ID XYNA_THEAU STANDARD; PRT; 329 AA. AC P23360; Q9UQZ4; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 4. DT 07-MAR-2006, entry version 52. DE Endo-1,4-beta-xylanase precursor (EC 3.2.1.8) (Xylanase) (1,4-beta-D- DE xylan xylanohydrolase) (TAXI). GN Name=XYNA; OS Thermoascus aurantiacus. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Thermoascus. OX NCBI_TaxID=5087; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Bousson J.-C., Parriche M.; RT "Cloning, sequencing and overexpression of Thermoascus aurantiacus RT xylanase A (xynA)."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 27-328. RA Srinivasa B.R., Vithayathil P.J., Roy R.P., Swaminathan K.R.; RT "Significance of structural homology of Thermoascus aurantiacus RT xylanase with the exoglucanase of Cellulomonas fimi."; RL J. Protein Chem. 9:337-338(1990). RN [3] RP PROTEIN SEQUENCE OF 27-328. RX MEDLINE=92020806; PubMed=1924265; RA Srinivasa B.R., Swaminathan K.R., Ganapathy C., Roy R.P., Murthy S.K., RA Vithayathil P.J.; RT "The primary structure of xylanase from Thermoascus aurantiacus."; RL Protein Seq. Data Anal. 4:15-20(1991). RN [4] RP PROTEIN SEQUENCE OF 27-328, AND X-RAY CRYSTALLOGRAPHY (1.14 RP ANGSTROMS). RC STRAIN=IMI 216529; RX MEDLINE=21127676; PubMed=11223515; DOI=10.1107/S0907444900019089; RA Teixeira S., Lo Leggio L., Pickersgill R.W., Cardin C.; RT "Anisotropic refinement of the structure of Thermoascus aurantiacus RT xylanase I."; RL Acta Crystallogr. D 57:385-392(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS). RC STRAIN=IMI 216529; RX MEDLINE=99340281; PubMed=10409823; RX DOI=10.1002/(SICI)1097-0134(19990815)36:3<295::AID-PROT4>3.3.CO;2-Y; RA Lo Leggio L., Kalogiannis S., Bhat M.K., Pickersgill R.W.; RT "High resolution structure and sequence of T. aurantiacus xylanase I: RT implications for the evolution of thermostability in family 10 RT xylanases and enzymes with (beta)alpha-barrel architecture."; RL Proteins 36:295-306(1999). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-xylosidic CC linkages in xylans. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) CC family. CC -!- CAUTION: Ref.2 and Ref.3 sequences were incorrect. CC -!- CAUTION: Ref.2, Ref.3 and Ref.5 N-terminal modification was CC incorrect. X-ray structure has cyclic pyroglutamic acid. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ132635; CAB65468.1; -; Genomic_DNA. DR EMBL; AF127529; AAF24127.1; -; Genomic_DNA. DR PIR; A59381; A59381. DR PDB; 1GOK; X-ray; A=27-329. DR PDB; 1GOM; X-ray; A=27-329. DR PDB; 1GOO; X-ray; A=27-329. DR PDB; 1GOQ; X-ray; A=27-329. DR PDB; 1GOR; X-ray; A=27-329. DR PDB; 1I1W; X-ray; A=27-329. DR PDB; 1I1X; X-ray; A=27-329. DR PDB; 1K6A; X-ray; A=27-329. DR PDB; 1TUX; X-ray; @=28-327. DR PDB; 2BNJ; X-ray; A=27-329. DR InterPro; IPR001000; Glyco_hydro_10. DR Pfam; PF00331; Glyco_hydro_10; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00633; Glyco_10; 1. DR PROSITE; PS00591; GLYCOSYL_HYDROL_F10; 1. KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; KW Pyrrolidone carboxylic acid; Signal; Xylan degradation. FT SIGNAL 1 26 FT CHAIN 27 329 Endo-1,4-beta-xylanase. FT /FTId=PRO_0000007985. FT ACT_SITE 157 157 Proton donor. FT ACT_SITE 263 263 Nucleophile. FT MOD_RES 27 27 Pyrrolidone carboxylic acid. FT DISULFID 281 287 FT CONFLICT 243 243 G -> S (in Ref. 1). FT CONFLICT 271 271 P -> S (in Ref. 1). FT STRAND 29 30 FT HELIX 32 37 FT TURN 38 40 FT STRAND 42 48 FT HELIX 50 53 FT TURN 54 54 FT STRAND 55 55 FT TURN 56 57 FT HELIX 58 65 FT STRAND 67 73 FT TURN 74 75 FT STRAND 76 76 FT HELIX 77 80 FT STRAND 82 83 FT TURN 84 85 FT STRAND 86 86 FT HELIX 90 102 FT TURN 103 103 FT STRAND 105 112 FT STRAND 114 114 FT TURN 115 116 FT HELIX 119 122 FT TURN 123 123 FT HELIX 127 144 FT TURN 145 147 FT STRAND 148 148 FT STRAND 150 157 FT STRAND 159 159 FT TURN 161 162 FT STRAND 163 165 FT HELIX 169 173 FT TURN 174 174 FT TURN 176 177 FT HELIX 178 189 FT TURN 191 192 FT STRAND 193 201 FT STRAND 205 207 FT HELIX 208 222 FT TURN 223 224 FT STRAND 229 232 FT STRAND 235 236 FT TURN 238 240 FT HELIX 241 252 FT TURN 253 254 FT STRAND 257 266 FT TURN 267 268 FT HELIX 271 283 FT TURN 285 286 FT STRAND 287 293 FT STRAND 295 296 FT HELIX 297 299 FT STRAND 300 300 FT TURN 301 302 FT HELIX 303 305 FT STRAND 308 310 FT TURN 312 313 FT STRAND 314 314 FT STRAND 316 316 FT HELIX 318 327 SQ SEQUENCE 329 AA; 35686 MW; 8FE2F3D1A9F89815 CRC64; MVRPTILLTS LLLAPFAAAS PILEERQAAQ SVDQLIKARG KVYFGVATDQ NRLTTGKNAA IIQADFGQVT PENSMKWDAT EPSQGNFNFA GADYLVNWAQ QNGKLIRGHT LVWHSQLPSW VSSITDKNTL TNVMKNHITT LMTRYKGKIR AWDVVNEAFN EDGSLRQTVF LNVIGEDYIP IAFQTARAAD PNAKLYINDY NLDSASYPKT QAIVNRVKQW RAAGVPIDGI GSQTHLSAGQ GAGVLQALPL LASAGTPEVA ITELDVAGAS PTDYVNVVNA CLNVQSCVGI TVWGVADPDS WRASTTPLLF DGNFNPKPAY NAIVQDLQQ //