ID GUN1_ACIC1 Reviewed; 562 AA. AC P54583; A0LSH7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 143. DE RecName: Full=Endoglucanase E1; DE EC=3.2.1.4; DE AltName: Full=Cellulase E1; DE AltName: Full=Endo-1,4-beta-glucanase E1; DE AltName: Full=Endocellulase E1; DE Flags: Precursor; GN OrderedLocusNames=Acel_0614; OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Acidothermales; OC Acidothermaceae; Acidothermus. OX NCBI_TaxID=351607; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Laymon R.A., Himmel M.E., Thomas S.R.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / DSM 8971 / 11B; RX PubMed=19270083; DOI=10.1101/gr.084848.108; RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V., RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C., RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.; RT "Complete genome of the cellulolytic thermophile Acidothermus RT cellulolyticus 11B provides insights into its ecophysiological and RT evolutionary adaptations."; RL Genome Res. 19:1033-1043(2009). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-398. RX PubMed=8718854; DOI=10.1021/bi9604439; RA Sakon J., Adney W.S., Himmel M.E., Thomas S.R., Kaplus P.A.; RT "Crystal structure of thermostable family 5 endocellulase E1 from RT Acidothermus cellulolyticus in complex with cellotetraose."; RL Biochemistry 35:10648-10660(1996). CC -!- FUNCTION: Has a very high specific activity on carboxymethylcellulose. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 81 degrees Celsius. Thermostable.; 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; U33212; AAA75477.1; -; Genomic_DNA. DR EMBL; CP000481; ABK52387.1; -; Genomic_DNA. DR RefSeq; WP_011719450.1; NC_008578.1. DR PDB; 1ECE; X-ray; 2.40 A; A/B=42-399. DR PDB; 1VRX; X-ray; 2.40 A; A/B=42-399. DR AlphaFoldDB; P54583; -. DR SMR; P54583; -. DR STRING; 351607.Acel_0614; -. DR DrugBank; DB02379; Beta-D-Glucose. DR CAZy; CBM2; Carbohydrate-Binding Module Family 2. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR KEGG; ace:Acel_0614; -. DR eggNOG; COG2730; Bacteria. DR HOGENOM; CLU_020735_1_0_11; -. DR InParanoid; P54583; -. DR OrthoDB; 4902692at2; -. DR EvolutionaryTrace; P54583; -. DR Proteomes; UP000008221; Chromosome. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro. 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; IPR017853; GH_hydrolase_sf. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR018087; Glyco_hydro_5_CS. DR PANTHER; PTHR35923:SF2; ENDOGLUCANASE; 1. DR PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 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. DR PDBsum; 1ECE; -. DR PDBsum; 1VRX; -. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; KW Reference proteome; Signal. FT SIGNAL 1..41 FT CHAIN 42..562 FT /note="Endoglucanase E1" FT /id="PRO_0000007834" FT DOMAIN 458..562 FT /note="CBM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135" FT REGION 42..400 FT /note="Catalytic" FT REGION 399..462 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 401..411 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 437..449 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 203 FT /note="Proton donor" FT ACT_SITE 323 FT /note="Nucleophile" FT DISULFID 75..161 FT DISULFID 209..212 FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 73..76 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 80..84 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 87..96 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 101..107 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 108..111 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 127..131 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 134..147 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 151..160 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 175..188 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 195..199 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 215..217 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 219..233 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 244..247 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 259..263 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 283..285 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 294..299 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 300..304 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 305..309 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 310..313 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 331..343 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 347..350 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 356..360 FT /evidence="ECO:0007829|PDB:1ECE" FT TURN 367..369 FT /evidence="ECO:0007829|PDB:1ECE" FT STRAND 377..380 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 382..388 FT /evidence="ECO:0007829|PDB:1ECE" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:1ECE" SQ SEQUENCE 562 AA; 60748 MW; 84E6256406A35041 CRC64; MPRALRRVPG SRVMLRVGVV VAVLALVAAL ANLAVPRPAR AAGGGYWHTS GREILDANNV PVRIAGINWF GFETCNYVVH GLWSRDYRSM LDQIKSLGYN TIRLPYSDDI LKPGTMPNSI NFYQMNQDLQ GLTSLQVMDK IVAYAGQIGL RIILDRHRPD CSGQSALWYT SSVSEATWIS DLQALAQRYK GNPTVVGFDL HNEPHDPACW GCGDPSIDWR LAAERAGNAV LSVNPNLLIF VEGVQSYNGD SYWWGGNLQG AGQYPVVLNV PNRLVYSAHD YATSVYPQTW FSDPTFPNNM PGIWNKNWGY LFNQNIAPVW LGEFGTTLQS TTDQTWLKTL VQYLRPTAQY GADSFQWTFW SWNPDSGDTG GILKDDWQTV DTVKDGYLAP IKSSIFDPVG ASASPSSQPS PSVSPSPSPS PSASRTPTPT PTPTASPTPT LTPTATPTPT ASPTPSPTAA SGARCTASYQ VNSDWGNGFT VTVAVTNSGS VATKTWTVSW TFGGNQTITN SWNAAVTQNG QSVTARNMSY NNVIQPGQNT TFGFQASYTG SNAAPTVACA AS //