ID GUN2_THEFU Reviewed; 441 AA. AC P26222; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 13-SEP-2023, entry version 146. DE RecName: Full=Endoglucanase E-2; DE EC=3.2.1.4; DE AltName: Full=Cellulase E-2; DE AltName: Full=Cellulase E2; DE AltName: Full=Endo-1,4-beta-glucanase E-2; DE Flags: Precursor; GN Name=celB; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. RC STRAIN=YX; RA Jung E.D., Lao G., Irwin D., Barr B., Benjamin A., Wilson D.B.; RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 32-47. RA Wilson D.B.; RT "Cellulases of Thermomonospora fusca."; RL Methods Enzymol. 160:314-323(1988). RN [4] RP SUBUNIT, AND MUTAGENESIS OF GLU-163. RX PubMed=8347613; DOI=10.1021/bi00083a013; RA McGinnis K., Kroupis C., Wilson D.B.; RT "Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2."; RL Biochemistry 32:8146-8150(1993). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317. RX PubMed=8399160; DOI=10.1021/bi00089a006; RA Spezio M., Wilson D.B., Karplus P.A.; RT "Crystal structure of the catalytic domain of a thermophilic RT endocellulase."; RL Biochemistry 32:9906-9916(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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8347613}. CC -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has been experimentally proven. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) 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; M73321; AAC06388.1; -; mRNA. DR PIR; A42360; A42360. DR PIR; T12011; T12011. DR RefSeq; WP_011291521.1; NZ_QGVG01000015.1. DR PDB; 1TML; X-ray; 1.80 A; A=32-317. DR PDB; 2BOD; X-ray; 1.50 A; X=32-317. DR PDB; 2BOE; X-ray; 1.15 A; X=32-317. DR PDB; 2BOF; X-ray; 1.64 A; X=32-317. DR PDB; 2BOG; X-ray; 1.04 A; X=32-317. DR PDB; 3RPT; X-ray; 1.30 A; A/X=33-103, A/X=128-145, A/X=169-317. DR PDBsum; 1TML; -. DR PDBsum; 2BOD; -. DR PDBsum; 2BOE; -. DR PDBsum; 2BOF; -. DR PDBsum; 2BOG; -. DR PDBsum; 3RPT; -. DR AlphaFoldDB; P26222; -. DR SMR; P26222; -. DR CAZy; CBM2; Carbohydrate-Binding Module Family 2. DR CAZy; GH6; Glycoside Hydrolase Family 6. DR OMA; SNVSNFH; -. DR UniPathway; UPA00696; -. DR EvolutionaryTrace; P26222; -. 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; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1. DR InterPro; IPR016288; Beta_cellobiohydrolase. DR InterPro; IPR036434; Beta_cellobiohydrolase_sf. DR InterPro; IPR001919; CBD2. DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR012291; CBM2_carb-bd_dom_sf. DR InterPro; IPR018366; CBM2_CS. DR InterPro; IPR001524; Glyco_hydro_6_CS. DR InterPro; IPR006311; TAT_signal. DR PANTHER; PTHR34876; -; 1. DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1. DR Pfam; PF00553; CBM_2; 1. DR Pfam; PF01341; Glyco_hydro_6; 1. DR PRINTS; PR00733; GLHYDRLASE6. DR SMART; SM00637; CBD_II; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1. DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1. DR PROSITE; PS51173; CBM2; 1. DR PROSITE; PS00561; CBM2_A; 1. DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1. DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1. DR PROSITE; PS51318; TAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Polysaccharide degradation; Signal. FT SIGNAL 1..31 FT /note="Tat-type signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, FT ECO:0000269|Ref.3" FT CHAIN 32..441 FT /note="Endoglucanase E-2" FT /id="PRO_0000007909" FT DOMAIN 339..441 FT /note="CBM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135" FT REGION 32..320 FT /note="Catalytic" FT REGION 317..343 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..340 FT /note="Linker" FT COMPBIAS 323..341 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 110 FT ACT_SITE 148 FT /note="Proton donor" FT ACT_SITE 296 FT /note="Nucleophile" FT DISULFID 111..156 FT DISULFID 263..298 FT DISULFID 346..438 FT /evidence="ECO:0000255" FT MUTAGEN 163 FT /note="E->G: Loss of ability to form dimers." FT /evidence="ECO:0000269|PubMed:8347613" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 43..50 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 57..63 FT /evidence="ECO:0007829|PDB:2BOG" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:2BOG" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 81..95 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:2BOD" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:1TML" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:2BOE" FT HELIX 122..134 FT /evidence="ECO:0007829|PDB:2BOG" FT TURN 135..138 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 149..153 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 158..178 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 196..205 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 208..211 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 213..218 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 225..239 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:2BOG" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:2BOG" FT HELIX 307..315 FT /evidence="ECO:0007829|PDB:2BOG" SQ SEQUENCE 441 AA; 45844 MW; 87218E4537092AE5 CRC64; MSPRPLRALL GAAAAALVSA AALAFPSQAA ANDSPFYVNP NMSSAEWVRN NPNDPRTPVI RDRIASVPQG TWFAHHNPGQ ITGQVDALMS AAQAAGKIPI LVVYNAPGRD CGNHSSGGAP SHSAYRSWID EFAAGLKNRP AYIIVEPDLI SLMSSCMQHV QQEVLETMAY AGKALKAGSS QARIYFDAGH SAWHSPAQMA SWLQQADISN SAHGIATNTS NYRWTADEVA YAKAVLSAIG NPSLRAVIDT SRNGNGPAGN EWCDPSGRAI GTPSTTNTGD PMIDAFLWIK LPGEADGCIA GAGQFVPQAA YEMAIAAGGT NPNPNPNPTP TPTPTPTPPP GSSGACTATY TIANEWNDGF QATVTVTANQ NITGWTVTWT FTDGQTITNA WNADVSTSGS SVTARNVGHN GTLSQGASTE FGFVGSKGNS NSVPTLTCAA S //