ID XYLA_PSE14 Reviewed; 438 AA. AC Q48J73; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 97. 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}; GN OrderedLocusNames=PSPPH_2356; OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1448A / Race 6; RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R., RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., RA Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola RT 1448A reveals divergence among pathovars in genes involved in virulence and RT transposition."; RL J. Bacteriol. 187:6488-6498(2005). 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; Evidence={ECO:0000255|HAMAP- CC 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; CP000058; AAZ36203.1; -; Genomic_DNA. DR RefSeq; WP_011168525.1; NC_005773.3. DR AlphaFoldDB; Q48J73; -. DR SMR; Q48J73; -. DR KEGG; psp:PSPPH_2356; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_037261_1_0_6; -. DR Proteomes; UP000000551; Chromosome. 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; IPR013452; Xylose_isom_bac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; TIGR02630; xylose_isom_A; 1. DR PANTHER; PTHR48320; -; 1. DR PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 1. DR PRINTS; PR00688; XYLOSISMRASE. DR SUPFAM; SSF51658; Xylose isomerase-like; 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..438 FT /note="Xylose isomerase" FT /id="PRO_0000236967" FT ACT_SITE 100 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT ACT_SITE 103 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 270 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 295 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 306 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 308 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 338 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" SQ SEQUENCE 438 AA; 49396 MW; FDADDF19F1C8CA04 CRC64; MPYFPAVDKV RYEGPDSDSP LAFRHYDADK LILGKPMREH LRMAACYWHT FVWPGADMFG VGTFKRPWQG SGDPLELAIG KAETAFEFFS KLGIDYYSFH DTDVAPEGSS LKEYRNNFAQ MIDQLERHQE QTGIKLLWGT ANCFSNPRFA AGAASNPDPE VFAYAATQVF SAMNATQRLK GANYVLWGGR EGYETLLNTD LRQEREQLGR FMRMVVEHKH KIGFKGDLLI EPKPQEPTKH QYDYDSATVF GFLQQYGLEK EIKVNIEANH ATLAGHSFHH EIATAVSLGI FGSIDANRGD PQNGWDTDQF PNSVEEMTLA TYEILKAGGF TNGGYNFDSK VRRQSLDEVD LFHGHVAAMD VLALALERAA AMVQNDKLQQ FKDQRYAGWQ QPFGKSLLAG EFSLESLAKH AFDKDLNPQA VSGRQELLEG VVNRFIYF //