ID XYLA_THET8 Reviewed; 387 AA. AC P26997; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Xylose isomerase; DE EC=5.3.1.5; GN Name=xylA; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2022613; DOI=10.1128/jb.173.10.3078-3083.1991; RA Dekker K., Yamagata H., Sakaguchi K., Udaka S.; RT "Xylose (glucose) isomerase gene from the thermophile Thermus thermophilus: RT cloning, sequencing, and comparison with other thermostable xylose RT isomerases."; RL J. Bacteriol. 173:3078-3083(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=10329168; DOI=10.1006/jmbi.1999.2696; RA Chang C., Park B.C., Lee D.-S., Suh S.W.; RT "Crystal structures of thermostable xylose isomerases from Thermus RT caldophilus and Thermus thermophilus: possible structural determinants of RT thermostability."; RL J. Mol. Biol. 288:623-634(1999). CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-xylose = alpha-D-xylulofuranose; Xref=Rhea:RHEA:22816, CC ChEBI:CHEBI:28518, ChEBI:CHEBI:188998; EC=5.3.1.5; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D90256; BAA14301.1; -; Genomic_DNA. DR RefSeq; WP_014677651.1; NC_017767.1. DR RefSeq; YP_006250271.1; NC_017767.1. DR PDB; 1BXB; X-ray; 2.20 A; A/B/C/D=1-387. DR PDBsum; 1BXB; -. DR AlphaFoldDB; P26997; -. DR SMR; P26997; -. DR BRENDA; 5.3.1.5; 2305. DR SABIO-RK; P26997; -. DR EvolutionaryTrace; P26997; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009045; F:xylose isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1. DR HAMAP; MF_00455; Xylose_isom_A; 1. DR InterPro; IPR036237; Xyl_isomerase-like_sf. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR InterPro; IPR013453; XylA_actinobac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; TIGR02631; xylA_Arthro; 1. DR PANTHER; PTHR48320; -; 1. DR PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR PRINTS; PR00688; XYLOSISMRASE. DR SUPFAM; SSF51658; Xylose isomerase-like; 1. DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; KW Metal-binding; Xylose metabolism. FT CHAIN 1..387 FT /note="Xylose isomerase" FT /id="PRO_0000195816" FT ACT_SITE 53 FT /evidence="ECO:0000250" FT ACT_SITE 56 FT /evidence="ECO:0000250" FT BINDING 180 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 216 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 216 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 244 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 254 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 286 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 10..13 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 14..17 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 35..45 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 54..57 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 66..81 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 96..100 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 108..128 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 153..171 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 176..179 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 183..192 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 195..202 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 217..222 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 227..236 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 250..253 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 264..276 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 295..320 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 323..332 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 337..340 FT /evidence="ECO:0007829|PDB:1BXB" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 349..356 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 361..366 FT /evidence="ECO:0007829|PDB:1BXB" FT HELIX 371..382 FT /evidence="ECO:0007829|PDB:1BXB" SQ SEQUENCE 387 AA; 43907 MW; B2ED05466E4C88CE CRC64; MYEPKPEHRF TFGLWTVGNV GRDPFGDAVR ERLDPVYVVH KLAELGAYGV NLHDEDLIPR GTPPQERDQI VRRFKKALDE TGLKVPMVTA NLFSDPAFKD GAFTSPDPWV RAYALRKSLE TMDLGAELGA EIYVVWPGRE GAEVEATGKA RKVWDWVREA LNFMAAYAED QGYGYRFALE PKPNEPRGDI YFATVGSMLA FIHTLDRPER FGLNPEFAHE TMAGLNFVHA VAQALDAGKL FHIDLNDQRM SRFDQDLRFG SENLKAAFFL VDLLESSGYQ GPRHFDAHAL RTEDEEGVWA FARGCMRTYL ILKERAEAFR EDPEVKELLA AYYQEDPAAL ALLGPYSREK AEALKRAELP LEAKRRRGYA LERLDQLAVE YLLGVRG //