ID XYLA_ECO7I Reviewed; 440 AA. AC B7NP65; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 04-NOV-2026, entry version 84. 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=ECIAI39_4077; OS Escherichia coli O7:K1 (strain IAI39 / ExPEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IAI39 / ExPEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). 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; CU928164; CAR20185.1; -; Genomic_DNA. DR RefSeq; WP_001149592.1; NC_011750.1. DR AlphaFoldDB; B7NP65; -. DR SMR; B7NP65; -. DR STRING; 585057.ECIAI39_4077; -. DR GeneID; 75173765; -. DR KEGG; ect:ECIAI39_4077; -. DR PATRIC; fig|585057.6.peg.4228; -. DR HOGENOM; CLU_037261_1_0_6; -. DR OMA; AAAICKC; -. 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 FunFam; 3.20.20.150:FF:000002; Xylose isomerase; 1. 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; XylA_bac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; NF003998; PRK05474.1; 1. DR NCBIfam; TIGR02630; xylose_isom_A; 1. DR PANTHER; PTHR48408; -; 1. DR PANTHER; PTHR48408:SF1; XYLOSE ISOMERASE; 1. DR Pfam; PF27526; XylA2_C; 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..440 FT /note="Xylose isomerase" FT /id="PRO_1000200295" FT ACT_SITE 101 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT ACT_SITE 104 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 271 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 296 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 307 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 309 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" FT BINDING 339 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455" SQ SEQUENCE 440 AA; 49719 MW; 6E21039B6EC0561F CRC64; MQAYFDQLDR VRYEGSKSSN PLAFRHYNPD ELVLGKRMEE HLRFAACYWH TFCWNGADMF GVGAFNRPWQ QPGEALALAK RKADVAFEFF HKLHVPFYCF HDVDVSPEGA SLKEYINNFA QMVDVLAGKQ EESGVKLLWG TANCFTNPRY GAGAATNPDP EVFSWAATQV VTAMEATHKL GGENYVLWGG REGYETLLNT DLRQEREQLG RFMQMVVEHK HKIGFQGTLL IEPKPQEPTK HQYDYDAATV YGFLKQFGLE KEIKLNIEAN HATLAGHSFH HEIATAIALG LFGSVDANRG DAQLGWDTDQ FPNSVEENAL VMYEILKAGG FTTGGLNFDA KVRRQSTDKY DLFYGHIGAM DTMALALKIA ARMIEDGELD KRIAQRYSGW NSELGQQILK GQMSLADLAK YAQEHNLSPV HQSGRQEQLE NLVNHYLFDK //