ID   A9KT91_LACP7            Unreviewed;       919 AA.
AC   A9KT91;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   04-NOV-2026, entry version 82.
DE   SubName: Full=Cellulose 1,4-beta-cellobiosidase {ECO:0000313|EMBL:ABX43721.1};
DE            EC=3.2.1.91 {ECO:0000313|EMBL:ABX43721.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Cphy_3368 {ECO:0000313|EMBL:ABX43721.1};
OS   Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS   (Clostridium phytofermentans).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC   Lachnospiraceae.
OX   NCBI_TaxID=357809 {ECO:0000313|EMBL:ABX43721.1, ECO:0000313|Proteomes:UP000000370};
RN   [1] {ECO:0000313|Proteomes:UP000000370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700394 / DSM 18823 / ISDg
RC   {ECO:0000313|Proteomes:UP000000370};
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000885; ABX43721.1; -; Genomic_DNA.
DR   RefSeq; WP_012201370.1; NC_010001.1.
DR   AlphaFoldDB; A9KT91; -.
DR   STRING; 357809.Cphy_3368; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH48; Glycoside Hydrolase Family 48.
DR   KEGG; cpy:Cphy_3368; -.
DR   eggNOG; COG4447; Bacteria.
DR   eggNOG; COG5297; Bacteria.
DR   HOGENOM; CLU_009014_0_0_9; -.
DR   OMA; AAWTLME; -.
DR   OrthoDB; 33861at2; -.
DR   Proteomes; UP000000370; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.170.160.10; Endo-1,4-beta-glucanase f. Domain 2; 1.
DR   Gene3D; 4.10.870.10; Endo-1,4-beta-glucanase f. Domain 3; 1.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 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; IPR005102; Carbo-bd_X2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR023309; Endo-1-4-beta-glucanase_dom2.
DR   InterPro; IPR027390; Endoglucanase_F_dom3.
DR   InterPro; IPR000556; Glyco_hydro_48F.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF03442; CBM_X2; 1.
DR   Pfam; PF02011; Glyco_hydro_48; 1.
DR   PRINTS; PR00844; GLHYDRLASE48.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51172; CBM3; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ABX43721.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABX43721.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000370};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..919
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5053252961"
FT   DOMAIN          768..919
FT                   /note="CBM3"
FT                   /evidence="ECO:0000259|PROSITE:PS51172"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600556-1"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600556-1"
SQ   SEQUENCE   919 AA;  101800 MW;  D68766E48F77078A CRC64;
     MQKRIYKRVA AAIMTAAMVV TLVPQGAKTS ALAGETEQAL AAAATRGTYE QRFMDLWSDI
     KNPKNGYFSP QGIPYHSIET MIVEAPDYGH VTTSEAMSYY MWLEAMYGKF TGDFSGYGTA
     WNVAEKYMIP TDADQPPTSM SKYTPSKPAT YAPEYQDPSQ YPAKLDSSAP VGSDPIWSQL
     VAAYGRNTIY GMHWLLDVDN WYGFGSRGDG TSKPSYINTF QRGEQESTWE TIPQPCWDTM
     KYGGTNGFLD LFTGDSSYAQ QFKYTDAPDA DARAIQAAYW ASEWAKDYGV NVDTYSSKAT
     MMGDYLRYSM FDKYFRKIGN STVAGTGYDA SHYLLSWYYA WGGGITADWA WVIGSSHNHF
     GYQNPMAAWV LSQNSKFKPK TTNGQADWAT SLTRQLEFYQ WLQSSEGGIA GGASNSKNGR
     YETWPAGTAT FYGMGYEANP VYKDPGSNTW FGFQAWSMQR VAEYYYKTND VKAKQILDKW
     VAWVKSVVVL KADGTFTIPS TLDWSGQPDT WTGSYTGNSK LHVTVVDSGT DLGVTGSLAN
     ALLYYSKAAN DVAAKNLAKE LLDRVWKLYR DDKGVAAPEA RADYKRFFEQ TVYVPSTFNG
     KMPNGDVIKS GIKFLDIRSK YLQDPSYPKL LAAYQSNKSP EFIYHRFWAQ CDVALANGVY
     ALLYENGSGT TDYANINPTN GSFDKAVGKQ ADLSTTLSMQ GYTFVNLSKG TTPLTLNTDY
     TVNGTTVVLK KEFLSTLPLG DTTITFNFSN SYTKPFVVTV VDTTVVVVVG DVKVQMFNGN
     TSATTNGIAP RFYLVNTGSN SINLSDVKLR YYYTIDGEKS QSFWCDWSSI GSSNVTGTFV
     KMATPKTGAD YYLEIGFTSG AGSLKAGQGI EVQGRFSKTD WSNYTQTGDY SFNSSGNSYV
     DWNKATAYIS GKLNWGIEP
//