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   25-MAY-2022, entry version 84.
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}.
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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; -; 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   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF81296; SSF81296; 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