ID GUNC_BUTFI Reviewed; 547 AA. AC P23658; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 22-FEB-2023, entry version 86. DE RecName: Full=Cellodextrinase {ECO:0000303|PubMed:2250655}; DE EC=3.2.1.4 {ECO:0000269|PubMed:2250655}; GN Name=ced1 {ECO:0000303|PubMed:2250655}; OS Butyrivibrio fibrisolvens. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=831; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE RP SPECIFICITY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION. RC STRAIN=H17C; RX PubMed=2250655; DOI=10.1007/bf00265068; RA Berger E., Jones W.A., Jones D.T., Woods D.R.; RT "Sequencing and expression of a cellodextrinase (ced1) gene from RT Butyrivibrio fibrisolvens H17c cloned in Escherichia coli."; RL Mol. Gen. Genet. 223:310-318(1990). CC -!- FUNCTION: Glycoside hydrolase that rapidly hydrolyzes short-chain CC cellodextrins to yield either cellobiose or cellobiose and glucose as CC end products; cellobiose is not hydrolyzed further. Also shows limited CC activity against endoglucanase specific substrates CC (carboxymethylcellulose (CMC), lichenan, laminarin and xylan). CC {ECO:0000269|PubMed:2250655}. 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 Evidence={ECO:0000269|PubMed:2250655}; CC -!- ACTIVITY REGULATION: Is not inhibited by methylcellulose. CC {ECO:0000269|PubMed:2250655}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:2250655}. 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; X55732; CAA39264.1; -; Genomic_DNA. DR PIR; S12025; S12025. DR AlphaFoldDB; P23658; -. DR SMR; P23658; -. DR CAZy; GH9; Glycoside Hydrolase Family 9. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR CDD; cd02850; E_set_Cellulase_N; 1. DR Gene3D; 1.50.10.10; -; 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; IPR004197; Cellulase_Ig-like. 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 InterPro; IPR014756; Ig_E-set. DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1. DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1. DR Pfam; PF02927; CelD_N; 1. DR Pfam; PF00759; Glyco_hydro_9; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF48208; Six-hairpin glycosidases; 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 Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase; KW Polysaccharide degradation; Secreted. FT CHAIN 1..547 FT /note="Cellodextrinase" FT /id="PRO_0000184058" FT ACT_SITE 148 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140" FT ACT_SITE 474 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059" FT ACT_SITE 520 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060" FT ACT_SITE 529 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060" SQ SEQUENCE 547 AA; 61056 MW; 526CD2713AAA13B4 CRC64; MKKVLVNQVG FLCNAPKKAV LNFQANEFSV VDGNGKKAFD GKVEHFGTDE ISGEDTYVAD FSALTEEGKY KIVADGQESV LFSISNDAYD KLMKDICKCF YYLRCGDALS KEFAGEYYHK PCHMTKATVY GEDVEPVDVT GGWHDAGDYG RYSTAGAVAV AHLLYGVRFF KGLLDVHYDI PKVAGDKGNL PEILAEVKVE LDFLMKMQRE NGSVWHKVTT FNHAPFLMPE DDREELFLFS VSSLATADIA AVFALAYTVY KEYDAEYADK LMQKSLLAYK WLLDNPDELL FFNPDGSNTG QYDEAEDISN RFWAACALYE ATSDGKYYSD AQELKNRLEE FDKNAQKKGY QGNVFTCLGW AEVAGLGSLS LLLKREENAL CSLARNSFVA EADRLVKVSK ENGFGLCMGE NDFIWGSNME LLKYMMVLST AIRIDNKPEY KLALEAGLDY ILGCNSMDIS YVTGNGEKAF KNPHLRPTAV DDIEEPWPGL VSGGPNSGLH DERAQTLRGK GLPPMKCYID HIDCYSLNEI TIYWNSPLVF ALSGILE //