GUX_CELFI
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 25-MAY-2022, entry version 141.
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; Micrococcales; 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 fimi.";
RL Gene 44:325-330(1986).
RN [2]
RP ACTIVE SITE GLU-274.
RX PubMed=1678739; DOI=10.1016/s0021-9258(18)98451-6;
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 'retaining'
RT 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 cex
RT 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 a
RT 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 cex
RT 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 / NCTC
RC 7547;
RX PubMed=9731776; DOI=10.1038/1852;
RA Notenboom V., Birsan C., Nitz M., Rose D.R., Warren R.A., Withers S.G.;
RT "Insights into transition state stabilization of the beta-1,4-glycosidase
RT Cex by covalent intermediate accumulation in active site 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 fimi by
RT 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 fimi
RT is glutamic acid 127: evidence from detailed kinetic studies of 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 generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
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) family.
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 PDB; 6QFS; X-ray; 2.20 A; A/B/C/D/E/F/G/H=380-484.
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 PDBsum; 6QFS; -.
DR AlphaFoldDB; P07986; -.
DR BMRB; P07986; -.
DR SMR; P07986; -.
DR DrugBank; DB04282; 2-deoxy-2-fluoro-Alpha-D-glucose.
DR DrugBank; DB03717; 3-Hydroxy-4-(3,4,5-trihydroxy-tetrahydro-pyran-2-yloxy)-piperidin-2-one.
DR DrugBank; DB03389; alpha-D-Xylopyranose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB02374; Xylose-Derived Imidazole.
DR DrugBank; DB01921; Xylose-derived lactam oxime.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR BRENDA; 3.2.1.91; 1233.
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 DisProt; DP01933; -.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
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; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 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
FT /note="Exoglucanase/xylanase"
FT /id="PRO_0000007960"
FT DOMAIN 42..352
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT DOMAIN 375..484
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..376
FT /note="Linker ('hinge') (Pro-Thr box)"
FT COMPBIAS 359..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:7918478"
FT ACT_SITE 274
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061,
FT ECO:0000269|PubMed:1678739"
FT DISULFID 208..240
FT /evidence="ECO:0000269|PubMed:1761039"
FT DISULFID 302..308
FT /evidence="ECO:0000269|PubMed:1761039"
FT DISULFID 382..481
FT /evidence="ECO:0000269|PubMed:1761039"
FT MUTAGEN 168
FT /note="E->A,D,G: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7910761"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 138..156
FT /evidence="ECO:0007829|PDB:3CUI"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1EXP"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 203..213
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:3CUI"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 269..282
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 285..303
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:3CUI"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:3CUI"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:3CUI"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:6QFS"
FT STRAND 392..402
FT /evidence="ECO:0007829|PDB:6QFS"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6QFS"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6QFS"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:6QFS"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1EXG"
FT STRAND 423..435
FT /evidence="ECO:0007829|PDB:6QFS"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:6QFS"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:1EXG"
FT STRAND 455..463
FT /evidence="ECO:0007829|PDB:6QFS"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:1EXG"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6QFS"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:6QFS"
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
