ID GUN1_HUMIN Reviewed; 402 AA. AC P56680; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 1. DT 13-SEP-2023, entry version 109. DE RecName: Full=Endoglucanase 1; DE EC=3.2.1.4; DE AltName: Full=Cellulase 1; DE AltName: Full=Endo-1,4-beta-glucanase 1; DE AltName: Full=Endoglucanase I; GN Name=CEL7B; OS Humicola insolens (Soft-rot fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Humicola. OX NCBI_TaxID=34413; RN [1] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT TRP-37/TRP-39, AND RP PYROGLUTAMATE FORMATION AT GLN-1. RX PubMed=9335168; DOI=10.1016/s0168-1656(97)00092-8; RA Davies G.J., Ducros V., Lewis R.J., Borchert T.V., Schuelein M.; RT "Oligosaccharide specificity of a family 7 endoglucanase: insertion of RT potential sugar-binding subsites."; RL J. Biotechnol. 57:91-100(1997). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND MUTAGENESIS. RX PubMed=9761741; DOI=10.1042/bj3350409; RA MacKenzie L.F., Sulzenbacher G., Divne C., Jones T.A., Woeldike H.F., RA Schuelein M., Withers S.G., Davies G.J.; RT "Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola RT insolens at 2.2 A resolution and identification of the catalytic RT nucleophile by trapping of the covalent glycosyl-enzyme intermediate."; RL Biochem. J. 335:409-416(1998). CC -!- FUNCTION: The biological conversion of cellulose to glucose generally CC requires three types of hydrolytic enzymes: (1) Endoglucanases which CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that CC cut the disaccharide cellobiose from the non-reducing end of the CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the CC cellobiose and other short cello-oligosaccharides to glucose. 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 -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) 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; 1A39; X-ray; 2.20 A; A=2-402. DR PDB; 1DYM; X-ray; 1.75 A; A=2-402. DR PDB; 1OJI; X-ray; 2.15 A; A=2-402. DR PDB; 1OJJ; X-ray; 1.40 A; A/B=2-402. DR PDB; 1OJK; X-ray; 1.50 A; A/B=2-402. DR PDB; 2A39; X-ray; 2.20 A; A/B=2-398. DR PDB; 6YOZ; X-ray; 1.88 A; AAA/BBB=2-400. DR PDB; 6YP1; X-ray; 1.20 A; AAA=1-402. DR PDBsum; 1A39; -. DR PDBsum; 1DYM; -. DR PDBsum; 1OJI; -. DR PDBsum; 1OJJ; -. DR PDBsum; 1OJK; -. DR PDBsum; 2A39; -. DR PDBsum; 6YOZ; -. DR PDBsum; 6YP1; -. DR AlphaFoldDB; P56680; -. DR SMR; P56680; -. DR Allergome; 8280; Hum in Cellulase. DR CAZy; GH7; Glycoside Hydrolase Family 7. DR CLAE; EGL7B_HUMIN; -. DR GlyCosmos; P56680; 2 sites, No reported glycans. DR BioCyc; MetaCyc:MONOMER-17623; -. DR EvolutionaryTrace; P56680; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR CDD; cd07999; GH7_CBH_EG; 1. DR Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR001722; Glyco_hydro_7. DR InterPro; IPR037019; Glyco_hydro_7_sf. DR PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1. DR PANTHER; PTHR33753:SF1; ENDO-BETA-1,4-GLUCANASE CELB; 1. DR Pfam; PF00840; Glyco_hydro_7; 1. DR PRINTS; PR00734; GLHYDRLASE7. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; KW Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted. FT CHAIN 1..402 FT /note="Endoglucanase 1" FT /id="PRO_0000184057" FT ACT_SITE 197 FT /note="Nucleophile" FT ACT_SITE 202 FT /note="Proton donor" FT MOD_RES 1 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:9335168" FT CARBOHYD 89 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 247 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 18..24 FT DISULFID 51..73 FT DISULFID 63..69 FT DISULFID 140..365 FT DISULFID 172..195 FT DISULFID 176..194 FT DISULFID 215..234 FT DISULFID 223..228 FT DISULFID 239..315 FT STRAND 12..19 FT /evidence="ECO:0007829|PDB:1OJJ" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 23..33 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:1OJJ" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 66..72 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 81..84 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 92..98 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 127..134 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:1OJJ" FT TURN 153..156 FT /evidence="ECO:0007829|PDB:1OJI" FT HELIX 164..167 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 243..246 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 250..255 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 266..274 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 280..289 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 312..317 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 321..325 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 328..338 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 340..347 FT /evidence="ECO:0007829|PDB:1OJJ" FT TURN 350..354 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 355..358 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:1OJJ" FT TURN 367..370 FT /evidence="ECO:0007829|PDB:1OJJ" FT HELIX 372..378 FT /evidence="ECO:0007829|PDB:1OJJ" FT STRAND 383..393 FT /evidence="ECO:0007829|PDB:1OJJ" SQ SEQUENCE 402 AA; 44577 MW; E0C6D31375D1635F CRC64; QKPGETKEVH PQLTTFRCTK RGGCKPATNF IVLDSLSHPI HRAEGLGPGG CGDWGNPPPK DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP DGRVPSPRVY LLDKTKRRYE MLHLTGFEFT FDVDATKLPC GMNSALYLSE MHPTGAKSKY NPGGAYYGTG YCDAQCFVTP FINGLGNIEG KGSCCNEMDI WEANSRASHV APHTCNKKGL YLCEGEECAF EGVCDKNGCG WNNYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRRGKL EKIHRFYVQD GKVIESFYTN KEGVPYTNMI DDEFCEATGS RKYMELGATQ GMGEALTRGM VLAMSIWWDQ GGNMEWLDHG EAGPCAKGEG APSNIVQVEP FPEVTYTNLR WGEIGSTYQE LQ //