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-MAY-2013, entry version 105.
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.
CC -!- SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) domain.
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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=43-353.
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:EC.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA: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; Cellul_bind; 1.
DR SUPFAM; SSF51445; Glyco_hydro_cat; 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 ACT_SITE 274 274 Nucleophile.
FT DISULFID 208 240
FT DISULFID 302 308
FT DISULFID 382 481
FT MUTAGEN 168 168 E->A,D,G: Reduced activity.
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
//
