GUNF_ACET2
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 03-AUG-2022, entry version 147.
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; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC 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 / 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.
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 EnsemblBacteria; ABN51779; ABN51779; Cthe_0543.
DR KEGG; cth:Cthe_0543; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_008926_0_2_9; -.
DR OMA; PRFASHS; -.
DR OrthoDB; 1226595at2; -.
DR BioCyc; MetaCyc:MON-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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.710; -; 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 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; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF63446; SSF63446; 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
