ID GUN5_THEFU Reviewed; 466 AA. AC Q01786; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 28-JUN-2023, entry version 116. DE RecName: Full=Endoglucanase E-5; DE EC=3.2.1.4; DE AltName: Full=Cellulase E-5; DE AltName: Full=Cellulase E5; DE AltName: Full=Endo-1,4-beta-glucanase E-4; DE Flags: Precursor; GN Name=celE; OS Thermobifida fusca (Thermomonospora fusca). OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales; OC Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=2021; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=YX; RX PubMed=1904434; DOI=10.1128/jb.173.11.3397-3407.1991; RA Lao G., Ghangas G.S., Jung E.D., Wilson D.B.; RT "DNA sequences of three beta-1,4-endoglucanase genes from Thermomonospora RT 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, synergism, and RT binding domain effects."; RL Biotechnol. Bioeng. 42:1002-1013(1993). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; CC -!- PATHWAY: Glycan metabolism; cellulose degradation. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L01577; AAC09379.1; -; Genomic_DNA. DR PIR; C42360; C42360. DR PDB; 2CKR; X-ray; 1.77 A; A/B=161-466. DR PDB; 2CKS; X-ray; 1.60 A; A/B=161-466. DR PDBsum; 2CKR; -. DR PDBsum; 2CKS; -. DR SMR; Q01786; -. DR CAZy; CBM2; Carbohydrate-Binding Module Family 2. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR UniPathway; UPA00696; -. DR EvolutionaryTrace; Q01786; -. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.60.40.290; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001919; CBD2. DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR012291; CBM2_carb-bd_dom_sf. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR018087; Glyco_hydro_5_CS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1. DR Pfam; PF00553; CBM_2; 1. DR Pfam; PF00150; Cellulase; 1. DR SMART; SM00637; CBD_II; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1. DR PROSITE; PS51173; CBM2; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Direct protein sequencing; Glycosidase; Hydrolase; KW Polysaccharide degradation; Signal. FT SIGNAL 1..36 FT CHAIN 37..466 FT /note="Endoglucanase E-5" FT /id="PRO_0000007866" FT DOMAIN 37..139 FT /note="CBM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135" FT REGION 113..166 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 113..128 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 299 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O85465" FT ACT_SITE 391 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:O85465" FT HELIX 164..168 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 205..213 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 218..227 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 235..250 FT /evidence="ECO:0007829|PDB:2CKS" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 255..261 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 268..271 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 272..286 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 290..295 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 305..322 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 328..330 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 333..336 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 340..342 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 347..351 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 357..366 FT /evidence="ECO:0007829|PDB:2CKS" FT TURN 367..369 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 372..384 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 387..395 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 405..418 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 422..425 FT /evidence="ECO:0007829|PDB:2CKS" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 441..444 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 450..452 FT /evidence="ECO:0007829|PDB:2CKS" FT HELIX 455..465 FT /evidence="ECO:0007829|PDB:2CKS" 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 //