CEXY_THEST
ID CEXY_THEST Reviewed; 387 AA.
AC P40942;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Thermostable celloxylanase;
DE EC=3.2.1.4;
DE EC=3.2.1.8;
GN Name=xynB;
OS Thermoclostridium stercorarium (Clostridium stercorarium).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Thermoclostridium.
OX NCBI_TaxID=1510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F-9;
RX PubMed=7765974; DOI=10.1271/bbb.59.40;
RA Fukumura M., Sakka K., Shimada K., Ohmiya K.;
RT "Nucleotide sequence of the Clostridium stercorarium xynB gene encoding an
RT extremely thermostable xylanase, and characterization of the translated
RT product.";
RL Biosci. Biotechnol. Biochem. 59:40-46(1995).
CC -!- FUNCTION: Active toward xylan, carboxymethylcellulose, P-nitrophenyl-
CC beta-D-xylopyranoside and P-nitrophenyl-beta-D-cellobioside.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0.;
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; D12504; BAA02069.1; -; Genomic_DNA.
DR PIR; JC2484; JC2484.
DR PDB; 2DEP; X-ray; 1.80 A; A/B=41-387.
DR PDBsum; 2DEP; -.
DR AlphaFoldDB; P40942; -.
DR SMR; P40942; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P40942; -.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
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; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 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; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..387
FT /note="Thermostable celloxylanase"
FT /id="PRO_0000184061"
FT DOMAIN 41..382
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 185
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 293
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2DEP"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 148..173
FT /evidence="ECO:0007829|PDB:2DEP"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:2DEP"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 288..299
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 313..331
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:2DEP"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2DEP"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:2DEP"
SQ SEQUENCE 387 AA; 44378 MW; C7221BD5E32C8E48 CRC64;
MNKFLNKKWS LILTMGGIFL MATLSLIFAT GKKAFNDQTS AEDIPSLAEA FRDYFPIGAA
IEPGYTTGQI AELYKKHVNM LVAENAMKPA SLQPTEGNFQ WADADRIVQF AKENGMELRF
HTLVWHNQTP TGFSLDKEGK PMVEETDPQK REENRKLLLQ RLENYIRAVV LRYKDDIKSW
DVVNEVIEPN DPGGMRNSPW YQITGTEYIE VAFRATREAG GSDIKLYIND YNTDDPVKRD
ILYELVKNLL EKGVPIDGVG HQTHIDIYNP PVERIIESIK KFAGLGLDNI ITELDMSIYS
WNDRSDYGDS IPDYILTLQA KRYQELFDAL KENKDIVSAV VFWGISDKYS WLNGFPVKRT
NAPLLFDRNF MPKPAFWAIV DPSRLRE
