ID   GUNG_ACET2              Reviewed;         566 AA.
AC   Q05332; A3DJE1;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Endoglucanase G;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase G;
DE   AltName: Full=Endo-1,4-beta-glucanase G;
DE            Short=EgG;
DE   Flags: Precursor;
GN   Name=celG; OrderedLocusNames=Cthe_2872;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8501039; DOI=10.1128/jb.175.11.3353-3360.1993;
RA   Lemaire M., Beguin P.;
RT   "Nucleotide sequence of the celG gene of Clostridium thermocellum and
RT   characterization of its product, endoglucanase CelG.";
RL   J. Bacteriol. 175:3353-3360(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; X69390; CAA49187.1; -; Genomic_DNA.
DR   EMBL; CP000568; ABN54070.1; -; Genomic_DNA.
DR   PIR; A40589; A40589.
DR   RefSeq; WP_003514548.1; NC_009012.1.
DR   AlphaFoldDB; Q05332; -.
DR   SMR; Q05332; -.
DR   IntAct; Q05332; 1.
DR   STRING; 203119.Cthe_2872; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblBacteria; ABN54070; ABN54070; Cthe_2872.
DR   KEGG; cth:Cthe_2872; -.
DR   eggNOG; COG2730; Bacteria.
DR   HOGENOM; CLU_020735_2_0_9; -.
DR   OMA; INWYGAS; -.
DR   OrthoDB; 1395441at2; -.
DR   BioCyc; MetaCyc:MON-16420; -.
DR   Proteomes; UP000002145; Chromosome.
DR   GO; GO:0043263; C:cellulosome; IDA:MENGO.
DR   GO; GO:0008810; F:cellulase activity; IDA:MENGO.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1330.10; -; 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; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..30
FT   CHAIN           31..566
FT                   /note="Endoglucanase G"
FT                   /id="PRO_0000007853"
FT   DOMAIN          497..564
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   REGION          473..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        226
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   566 AA;  63199 MW;  2CC9DE1AD87C3178 CRC64;
     MKKAKAIFSL VVALMVLAIF CFAQNTGSTA TTAAAAVDSN NDDWLHCKGN KIYDMYGNEV
     WLTGANWFGF NCSENCFHGA WYDVKTILTS IADRGINLLR IPISTELLYS WMIGKPNPVS
     SVTASNNPPY HVVNPDFYDP ETDDVKNSME IFDIIMGYCK ELGIKVMIDI HSPDANNSGH
     NYELWYGKET STCGVVTTKM WIDTLVWLAD KYKNDDTIIA FDLKNEPHGK RGYTAEVPKL
     LAKWDNSTDE NNWKYAAETC AKAILEVNPK VLIVIEGVEQ YPKTEKGYTY DTPDIWGATG
     DASPWYSAWW GGNLRGVKDY PIDLGPLNSQ IVYSPHDYGP SVYAQPWFEK DFTMQTLLDD
     YWYDTWAYIH DQGIAPILIG EWGGHMDGGK NQKWMTLLRD YIVQNRIHHT FWCINPNSGD
     TGGLLGNDWS TWDEAKYALL KPALWQTKDG KFIGLDHKIP LGSKGISLGE YYGTPQASDP
     PATPTATPTK PAASSTPSFI YGDINSDGNV NSTDLGILKR IIVKNPPASA NMDAADVNAD
     GKVNSTDYTV LKRYLLRSID KLPHTT