ID XYLA_STROI Reviewed; 388 AA. AC Q93RJ9; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 28-JUN-2023, entry version 78. DE RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455}; DE EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455}; GN Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455}; OS Streptomyces olivaceoviridis (Streptomyces corchorusii). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1921; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kaneko T.; RT "Streptomyces olivaceoviridis D-xylose isomerase (xylA) gene."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00455}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00455}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00455}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00455}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00455}. CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000255|HAMAP- CC Rule:MF_00455}. 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; AB038265; BAB62014.1; -; Genomic_DNA. DR PIR; JC7663; JC7663. DR AlphaFoldDB; Q93RJ9; -. DR SMR; Q93RJ9; -. 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 PANTHER; PTHR12110; HYDROXYPYRUVATE ISOMERASE; 1. DR PANTHER; PTHR12110:SF54; XYLOSE ISOMERASE; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR PRINTS; PR00688; XYLOSISMRASE. DR SUPFAM; SSF51658; Xylose isomerase-like; 1. DR TIGRFAMs; TIGR02631; xylA_Arthro; 1. DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; Metal-binding; KW Xylose metabolism. FT CHAIN 1..388 FT /note="Xylose isomerase" FT /id="PRO_0000195802" FT ACT_SITE 54 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT ACT_SITE 57 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 220 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 255 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 257 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 287 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" SQ SEQUENCE 388 AA; 42993 MW; C13A578836CD996C CRC64; MSYQPTPEDR FTFGLWTVGW QGRDPFGDAT RRALDPVETV QRLAELGAHG VTFHDDDLIP FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK DGAFTANDRD VRRYALRKTI RNIDLAAELG AKTYVAWGGR EGAESGAAKD VRSALDRMKE AFDLLGEYVT SQGYVLRFAI EPKPNEPRGD ILLPTVGHAL AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQS GIKYDQDLRF GAGDLRSALW MVDLLESAGY EGPRHFDFKP PRTEDLDGVW ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDQLAQ PTAADGLEDL LADRAAFEDF DVEAAAARGM AFERLDQLAM DHLLGARG //