ID GUN4_RUMAL Reviewed; 312 AA. AC Q07940; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Endoglucanase 4; DE EC=3.2.1.4; DE AltName: Full=Cellulase 4; DE AltName: Full=Endo-1,4-beta-glucanase 4; DE AltName: Full=Endoglucanase IV; DE Short=EG-IV; GN Name=Eg IV; OS Ruminococcus albus. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Ruminococcus. OX NCBI_TaxID=1264; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19. RC STRAIN=F-40; RA Karita S., Morioka K., Kajino T., Sakka K., Shimada K., Ohmiya K.; RT "Cloning and sequencing of a novel endo-1,4-beta-glucanase gene from RT Ruminococcus albus."; RL J. Ferment. Bioeng. 76:439-444(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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.; CC Temperature dependence: CC Optimum temperature is 40 degrees Celsius.; 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; AB016777; BAA32286.1; -; Genomic_DNA. DR AlphaFoldDB; Q07940; -. DR SMR; Q07940; -. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR OMA; VNLCNQY; -. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR018087; Glyco_hydro_5_CS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1. DR Pfam; PF00150; Cellulase; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing; KW Glycosidase; Hydrolase; Polysaccharide degradation. FT CHAIN 1..312 FT /note="Endoglucanase 4" FT /id="PRO_0000184050" FT ACT_SITE 135 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O85465" FT ACT_SITE 222 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:O85465" SQ SEQUENCE 312 AA; 35767 MW; A8BAADD9F93A8CBC CRC64; MLDKLKVING KLTAGEKPVR LFGLSTHGIA WYPEYICEES FNALKKDWRT NCIRIAMYTD EFRGYCKDGN KQHLKELIEK GVVIAEKLDM YVIVDWHVLC DQDPMKYIDE AEEFFSDMSK RFANKTNVIY EICNEPNCSG TWDKITEYAD RIIPIIRSNS PDALIVTGTS TWSQDIHCAL EKPLKWDNVM YSLHFYAATH KGTLRSRLER CIEAGLPVFI NEFNLCEASG KGDIDIDEAN AWYEVIDRLG LSCISWCLSN SGDTCGVFTQ NCTKLSGWTD EDIKTSGKII KGWFEAFADE ENTNEQCFRI DK //