ID Q9RDB3_STRCO Unreviewed; 332 AA. AC Q9RDB3; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 02-SEP-2026, entry version 116. DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186}; DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186}; GN OrderedLocusNames=SCO2838 {ECO:0000313|EMBL:CAB65568.1}; GN ORFNames=SCE20.12c {ECO:0000313|EMBL:CAB65568.1}; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB65568.1, ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAB65568.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; RX PubMed=8843436; DOI=10.1046/j.1365-2958.1996.6191336.x; RA Redenbach M., Kieser H.M., Denapaite D., Eichner A., Cullum J., Kinashi H., RA Hopwood D.A.; RT "A set of ordered cosmids and a detailed genetic and physical map for the 8 RT Mb Streptomyces coelicolor A3(2) chromosome."; RL Mol. Microbiol. 21:77-96(1996). RN [2] {ECO:0000313|EMBL:CAB65568.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H., RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6. CC {ECO:0000256|RuleBase:RU361186}. 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; AL645882; CAB65568.1; -; Genomic_DNA. DR EMBL; AL939114; CAB65568.1; -; Genomic_DNA. DR AlphaFoldDB; Q9RDB3; -. DR SMR; Q9RDB3; -. DR FunCoup; Q9RDB3; 87. DR STRING; 100226.gene:17760449; -. DR PaxDb; 100226-gene:17760449; -. DR KEGG; sco:SCO2838; -. DR PATRIC; fig|100226.15.peg.2897; -. DR eggNOG; COG5297; Bacteria. DR HOGENOM; CLU_015488_2_1_11; -. DR InParanoid; Q9RDB3; -. DR OrthoDB; 309899at2; -. DR PhylomeDB; Q9RDB3; -. DR Proteomes; UP000001973; Chromosome. DR AbasyAtlas; Q9RDB3; -. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro. DR Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1. DR InterPro; IPR016288; Beta_cellobiohydrolase. DR InterPro; IPR036434; Beta_cellobiohydrolase_sf. DR PANTHER; PTHR34876; -; 1. DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1. DR Pfam; PF01341; Glyco_hydro_6; 1. DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1. DR PRINTS; PR00733; GLHYDRLASE6. DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361186}; KW Cellulose degradation {ECO:0000256|RuleBase:RU361186}; KW Glycosidase {ECO:0000256|RuleBase:RU361186}; KW Hydrolase {ECO:0000256|RuleBase:RU361186}; KW Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303}; KW Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303}; KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361186}; KW Reference proteome {ECO:0000313|Proteomes:UP000001973}; KW Signal {ECO:0000256|PROSITE-ProRule:PRU00303, KW ECO:0000256|RuleBase:RU361186}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|RuleBase:RU361186" FT CHAIN 22..332 FT /note="Glucanase" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" FT /id="PRO_5050346341" FT CHAIN 26..332 FT /note="Glucanase" FT /evidence="ECO:0000256|RuleBase:RU361186" FT /id="PRO_5039760654" FT ACT_SITE 158 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1" FT ACT_SITE 309 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR001100-1" FT BINDING 85 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2" FT BINDING 231 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2" FT BINDING 275 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2" FT BINDING 303 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2" FT BINDING 307 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001100-2" FT LIPID 22 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" FT LIPID 22 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00303" SQ SEQUENCE 332 AA; 34996 MW; A616E21D0E3EA277 CRC64; MSRRRAASAA ALGAAALLLA GCSSSGDGDD KAAGAGITQQ PKETGPFWVN PDGNAAQQVA SLADAGKKDQ AEEIRKIAQQ PTGEWISPEN PEEQARGFTE AADEAGRTAL LVLYNIPHRD CGQYSEGGAA DGDAYRSFVD GVAKGIGDRA ATVVLEPDAV LHLVDGCTPQ EFHEERYDLL KGAVAKLGAL KNTKVYLDAG NAGWGHPDQI FDPLKRAGVD QADGFAVNVS NFYTTEDSIA YGKQLSAKVG GKPFVIDTSR NGNGPYTEGA PDERWCNPPG RALGETPTTK TADPLVDAYL WVKRPGESDG ECKGGPKAGE WYPEYALKLA QG //