ID GUN2_SCLSC Reviewed; 31 AA. AC P21834; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 02-SEP-2026, entry version 46. DE RecName: Full=Endoglucanase 2; DE Short=EG2; DE EC=3.2.1.4; DE AltName: Full=Cellulase; DE AltName: Full=Endo-1,4-beta-glucanase; DE Flags: Fragment; OS Sclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Sclerotinia. OX NCBI_TaxID=5180; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=De Bary; RX PubMed=1991146; DOI=10.1016/0304-4165(91)90181-f; RA Waksman G.; RT "Purification and characterization of two endo-beta-1,4-D-glucanases from RT Sclerotinia sclerotiorum."; RL Biochim. Biophys. Acta 1073:49-55(1991). 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 -!- MISCELLANEOUS: Active towards carboxymethyl cellulose. 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 PIR; S13663; S13663. DR BRENDA; 3.2.1.4; 5625. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing; KW Glycosidase; Hydrolase; Polysaccharide degradation. FT CHAIN 1..>31 FT /note="Endoglucanase 2" FT /id="PRO_0000184079" FT NON_TER 31 SQ SEQUENCE 31 AA; 3192 MW; A0C6D4AC68135A68 CRC64; NIYYAGVAES GGEFGVYSGS GTVLXXLPLT F //