ID GUNC_BUTFI STANDARD; PRT; 547 AA. AC P23658; DT 01-NOV-1991 (REL. 20, CREATED) DT 01-NOV-1991 (REL. 20, LAST SEQUENCE UPDATE) DT 01-AUG-1992 (REL. 23, LAST ANNOTATION UPDATE) DE CELLODEXTRINASE (EC 3.2.1.-). GN CED1. OS BUTYRIVIBRIO FIBRISOLVENS. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; ANAEROBIC RODS; OC BACTEROIDACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=H17C; RX MEDLINE; 91066844. RA BERGER E., JONES W.A., JONES D.T., WOODS D.R.; RL MOL. GEN. GENET. 223:310-318(1990). CC -!- FUNCTION: RAPIDLY HYDROLYSES SHORT-CHAIN CELLODEXTRINS TO YIELD CC EITHER CELLOBIOSE OR CELLOBIOSE AND GLUCOSE AS ENDS PRODUCTS. CC -!- CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-BETA-D-GLUCOSIDIC CC LINKAGES IN CELLULOSE. CC -!- SIMILARITY: BELONGS TO CELLULASE FAMILY E (FAMILY 9 OF GLYCOSYL CC HYDROLASES). 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; X55732. DR PIR; S12025; S12025. DR PROSITE; PS00592; GLYCOSYL_HYDROL_F9_1. DR PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2. KW CELLULOSE DEGRADATION; HYDROLASE; GLYCOSIDASE. FT ACT_SITE 474 474 BY SIMILARITY. FT ACT_SITE 520 520 BY SIMILARITY. FT ACT_SITE 529 529 BY SIMILARITY. SQ SEQUENCE 547 AA; 61056 MW; 1503350 CN; 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 //