ID GUNA_CELFI Reviewed; 449 AA. AC P07984; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 28-JUN-2023, entry version 120. DE RecName: Full=Endoglucanase A; DE EC=3.2.1.4; DE AltName: Full=Cellulase A; DE AltName: Full=Endo-1,4-beta-glucanase A; DE Flags: Precursor; GN Name=cenA; OS Cellulomonas fimi. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=1708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3023193; DOI=10.1016/0378-1119(86)90196-4; RA Wong W.K.R., Gerhard B., Guo Z.M., Kilburn D.G., Warren R.A.J., RA Miller R.C. Jr.; RT "Characterization and structure of an endoglucanase gene cenA of RT Cellulomonas fimi."; RL Gene 44:315-324(1986). RN [2] RP DOMAINS. RX PubMed=2681184; DOI=10.1016/s0021-9258(19)84644-6; RA Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.; RT "Structural and functional analysis of a bacterial cellulase by RT proteolysis."; RL J. Biol. Chem. 264:17802-17808(1989). RN [3] RP DISULFIDE BONDS. RX PubMed=1761039; DOI=10.1111/j.1432-1033.1991.tb16384.x; RA Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A., RA Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.; RT "Structural and functional relationships in two families of beta-1,4- RT glycanases."; RL Eur. J. Biochem. 202:367-377(1991). CC -!- FUNCTION: The biological conversion of cellulose to glucose generally CC requires three types of hydrolytic enzymes: (1) Endoglucanases which CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that CC cut the disaccharide cellobiose from the non-reducing end of the CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the CC cellobiose and other short cello-oligosaccharides to glucose. 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 -!- PTM: The linker region (also termed 'hinge') may be a potential site CC for proteolysis. CC -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has not 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; M15823; AAA23084.1; -; Genomic_DNA. DR PIR; A24993; A24993. DR AlphaFoldDB; P07984; -. DR SMR; P07984; -. DR CAZy; CBM2; Carbohydrate-Binding Module Family 2. DR CAZy; GH6; Glycoside Hydrolase Family 6. DR SABIO-RK; P07984; -. 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-KW. 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 PIRSF; PIRSF001100; Beta_cellobiohydrolase; 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 Carbohydrate metabolism; Cellulose degradation; Disulfide bond; KW Glycosidase; Hydrolase; Polysaccharide degradation; Signal. FT SIGNAL 1..31 FT /note="Tat-type signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648" FT CHAIN 32..449 FT /note="Endoglucanase A" FT /id="PRO_0000007903" FT DOMAIN 32..137 FT /note="CBM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135" FT REGION 127..170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 139..168 FT /note="Linker ('hinge') (Pro-Thr box)" FT REGION 438..449 FT /note="Catalytic" FT COMPBIAS 127..141 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 142..167 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 247 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056" FT ACT_SITE 283 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057" FT ACT_SITE 423 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056" FT DISULFID 35..134 FT /evidence="ECO:0000269|PubMed:1761039" FT DISULFID 248..291 FT /evidence="ECO:0000269|PubMed:1761039" FT DISULFID 390..426 FT /evidence="ECO:0000269|PubMed:1761039" SQ SEQUENCE 449 AA; 46731 MW; 67FF887814B3348D CRC64; MSTRRTAAAL LAAAAVAVGG LTALTTTAAQ AAPGCRVDYA VTNQWPGGFG ANVTITNLGD PVSSWKLDWT YTAGQRIQQL WNGTASTNGG QVSVTSLPWN GSIPTGGTAS FGFNGSWAGS NPTPASFSLN GTTCTGTVPT TSPTPTPTPT TPTPTPTPTP TPTPTVTPQP TSGFYVDPTT QGYRAWQAAS GTDKALLEKI ALTPQAYWVG NWADASHAQA EVADYTGRAV AAGKTPMLVV YAIPGRDCGS HSGGGVSESE YARWVDTVAQ GIKGNPIVIL EPDALAQLGD CSGQGDRVGF LKYAAKSLTL KGARVYIDAG HAKWLSVDTP VNRLNQVGFE YAVGFALNTS NYQTTADSKA YGQQISQRLG GKKFVIDTSR NGNGSNGEWC NPRGRALGER PVAVNDGSGL DALLWVKLPG ESDGACNGGP AAGQWWQEIA LEMARNARW //