ID GUN5_THEFU STANDARD; PRT; 466 AA. AC Q01786; DT 01-JUL-1993 (Rel. 26, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Endoglucanase E-5 precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase E-4) DE (Cellulase E-5) (Cellulase E5). GN Name=celE; OS Thermomonospora fusca. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptosporangineae; Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=2021; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=YX; RX MEDLINE=91258320; PubMed=1904434; RA Lao G., Ghangas G.S., Jung E.D., Wilson D.B.; RT "DNA sequences of three beta-1,4-endoglucanase genes from RT Thermomonospora fusca."; RL J. Bacteriol. 173:3397-3407(1991). RN [2] RP SEQUENCE REVISION. RA Lao G., Ghangas G.S., Jung E.D., Wilson D.B.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 137-142 AND 157-166. RC STRAIN=YX; RA Irwin D.C., Spezio M., Walker L.P., Wilson D.B.; RT "Activity studies of eight purified cellulases: specificity, RT synergism, and binding domain effects."; RL Biotechnol. Bioeng. 42:1002-1013(1993). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic CC linkages in cellulose, lichenin and cereal beta-D-glucans. CC -!- PATHWAY: Cellulose degradation. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) CC family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; L01577; AAC09379.1; -. DR PIR; C42360; C42360. DR HSSP; Q59232; 1LF1. DR InterPro; IPR001919; Bac_celose-bind. DR InterPro; IPR008965; Cellul_bind. DR InterPro; IPR001547; Glyco_hydro_5. DR Pfam; PF00553; CBM_2; 1. DR Pfam; PF00150; Cellulase; 1. DR SMART; SM00637; CBD_II; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. KW Cellulose degradation; Direct protein sequencing; Glycosidase; KW Hydrolase; Signal. FT SIGNAL 1 36 FT CHAIN 37 466 Endoglucanase E-5. FT ACT_SITE 299 299 Proton donor (By similarity). FT ACT_SITE 391 391 Nucleophile (By similarity). SQ SEQUENCE 466 AA; 49801 MW; 1CF0ADFBF2DEF82E CRC64; MAKSPAARKG XPPVAVAVTA ALALLIALLS PGVAQAAGLT ATVTKESSWD NGYSASVTVR NDTSSTVSQW EVVLTLPGGT TVAQVWNAQH TSSGNSHTFT GVSWNSTIPP GGTASSGFIA SGSGEPTHCT INGAPCDEGS EPGGPGGPGT PSPDPGTQPG TGTPVERYGK VQVCGTQLCD EHGNPVQLRG MSTHGIQWFD HCLTDSSLDA LAYDWKADII RLSMYIQEDG YETNPRGFTD RMHQLIDMAT ARGLYVIVDW HILTPGDPHY NLDRAKTFFA EIAQRHASKT NVLYEIANEP NGVSWASIKS YAEEVIPVIR QRDPDSVIIV GTRGWSSLGV SEGSGPAEIA ANPVNASNIM YAFHFYAASH RDNYLNALRE ASELFPVFVT EFGTETYTGD GANDFQMADR YIDLMAERKI GWTKWNYSDD FRSGAVFQPG TCASGGPWSG SSLKASGQWV RSKLQS //