ID GUN1_TRIRE STANDARD; PRT; 459 AA. AC P07981; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 21-MAR-2006, entry version 64. DE Endoglucanase EG-1 precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase) DE (Cellulase). GN Name=egl1; 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=87106822; PubMed=2948877; DOI=10.1016/0378-1119(86)90023-5; RA Penttilae M., Lehtovaara P., Nevalainen H., Bhikhabhai R., RA Knowles J.K.C.; RT "Homology between cellulase genes of Trichoderma reesei: complete RT nucleotide sequence of the endoglucanase I gene."; RL Gene 45:253-263(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=L27; RA van Arsdell J.N., Kwok S., Schweickart V.L., Ladner M.B., RA Gelfand D.H., Innis M.A.; RT "Cloning, characterization, and expression in Saccharomyces cerevisiae RT of endoglucanase I from Trichoderma reesei."; RL Biotechnology (N.Y.) 5:60-64(1987). RN [3] RP ACTIVE SITE GLU-149. 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 [4] RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 23-393. RX MEDLINE=97467423; PubMed=9325098; DOI=10.1006/jmbi.1997.1243; RA Kleywegt G.J., Zou J.-Y., Divne C., Davies G.J., Sinning I., RA Staehlberg J., Reinikainen T., Srisodsuk M., Teeri T.T., Jones T.A.; RT "The crystal structure of the catalytic core domain of endoglucanase I RT from Trichoderma reesei at 3.6-A resolution, and a comparison with RT related enzymes."; RL J. Mol. Biol. 272:383-397(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: Endohydrolysis of 1,4-beta-D-glucosidic CC linkages in cellulose, lichenin and cereal beta-D-glucans. CC -!- SUBCELLULAR LOCATION: Secreted protein. 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 EMBL; M15665; AAA34212.1; -; Genomic_DNA. DR PIR; A25928; A25928. DR PDB; 1EG1; X-ray; A/C=23-393. DR LinkHub; P07981; -. 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; 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 Signal. FT SIGNAL 1 22 FT CHAIN 23 459 Endoglucanase EG-1. FT /FTId=PRO_0000007915. FT DOMAIN 423 459 CBM1. FT REGION 23 397 Catalytic. FT REGION 398 423 Linker. FT ACT_SITE 149 149 FT ACT_SITE 218 218 Nucleophile. FT ACT_SITE 223 223 Proton donor. FT CARBOHYD 78 78 N-linked (GlcNAc...) (Potential). FT CARBOHYD 164 164 N-linked (GlcNAc...) (Potential). FT CARBOHYD 204 204 N-linked (GlcNAc...) (Potential). FT CARBOHYD 208 208 N-linked (GlcNAc...) (Potential). FT CARBOHYD 394 394 N-linked (GlcNAc...) (Potential). FT DISULFID 431 448 By similarity. FT DISULFID 442 458 By similarity. FT STRAND 24 25 FT STRAND 27 29 FT STRAND 35 35 FT STRAND 38 42 FT TURN 43 45 FT STRAND 46 50 FT STRAND 53 56 FT HELIX 58 60 FT STRAND 61 61 FT STRAND 63 64 FT TURN 66 67 FT STRAND 70 73 FT TURN 74 75 FT STRAND 76 77 FT TURN 79 81 FT STRAND 83 85 FT HELIX 86 91 FT STRAND 93 94 FT TURN 99 103 FT STRAND 104 106 FT STRAND 108 115 FT STRAND 117 118 FT STRAND 120 125 FT STRAND 130 134 FT TURN 136 137 FT STRAND 138 140 FT STRAND 143 143 FT TURN 146 147 FT STRAND 148 154 FT TURN 156 157 FT STRAND 158 158 FT TURN 161 162 FT STRAND 163 170 FT TURN 174 177 FT STRAND 180 181 FT HELIX 185 188 FT TURN 189 189 FT TURN 195 196 FT STRAND 199 199 FT STRAND 201 203 FT TURN 204 205 FT STRAND 206 207 FT TURN 209 210 FT STRAND 213 213 FT STRAND 218 224 FT STRAND 226 227 FT STRAND 229 229 FT STRAND 231 234 FT STRAND 236 236 FT STRAND 238 239 FT STRAND 241 241 FT STRAND 243 244 FT STRAND 248 248 FT TURN 250 254 FT TURN 256 257 FT STRAND 258 260 FT TURN 261 262 FT STRAND 263 265 FT TURN 267 268 FT STRAND 269 269 FT STRAND 271 279 FT TURN 280 281 FT STRAND 282 283 FT TURN 284 285 FT STRAND 286 286 FT STRAND 288 297 FT TURN 298 299 FT STRAND 300 301 FT STRAND 305 306 FT TURN 307 308 FT STRAND 310 312 FT STRAND 316 316 FT HELIX 317 321 FT TURN 322 324 FT HELIX 325 333 FT STRAND 335 343 FT TURN 345 349 FT HELIX 350 353 FT STRAND 354 354 FT HELIX 355 357 FT STRAND 359 360 FT TURN 362 365 FT HELIX 367 373 FT TURN 375 376 FT STRAND 378 388 FT TURN 389 391 SQ SEQUENCE 459 AA; 48208 MW; D235A256F808CBB9 CRC64; MAPSVTLPLT TAILAIARLV AAQQPGTSTP EVHPKLTTYK CTKSGGCVAQ DTSVVLDWNY RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCFIEGVDYA ASGVTTSGSS LTMNQYMPSS SGGYSSVSPR LYLLDSDGEY VMLKLNGQEL SFDVDLSALP CGENGSLYLS QMDENGGANQ YNTAGANYGS GYCDAQCPVQ TWRNGTLNTS HQGFCCNEMD ILEGNSRANA LTPHSCTATA CDSAGCGFNP YGSGYKSYYG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYQQNGV DIPSAQPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN WLDSGNAGPC SSTEGNPSNI LANNPNTHVV FSNIRWGDIG STTNSTAPPP PPASSTTFST TRRSSTTSSS PSCTQTHWGQ CGGIGYSGCK TCTSGTTCQY SNDYYSQCL //