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Database: UniProt
Entry: P07986
LinkDB: P07986
Original site: P07986 
ID   GUX_CELFI               Reviewed;         484 AA.
AC   P07986;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   01-OCT-2014, entry version 108.
DE   RecName: Full=Exoglucanase/xylanase;
DE   Includes:
DE     RecName: Full=Exoglucanase;
DE              EC=3.2.1.91;
DE     AltName: Full=1,4-beta-cellobiohydrolase;
DE     AltName: Full=Beta-1,4-glycanase CEX;
DE     AltName: Full=Exocellobiohydrolase;
DE   Includes:
DE     RecName: Full=Endo-1,4-beta-xylanase B;
DE              Short=Xylanase B;
DE              EC=3.2.1.8;
DE   Flags: Precursor;
GN   Name=cex; Synonyms=xynB;
OS   Cellulomonas fimi.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3096818; DOI=10.1016/0378-1119(86)90197-6;
RA   O'Neill G., Goh S.H., Warren R.A.J., Kilburn D.G., Miller R.C. Jr.;
RT   "Structure of the gene encoding the exoglucanase of Cellulomonas
RT   fimi.";
RL   Gene 44:325-330(1986).
RN   [2]
RP   ACTIVE SITE GLU-274.
RX   PubMed=1678739;
RA   Tull D., Withers S.G., Gilkes N.R., Kilburn D.G., Warren R.A.J.,
RA   Aebersold R.;
RT   "Glutamic acid 274 is the nucleophile in the active site of a
RT   'retaining' exoglucanase from Cellulomonas fimi.";
RL   J. Biol. Chem. 266:15621-15625(1991).
RN   [3]
RP   DISULFIDE BONDS.
RX   PubMed=1761039; DOI=10.1111/j.1432-1033.1991.tb16384.x;
RA   Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A.,
RA   Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr.;
RT   "Structural and functional relationships in two families of beta-1,4-
RT   glycanases.";
RL   Eur. J. Biochem. 202:367-377(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=7918478; DOI=10.1021/bi00208a003;
RA   White A., Withers S.G., Gilkes N.R., Rose D.R.;
RT   "Crystal structure of the catalytic domain of the beta-1,4-glycanase
RT   cex from Cellulomonas fimi.";
RL   Biochemistry 33:12546-12552(1994).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=8564541; DOI=10.1038/nsb0296-149;
RA   White A., Tull D., Johns K., Withers S.G., Rose D.R.;
RT   "Crystallographic observation of a covalent catalytic intermediate in
RT   a beta-glycosidase.";
RL   Nat. Struct. Biol. 3:149-154(1996).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-353.
RX   PubMed=9537990; DOI=10.1021/bi9729211;
RA   Notenboom V., Birsan C., Warren R.A.J., Withers S.G., Rose D.R.;
RT   "Exploring the cellulose/xylan specificity of the beta-1,4-glycanase
RT   cex from Cellulomonas fimi through crystallography and mutation.";
RL   Biochemistry 37:4751-4758(1998).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 42-353.
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547;
RX   PubMed=9731776; DOI=10.1038/1852;
RA   Notenboom V., Birsan C., Nitz M., Rose D.R., Warren R.A.,
RA   Withers S.G.;
RT   "Insights into transition state stabilization of the beta-1,4-
RT   glycosidase Cex by covalent intermediate accumulation in active site
RT   mutants.";
RL   Nat. Struct. Biol. 5:812-818(1998).
RN   [8]
RP   STRUCTURE BY NMR OF 377-484.
RX   PubMed=7766609; DOI=10.1021/bi00021a011;
RA   Xu G.-Y., Ong E., Gilkes N.R., Kilburn D.G., Muhandiram D.R.,
RA   Harris-Brandts M., Carver J.P., Kay L.E., Harvey T.S.;
RT   "Solution structure of a cellulose-binding domain from Cellulomonas
RT   fimi by nuclear magnetic resonance spectroscopy.";
RL   Biochemistry 34:6993-7009(1995).
RN   [9]
RP   MUTAGENESIS OF GLU-168.
RX   PubMed=7910761; DOI=10.1021/bi00186a042;
RA   Macleod A.M., Lindhorst T., Withers S.G., Warren R.A.J.;
RT   "The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas
RT   fimi is glutamic acid 127: evidence from detailed kinetic studies of
RT   mutants.";
RL   Biochemistry 33:6371-6376(1994).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 43-354.
RX   PubMed=10995222; DOI=10.1021/bi0010625;
RA   Notenboom V., Williams S.J., Hoos R., Withers S.G., Rose D.R.;
RT   "Detailed structural analysis of glycosidase/inhibitor interactions:
RT   complexes of Cex from Cellulomonas fimi with xylobiose-derived aza-
RT   sugars.";
RL   Biochemistry 39:11553-11563(2000).
CC   -!- FUNCTION: Hydrolyzes both cellulose and xylan. Has also weak
CC       endoglucanase activity.
CC   -!- FUNCTION: The biological conversion of cellulose to glucose
CC       generally requires three types of hydrolytic enzymes: (1)
CC       Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2)
CC       Exocellobiohydrolases that cut the dissaccharide cellobiose from
CC       the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-
CC       glucosidases which hydrolyze the cellobiose and other short cello-
CC       oligosaccharides to glucose.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose and cellotetraose, releasing cellobiose from
CC       the non-reducing ends of the chains.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- MISCELLANEOUS: The linker region (also termed "hinge") may be a
CC       potential site for proteolysis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
CC       {ECO:0000305}.
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DR   EMBL; M15824; AAA56791.1; -; Genomic_DNA.
DR   PIR; A24994; A24994.
DR   PDB; 1EXG; NMR; -; A=377-484.
DR   PDB; 1EXH; NMR; -; A=377-484.
DR   PDB; 1EXP; X-ray; 1.80 A; A=42-353.
DR   PDB; 1FH7; X-ray; 1.82 A; A=42-353.
DR   PDB; 1FH8; X-ray; 1.95 A; A=42-353.
DR   PDB; 1FH9; X-ray; 1.72 A; A=42-353.
DR   PDB; 1FHD; X-ray; 1.90 A; A=42-353.
DR   PDB; 1J01; X-ray; 2.00 A; A=42-353.
DR   PDB; 2EXO; X-ray; 1.80 A; A=42-353.
DR   PDB; 2HIS; X-ray; 1.84 A; A=42-353.
DR   PDB; 2XYL; X-ray; 1.90 A; A=42-353.
DR   PDB; 3CUF; X-ray; 1.67 A; A=42-356.
DR   PDB; 3CUG; X-ray; 1.68 A; A=42-356.
DR   PDB; 3CUH; X-ray; 1.89 A; A=42-356.
DR   PDB; 3CUI; X-ray; 1.50 A; A=42-356.
DR   PDB; 3CUJ; X-ray; 1.70 A; A=42-356.
DR   PDBsum; 1EXG; -.
DR   PDBsum; 1EXH; -.
DR   PDBsum; 1EXP; -.
DR   PDBsum; 1FH7; -.
DR   PDBsum; 1FH8; -.
DR   PDBsum; 1FH9; -.
DR   PDBsum; 1FHD; -.
DR   PDBsum; 1J01; -.
DR   PDBsum; 2EXO; -.
DR   PDBsum; 2HIS; -.
DR   PDBsum; 2XYL; -.
DR   PDBsum; 3CUF; -.
DR   PDBsum; 3CUG; -.
DR   PDBsum; 3CUH; -.
DR   PDBsum; 3CUI; -.
DR   PDBsum; 3CUJ; -.
DR   ProteinModelPortal; P07986; -.
DR   SMR; P07986; 42-353, 376-484.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EvolutionaryTrace; P07986; -.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; -; 1.
DR   InterPro; IPR008965; Carb-bd_dom.
DR   InterPro; IPR012291; CBD_carb-bd_dom.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR001919; Cellulose-bd_dom_fam2_bac.
DR   InterPro; IPR001000; Glyco_hydro_10.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS00591; GLYCOSYL_HYDROL_F10; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Disulfide bond; Glycosidase; Hydrolase; Multifunctional enzyme;
KW   Polysaccharide degradation; Repeat; Signal; Xylan degradation.
FT   SIGNAL        1     41
FT   CHAIN        42    484       Exoglucanase/xylanase.
FT                                /FTId=PRO_0000007960.
FT   DOMAIN      375    484       CBM2.
FT   REGION       42    356       Catalytic.
FT   REGION      357    376       Linker ("hinge") (Pro-Thr box).
FT   ACT_SITE    168    168       Proton donor.
FT                                {ECO:0000269|PubMed:7918478}.
FT   ACT_SITE    274    274       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10061,
FT                                ECO:0000269|PubMed:1678739}.
FT   DISULFID    208    240       {ECO:0000269|PubMed:1761039}.
FT   DISULFID    302    308       {ECO:0000269|PubMed:1761039}.
FT   DISULFID    382    481       {ECO:0000269|PubMed:1761039}.
FT   MUTAGEN     168    168       E->A,D,G: Reduced activity.
FT                                {ECO:0000269|PubMed:7910761}.
FT   HELIX        45     52
FT   STRAND       55     60
FT   HELIX        62     66
FT   HELIX        68     77
FT   STRAND       79     85
FT   HELIX        89     92
FT   HELIX       102    114
FT   STRAND      117    128
FT   HELIX       131    134
FT   HELIX       138    156
FT   TURN        157    159
FT   STRAND      162    167
FT   STRAND      174    176
FT   HELIX       181    186
FT   HELIX       187    189
FT   HELIX       190    201
FT   STRAND      203    213
FT   STRAND      215    218
FT   HELIX       219    234
FT   STRAND      240    243
FT   STRAND      246    248
FT   HELIX       256    264
FT   TURN        265    267
FT   STRAND      269    282
FT   HELIX       285    303
FT   STRAND      308    314
FT   TURN        318    320
FT   HELIX       323    326
FT   STRAND      334    336
FT   HELIX       344    353
FT   STRAND      382    385
FT   STRAND      388    403
FT   STRAND      405    407
FT   STRAND      409    417
FT   STRAND      419    421
FT   STRAND      423    435
FT   STRAND      438    443
FT   HELIX       446    448
FT   STRAND      452    463
FT   STRAND      465    467
FT   STRAND      474    476
FT   STRAND      479    483
SQ   SEQUENCE   484 AA;  51291 MW;  6EE5486BC0E9B02F CRC64;
     MPRTTPAPGH PARGARTALR TTRRRAATLV VGATVVLPAQ AATTLKEAAD GAGRDFGFAL
     DPNRLSEAQY KAIADSEFNL VVAENAMKWD ATEPSQNSFS FGAGDRVASY AADTGKELYG
     HTLVWHSQLP DWAKNLNGSA FESAMVNHVT KVADHFEGKV ASWDVVNEAF ADGDGPPQDS
     AFQQKLGNGY IETAFRAARA ADPTAKLCIN DYNVEGINAK SNSLYDLVKD FKARGVPLDC
     VGFQSHLIVG QVPGDFRQNL QRFADLGVDV RITELDIRMR TPSDATKLAT QAADYKKVVQ
     ACMQVTRCQG VTVWGITDKY SWVPDVFPGE GAALVWDASY AKKPAYAAVM EAFGASPTPT
     PTTPTPTPTT PTPTPTSGPA GCQVLWGVNQ WNTGFTANVT VKNTSSAPVD GWTLTFSFPS
     GQQVTQAWSS TVTQSGSAVT VRNAPWNGSI PAGGTAQFGF NGSHTGTNAA PTAFSLNGTP
     CTVG
//
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