ID GUN5_HUMIN Reviewed; 213 AA. AC P43316; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 101. DE RecName: Full=Endoglucanase-5; DE EC=3.2.1.4; DE AltName: Full=Cellulase V; DE AltName: Full=Endo-1,4-beta-glucanase V; DE Short=EG V; DE AltName: Full=Endoglucanase V; OS Humicola insolens (Soft-rot fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Mycothermus. OX NCBI_TaxID=85995; RN [1] RP NUCLEOTIDE SEQUENCE. RA Rasmussen G., Mikkelsen J.-M., Schuelein M., Patkar S.A., Hagen F., RA Hjort C.M., Hastrup S.; RT "A cellulase preparation comprising an endoglucanase enzyme."; RL Patent number WO9117243, 14-NOV-1991. RN [2] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX PubMed=8377830; DOI=10.1038/365362a0; RA Davies G.J., Dodson G.G., Hubbard R.E., Tolley S.P., Dauter Z., RA Wilson K.S., Hjort C., Mikkelsen J.M., Rasmussen G., Schuelein M.; RT "Structure and function of endoglucanase V."; RL Nature 365:362-364(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=8519779; DOI=10.1021/bi00049a037; RA Davies G.J., Tolley S.P., Henrissat B., Hjort C., Schuelein M.; RT "Structures of oligosaccharide-bound forms of the endoglucanase V from RT Humicola insolens at 1.9-A resolution."; RL Biochemistry 34:16210-16220(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). RX PubMed=15299721; DOI=10.1107/s0907444995009280; RA Davies G.J., Dodson G.G., Moore M.H., Tolley S.P., Dauter Z., Wilson K.S., RA Rasmussen G., Schuelein M.; RT "Structure determination and refinement of the Humicola insolens RT endoglucanase V at 1.5-A resolution."; RL Acta Crystallogr. D 52:7-17(1996). 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) 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 PDB; 1HD5; X-ray; 1.66 A; A=1-213. DR PDB; 2ENG; X-ray; 1.50 A; A=1-210. DR PDB; 3ENG; X-ray; 1.90 A; A=1-213. DR PDB; 4ENG; X-ray; 1.90 A; A=1-210. DR AlphaFoldDB; P43316; -. DR SMR; P43316; -. DR BindingDB; P43316; -. DR ChEMBL; CHEMBL1795107; -. DR CAZy; CBM1; Carbohydrate-Binding Module Family 1. DR CAZy; GH45; Glycoside Hydrolase Family 45. DR EvolutionaryTrace; P43316; -. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd22278; DPBB_GH45_endoglucanase; 1. DR Gene3D; 2.40.40.10; RlpA-like domain; 1. DR InterPro; IPR052288; GH45_Enzymes. DR InterPro; IPR000334; Glyco_hydro_45. DR InterPro; IPR036908; RlpA-like_sf. DR PANTHER; PTHR39730; ENDOGLUCANASE 1; 1. DR PANTHER; PTHR39730:SF1; ENDOGLUCANASE 1; 1. DR Pfam; PF02015; Glyco_hydro_45; 1. DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1. DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1. DR PDBsum; 1HD5; -. DR PDBsum; 2ENG; -. DR PDBsum; 3ENG; -. DR PDBsum; 4ENG; -. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; KW Hydrolase; Polysaccharide degradation. FT CHAIN 1..213 FT /note="Endoglucanase-5" FT /id="PRO_0000184074" FT ACT_SITE 10 FT /note="Nucleophile" FT ACT_SITE 121 FT /note="Proton donor" FT STRAND 2..8 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:2ENG" FT STRAND 21..26 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 27..29 FT /evidence="ECO:0007829|PDB:2ENG" FT STRAND 62..65 FT /evidence="ECO:0007829|PDB:2ENG" FT STRAND 68..76 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:2ENG" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:2ENG" FT STRAND 103..110 FT /evidence="ECO:0007829|PDB:2ENG" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:2ENG" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:1HD5" FT HELIX 135..139 FT /evidence="ECO:0007829|PDB:2ENG" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:2ENG" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 164..171 FT /evidence="ECO:0007829|PDB:2ENG" FT TURN 172..176 FT /evidence="ECO:0007829|PDB:3ENG" FT STRAND 181..187 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 191..197 FT /evidence="ECO:0007829|PDB:2ENG" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:2ENG" SQ SEQUENCE 213 AA; 22864 MW; 24334301BA3BC804 CRC64; ADGRSTRYWD CCKPSCGWAK KAPVNQPVFS CNANFQRITD FDAKSGCEPG GVAYSCADQT PWAVNDDFAL GFAATSIAGS NEAGWCCACY ELTFTSGPVA GKKMVVQSTS TGGDLGSNHF DLNIPGGGVG IFDGCTPQFG GLPGQRYGGI SSRNECDRFP DALKPGCYWR FDWFKNADNP SFSFRQVQCP AELVARTGCR RNDDGNFPAV QIP //