ID   GUNF_ACET2              Reviewed;         739 AA.
AC   P26224; A3DCV0;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   04-NOV-2026, entry version 158.
DE   RecName: Full=Endoglucanase F;
DE            Short=EGF;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase F;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=celF; OrderedLocusNames=Cthe_0543;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Acetivibrionales;
OC   Acetivibrionaceae; Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1805307; DOI=10.1016/0923-2508(91)90002-r;
RA   Navarro A., Chebrou M.-C., Beguin P., Aubert J.-P.;
RT   "Nucleotide sequence of the cellulase gene celF of Clostridium
RT   thermocellum.";
RL   Res. Microbiol. 142:927-936(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 /
RC   NRRL 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.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
RX   PubMed=1987137; DOI=10.1128/jb.173.1.80-85.1991;
RA   Mishra S., Beguin P., Aubert J.-P.;
RT   "Transcription of Clostridium thermocellum endoglucanase genes celF and
RT   celD.";
RL   J. Bacteriol. 173:80-85(1991).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
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; X60545; CAA43035.1; -; Genomic_DNA.
DR   EMBL; CP000568; ABN51779.1; -; Genomic_DNA.
DR   PIR; I40804; I40804.
DR   PIR; S15727; S15727.
DR   RefSeq; WP_003517595.1; NC_009012.1.
DR   AlphaFoldDB; P26224; -.
DR   SMR; P26224; -.
DR   STRING; 203119.Cthe_0543; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   GeneID; 35804292; -.
DR   KEGG; cth:Cthe_0543; -.
DR   eggNOG; COG5297; Bacteria.
DR   HOGENOM; CLU_008926_0_2_9; -.
DR   OMA; ADFNYGE; -.
DR   OrthoDB; 9758662at2; -.
DR   BioCyc; MetaCyc:MONOMER-16419; -.
DR   Proteomes; UP000002145; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   CDD; cd14256; Dockerin_I; 1.
DR   FunFam; 1.50.10.10:FF:000020; Endoglucanase; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
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; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS60032; GH9_1; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..27
FT   CHAIN           28..739
FT                   /note="Endoglucanase F"
FT                   /id="PRO_0000007950"
FT   DOMAIN          480..639
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   DOMAIN          664..737
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   REGION          28..470
FT                   /note="Catalytic"
FT   ACT_SITE        84
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        400
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        447
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   739 AA;  82089 MW;  0CD69EEFC6D4AEEF CRC64;
     MKKILAFLLT VALVAVVAIP QAVVSFAADF NYGEALQKAI MFYEFQRSGK LPENKRNNWR
     GDSALNDGAD NGLDLTGGWY DAGDHVKFNL PMAYAVTMLA WSVYESRDAY VQSGQLPYIL
     DNIKWATDYF IKCHPSPNVY YYQVGDGALD HSWWGPAEVM QMPRPSFKVD LTNPGSTVVA
     ETAAAMAASS IVFKPTDPEY AATLLRHAKE LFTFADTTRS DAGYRAAEGY YSSHSGFYDE
     LTWASIWLYL ATGDQSYLDK AESYEPHWER ERGTTLISYS WAHCWDNKLY GSLLLLAKIT
     GKSYYKQCIE NHLDYWTVGF NGSRVQYTPK GLAYLDRWGS LRYATTQAFL ASVYADWSGC
     DPAKAAVYKE FAKKQVDYAL GSTGRSFVVG FGKNPPRNPH HRTAHSSWSA LMTEPAECRH
     ILVGALVGGP DGSDSYVDRL DDYQCNEVAN DYNAGFVGAL AKMYEKYGGE PIPNFVAFET
     PGEEFYVEAA VNAAGPGFVN IKASIINKSG WPARGSDKLS AKYFVDISEA VAKGITLDQI
     TVQSTTNGGA KVSQLLPWDP DNHIYYVNID FTGINIFPGG INEYKRDVYF TITAPYGEGN
     WDNTNDFSFQ GLEQGFTSKK TEYIPLYDGN VRVWGKVPDG GSEPDPTPTI TVGPTPSVTP
     TSVPGIMLGD VNFDGRINST DYSRLKRYVI KSLEFTDPEE HQKFIAAADV DGNGRINSTD
     LYVLNRYILK LIEKFPAEQ
//