ID   GUNX_ACETH              Reviewed;         224 AA.
AC   P15329;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Putative endoglucanase X;
DE            Short=EGX;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Fragment;
GN   Name=celX;
OS   Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS   thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=1515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3066698; DOI=10.1016/0378-1119(88)90375-7;
RA   Hall J., Hazlewood G.P., Barker P.J., Gilbert H.J.;
RT   "Conserved reiterated domains in Clostridium thermocellum endoglucanases
RT   are not essential for catalytic activity.";
RL   Gene 69:29-38(1988).
CC   -!- FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta-
CC       glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
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;
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DR   EMBL; M22759; AAA23223.1; -; Genomic_DNA.
DR   PIR; A30476; A30476.
DR   PDB; 2VPT; X-ray; 1.40 A; A=9-149.
DR   PDBsum; 2VPT; -.
DR   AlphaFoldDB; P15329; -.
DR   SMR; P15329; -.
DR   EvolutionaryTrace; P15329; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1330.10; -; 1.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW   Hydrolase; Polysaccharide degradation.
FT   CHAIN           <1..224
FT                   /note="Putative endoglucanase X"
FT                   /id="PRO_0000184076"
FT   DOMAIN          162..224
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   REGION          147..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   224 AA;  24860 MW;  F8822C5663FF2E80 CRC64;
     IMKVTQDGSI PQIASNINNW LNTHNPDVVF LWIGGNDLLL SGNVNATGLS NLIDQIFTVK
     PNVTLFVADY YPWPEAVKQY NAVIPGIVQQ KANAGKKVYF VKLSEIQFDR NTDISWDGLH
     LSEIGYTKIA NIWYKYTIDI LKALAGQTQP TPSPSPTPTD SPLVKKGDVN LDGQVNSTDF
     SLLKRYILKV VDINSINVTN ADMNNDGNIN STDISILKRI LLRN