ID XYLA_THENN Reviewed; 444 AA. AC B9K7G3; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 75. 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=CTN_0720; OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=309803; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E; RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J., RA Kim J.J., Park K.J., Lee S.Y.; RT "The genome sequence of the hyperthermophilic bacterium Thermotoga RT neapolitana."; RL Submitted (NOV-2007) 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; 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; CP000916; ACM22896.1; -; Genomic_DNA. DR RefSeq; WP_015919215.1; NC_011978.1. DR AlphaFoldDB; B9K7G3; -. DR SMR; B9K7G3; -. DR STRING; 309803.CTN_0720; -. DR KEGG; tna:CTN_0720; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_037261_1_0_0; -. DR Proteomes; UP000000445; 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; IPR013022; Xyl_isomerase-like_TIM-brl. 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 Pfam; PF01261; AP_endonuc_2; 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..444 FT /note="Xylose isomerase" FT /id="PRO_1000200313" 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" SQ SEQUENCE 444 AA; 50893 MW; 21F606C4D5F68D0B CRC64; MAEFFPEIPK VQFEGKESTN PLAFKFYDPE EIIDGKPLKD HLKFSVAFWH TFVNEGRDPF GDPTADRPWN RYTDPMDKAF ARVDALFEFC EKLNIEYFCF HDRDIAPEGK TLRETNKILD KVVERIKERM KDSNVKLLWG TANLFSHPRY MHGAATTCSA DVFAYAAAQV KKALEITKEL GGEGYVFWGG REGYETLLNT DLGFELENLA RFLRMAVDYA KRIGFTGQFL IEPKPKEPTK HQYDFDVATA YAFLKSHGLD EYFKFNIEAN HATLAGHTFQ HELRMARILG KLGSIDANQG DLLLGWDTDQ FPTNVYDTTL AMYEVIKAGG FTKGGLNFDA KVRRASYKVE DLFIGHIAGM DTFALGFKVA YKLVKDGVLD KFIEEKYRSF REGIGRDIVE GKVDFEKLEE YIIDKETIEL PSGKQEYLES LINSYIVKTI LELR //