ID GUN4_THEFU Reviewed; 880 AA. AC P26221; Q08167; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 13-SEP-2023, entry version 142. DE RecName: Full=Endoglucanase E-4; DE EC=3.2.1.4; DE AltName: Full=Cellulase E-4; DE AltName: Full=Cellulase E4; DE AltName: Full=Endo-1,4-beta-glucanase E-4; DE Flags: Precursor; GN Name=celD; 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=8215374; DOI=10.1128/aem.59.9.3032-3043.1993; RA Jung E.D., Lao G., Irwin D., Barr B.K., Benjamin A., Wilson D.B.; RT "DNA sequences and expression in Streptomyces lividans of an exoglucanase RT gene and an endoglucanase gene from Thermomonospora fusca."; RL Appl. Environ. Microbiol. 59:3032-3043(1993). RN [2] RP SEQUENCE REVISION. RA Wilson D.B.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP PARTIAL 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 [4] RP PROTEIN SEQUENCE OF 47-67. RA Wilson D.B.; RT "Cellulases of Thermomonospora fusca."; RL Methods Enzymol. 160:314-323(1988). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 47-651. RX PubMed=9334746; DOI=10.1038/nsb1097-810; RA Sakon J., Irwin D., Wilson D.B., Karplus P.A.; RT "Structure and mechanism of endo/exocellulase E4 from Thermomonospora RT fusca."; RL Nat. Struct. Biol. 4:810-818(1997). 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 9 (cellulase E) family. CC {ECO:0000255|PROSITE-ProRule:PRU10140, 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; L20093; AAB42155.1; -; Genomic_DNA. DR PIR; B42360; B42360. DR RefSeq; WP_011292599.1; NZ_QGVG01000004.1. DR PDB; 1JS4; X-ray; 2.00 A; A/B=47-651. DR PDB; 1TF4; X-ray; 1.90 A; A/B=47-651. DR PDB; 3TF4; X-ray; 2.20 A; A/B=47-651. DR PDB; 4TF4; X-ray; 2.00 A; A/B=47-651. DR PDBsum; 1JS4; -. DR PDBsum; 1TF4; -. DR PDBsum; 3TF4; -. DR PDBsum; 4TF4; -. DR AlphaFoldDB; P26221; -. DR SMR; P26221; -. DR DrugBank; DB02379; Beta-D-Glucose. DR CAZy; CBM2; Carbohydrate-Binding Module Family 2. DR CAZy; CBM3; Carbohydrate-Binding Module Family 3. DR CAZy; GH9; Glycoside Hydrolase Family 9. DR OMA; RWLDYWT; -. DR BRENDA; 3.2.1.4; 6298. DR BRENDA; 3.2.1.B42; 6298. DR UniPathway; UPA00696; -. DR EvolutionaryTrace; P26221; -. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030248; F:cellulose binding; IEA:InterPro. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd00063; FN3; 1. DR Gene3D; 1.50.10.10; -; 1. DR Gene3D; 2.60.40.290; -; 1. DR Gene3D; 2.60.40.710; Endoglucanase-like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR012341; 6hp_glycosidase-like_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; IPR001956; CBM3. DR InterPro; IPR036966; CBM3_sf. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR001701; Glyco_hydro_9. DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS. DR InterPro; IPR018221; Glyco_hydro_9_His_AS. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1. DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1. DR Pfam; PF00553; CBM_2; 1. DR Pfam; PF00942; CBM_3; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF00759; Glyco_hydro_9; 1. DR SMART; SM00637; CBD_II; 1. DR SMART; SM01067; CBM_3; 1. DR SMART; SM00060; FN3; 1. DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1. DR PROSITE; PS51173; CBM2; 1. DR PROSITE; PS00561; CBM2_A; 1. DR PROSITE; PS51172; CBM3; 1. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS60032; GH9_1; 1. DR PROSITE; PS00592; GH9_2; 1. DR PROSITE; PS00698; GH9_3; 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..46 FT /evidence="ECO:0000269|Ref.4" FT CHAIN 47..880 FT /note="Endoglucanase E-4" FT /id="PRO_0000007959" FT DOMAIN 504..652 FT /note="CBM3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513" FT DOMAIN 678..770 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 771..880 FT /note="CBM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135" FT REGION 647..688 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 104 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140" FT ACT_SITE 422 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059" FT ACT_SITE 427 FT /evidence="ECO:0000250" FT ACT_SITE 461 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060" FT ACT_SITE 470 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060" FT HELIX 52..65 FT /evidence="ECO:0007829|PDB:1TF4" FT TURN 85..88 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 109..125 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 127..132 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 136..152 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 159..165 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 167..172 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 186..190 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 196..213 FT /evidence="ECO:0007829|PDB:1TF4" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 218..237 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 259..273 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 276..285 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 295..298 FT /evidence="ECO:0007829|PDB:1JS4" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 310..321 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 324..336 FT /evidence="ECO:0007829|PDB:1TF4" FT TURN 337..339 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 361..378 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 382..400 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 413..416 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 424..427 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 430..432 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 436..439 FT /evidence="ECO:0007829|PDB:1TF4" FT TURN 466..469 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 473..476 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 477..490 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 508..517 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 520..531 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 542..550 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 557..559 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 561..563 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 565..569 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 576..579 FT /evidence="ECO:0007829|PDB:1JS4" FT STRAND 582..588 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 596..598 FT /evidence="ECO:0007829|PDB:1TF4" FT TURN 599..602 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 603..611 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 618..620 FT /evidence="ECO:0007829|PDB:1TF4" FT HELIX 622..624 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 637..641 FT /evidence="ECO:0007829|PDB:1TF4" FT STRAND 644..648 FT /evidence="ECO:0007829|PDB:1TF4" SQ SEQUENCE 880 AA; 95203 MW; 5EA9A6ABF45A4D9A CRC64; MSVTEPPPRR RGRHSRARRF LTSLGATAAL TAGMLGVPLA TGTAHAEPAF NYAEALQKSM FFYEAQRSGK LPENNRVSWR GDSGLNDGAD VGLDLTGGWY DAGDHVKFGF PMAFTATMLA WGAIESPEGY IRSGQMPYLK DNLRWVNDYF IKAHPSPNVL YVQVGDGDAD HKWWGPAEVM PMERPSFKVD PSCPGSDVAA ETAAAMAASS IVFADDDPAY AATLVQHAKQ LYTFADTYRG VYSDCVPAGA FYNSWSGYQD ELVWGAYWLY KATGDDSYLA KAEYEYDFLS TEQQTDLRSY RWTIAWDDKS YGTYVLLAKE TGKQKYIDDA NRWLDYWTVG VNGQRVPYSP GGMAVLDTWG ALRYAANTAF VALVYAKVID DPVRKQRYHD FAVRQINYAL GDNPRNSSYV VGFGNNPPRN PHHRTAHGSW TDSIASPAEN RHVLYGALVG GPGSPNDAYT DDRQDYVANE VATDYNAGFS SALAMLVEEY GGTPLADFPP TEEPDGPEIF VEAQINTPGT TFTEIKAMIR NQSGWPARML DKGTFRYWFT LDEGVDPADI TVSSAYNQCA TPEDVHHVSG DLYYVEIDCT GEKIFPGGQS EHRREVQFRI AGGPGWDPSN DWSFQGIGNE LAPAPYIVLY DDGVPVWGTA PEEGEEPGGG EGPGGGEEPG EDVTPPSAPG SPAVRDVTST SAVLTWSASS DTGGSGVAGY DVFLRAGTGQ EQKVGSTTRT SFTLTGLEPD TTYIAAVVAR DNAGNVSQRS TVSFTTLAEN GGGPDASCTV GYSTNDWDSG FTASIRITYH GTAPLSSWEL SFTFPAGQQV THGWNATWRQ DGAAVTATPM SWNSSLAPGA TVEVGFNGSW SGSNTPPTDF TLNGEPCALA //