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-NOV-1991 (REL. 20, 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;
RM   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 SUBFAMILY E (FAMILY 9 OF
CC       GLYCOSYL HYDROLASES).
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DR   EMBL; X55732; BFCED1.
DR   PIR; S12025; S12025.
DR   PROSITE; PS00592; GLYCOSYL_HYDROLASES_F9.
KW   CELLULOSE DEGRADATION; HYDROLASE; GLYCOSIDASE.
FT   ACT_SITE    474    474       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
//