma reesei cellulolytic enzymes: gene RT sequence and expression of cellobiohydrolase II."; RL Gene 51:43-52(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=QM9414 / Rut C-30; RA Chen C.M., Gritzali M., Stafford D.W.; RT "Nucleotide sequence and deduced primary structure of RT cellobiohydrolase II from Trichoderma reesei."; RL Biotechnology (N.Y.) 5:274-278(1987). RN [3] RP PROTEIN SEQUENCE OF 25-44. RA Faegerstam L.G., Pettersson L.G.; RT "The 1,4-beta-glucan cellobiohydrolases of Trichoderma reesei QM RT 9414."; RL FEBS Lett. 119:97-100(1980). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=90333255; PubMed=2377893; RA Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K.C., Jones T.A.; RT "Three-dimensional structure of cellobiohydrolase II from Trichoderma RT reesei."; RL Science 249:380-386(1990). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=97029636; PubMed=8875646; RA Koivula A., Reinikainen T., Ruohonen L., Valkeajaervi A., RA Claeyssens M., Teleman O., Kleywegt G.J., Szardenings M., Rouvinen J., RA Jones T.A., Teeri T.T.; RT "The active site of Trichoderma reesei cellobiohydrolase II: the role RT of tyrosine 169."; RL Protein Eng. 9:691-699(1996). 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 6 (cellulase B) 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 EMBL; M16190; AAA34210.1; -; Genomic_DNA. DR EMBL; M55080; AAA72922.1; -; Genomic_DNA. DR PIR; A26160; A26160. DR PDB; 1CB2; X-ray; A/B=107-471. DR PDB; 1HGW; X-ray; A/B=107-471. DR PDB; 1HGY; X-ray; A/B=107-471. DR PDB; 1QJW; X-ray; A/B=107-471. DR PDB; 1QK0; X-ray; A/B=109-471. DR PDB; 1QK2; X-ray; A/B=109-471. DR PDB; 3CBH; X-ray; @=107-471. DR LinkHub; P07987; -. DR InterPro; IPR000254; CBD_fun. DR InterPro; IPR001524; Glyco_hydro_6. DR Pfam; PF00734; CBM_1; 1. DR Pfam; PF01341; Glyco_hydro_6; 1. DR PRINTS; PR00733; GLHYDRLASE6. DR ProDom; PD001821; CBD_fungal; 1. DR ProDom; PD003733; Glyco_hydro_6; 1. DR SMART; SM00236; fCBD; 1. DR PROSITE; PS00562; CBM1_1; 1. DR PROSITE; PS51164; CBM1_2; 1. DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1. DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1. KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; KW Polysaccharide degradation; Signal. FT SIGNAL 1 24 FT CHAIN 25 471 Exoglucanase 2. FT /FTId=PRO_0000007911. FT DOMAIN 26 62 CBM1. FT REGION 66 106 Linker. FT REGION 107 471 Catalytic. FT ACT_SITE 199 199 FT ACT_SITE 245 245 Proton donor. FT ACT_SITE 425 425 Nucleophile. FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 111 111 O-linked (Man...). FT CARBOHYD 121 121 O-linked (Man...). FT CARBOHYD 130 130 O-linked (Man...). FT CARBOHYD 133 133 O-linked (Man...). FT CARBOHYD 134 134 O-linked (Man...). FT CARBOHYD 139 139 O-linked (Man...). FT CARBOHYD 313 313 N-linked (GlcNAc...). FT CARBOHYD 334 334 N-linked (GlcNAc...). FT DISULFID 34 51 By similarity. FT DISULFID 45 61 By similarity. FT DISULFID 200 259 FT DISULFID 392 439 FT MUTAGEN 199 199 D->A: 20% of wild-type activity. FT MUTAGEN 245 245 D->A: No measurable activity. FT CONFLICT 359 359 P -> R (in Ref. 2). FT CONFLICT 449 449 P -> A (in Ref. 2). FT STRAND 113 114 FT TURN 116 119 FT STRAND 120 122 FT HELIX 126 135 FT TURN 136 136 FT HELIX 137 139 FT HELIX 142 151 FT TURN 152 153 FT STRAND 154 154 FT STRAND 158 160 FT STRAND 162 162 FT HELIX 163 181 FT TURN 182 183 FT STRAND 186 192 FT TURN 196 197 FT STRAND 199 199 FT TURN 200 201 FT STRAND 203 203 FT TURN 204 205 FT STRAND 208 208 FT HELIX 211 213 FT TURN 214 214 FT HELIX 215 232 FT TURN 233 235 FT STRAND 236 236 FT STRAND 238 242 FT STRAND 244 246 FT HELIX 247 252 FT TURN 254 255 FT STRAND 256 256 FT HELIX 257 260 FT TURN 261 262 FT HELIX 263 276 FT TURN 277 277 FT TURN 280 281 FT STRAND 282 287 FT TURN 291 293 FT STRAND 294 294 FT STRAND 296 296 FT HELIX 297 313 FT TURN 314 315 FT TURN 318 319 FT STRAND 320 326 FT TURN 327 328 FT STRAND 329 329 FT STRAND 333 334 FT STRAND 336 337 FT HELIX 340 342 FT TURN 343 344 FT STRAND 346 346 FT STRAND 349 349 FT HELIX 350 363 FT TURN 364 365 FT STRAND 368 368 FT STRAND 370 374 FT TURN 376 377 FT STRAND 379 382 FT STRAND 384 384 FT STRAND 386 387 FT TURN 388 389 FT STRAND 392 396 FT STRAND 401 401 FT STRAND 404 405 FT TURN 410 411 FT STRAND 412 416 FT STRAND 419 419 FT TURN 421 422 FT STRAND 423 423 FT STRAND 425 425 FT TURN 430 431 FT STRAND 432 432 FT TURN 433 434 FT HELIX 437 440 FT STRAND 441 441 FT TURN 442 443 FT STRAND 444 444 FT STRAND 446 447 FT STRAND 450 450 FT TURN 451 452 FT STRAND 453 454 FT HELIX 456 464 FT TURN 465 465 FT STRAND 467 468 SQ SEQUENCE 471 AA; 49653 MW; C4711BC335B1BD88 CRC64; MIVGILTTLA TLATLAASVP LEERQACSSV WGQCGGQNWS GPTCCASGST CVYSNDYYSQ CLPGAASSSS STRAASTTSR VSPTTSRSSS ATPPPGSTTT RVPPVGSGTA TYSGNPFVGV TPWANAYYAS EVSSLAIPSL TGAMATAAAA VAKVPSFMWL DTLDKTPLME QTLADIRTAN KNGGNYAGQF VVYDLPDRDC AALASNGEYS IADGGVAKYK NYIDTIRQIV VEYSDIRTLL VIEPDSLANL VTNLGTPKCA NAQSAYLECI NYAVTQLNLP NVAMYLDAGH AGWLGWPANQ DPAAQLFANV YKNASSPRAL RGLATNVANY NGWNITSPPS YTQGNAVYNE KLYIHAIGPL LANHGWSNAF FITDQGRSGK QPTGQQQWGD WCNVIGTGFG IRPSANTGDS LLDSFVWVKP GGECDGTSDS SAPRFDSHCA LPDALQPAPQ AGAWFQAYFV QLLTNANPSF L //