ID Q08YE2_STIAD Unreviewed; 438 AA. AC Q08YE2; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|HAMAP-Rule:MF_00455}; DE EC=5.3.1.5 {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|HAMAP-Rule:MF_00455}; GN Name=xylA {ECO:0000256|HAMAP-Rule:MF_00455, GN ECO:0000313|EMBL:EAU65496.1}; GN OrderedLocusNames=STAUR_2372 {ECO:0000313|EMBL:ADO70176.1}; GN ORFNames=STIAU_1199 {ECO:0000313|EMBL:EAU65496.1}; OS Stigmatella aurantiaca (strain DW4/3-1). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Archangiaceae; Stigmatella. OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU65496.1, ECO:0000313|Proteomes:UP000032702}; RN [1] {ECO:0000313|EMBL:EAU65496.1, ECO:0000313|Proteomes:UP000032702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU65496.1, RC ECO:0000313|Proteomes:UP000032702}; RA Nierman W.C.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADO70176.1, ECO:0000313|Proteomes:UP000001351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO70176.1, RC ECO:0000313|Proteomes:UP000001351}; RX PubMed=21037205; DOI=10.1093/molbev/msq292; RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M., RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C., RA Sogaard-Andersen L.; RT "Comparative genomic analysis of fruiting body formation in Myxococcales."; RL Mol. Biol. Evol. 28:1083-1097(2011). 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:0000256|ARBA:ARBA00033659, ECO:0000256|HAMAP- CC Rule:MF_00455, ECO:0000256|RuleBase:RU000609}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00455}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00455}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00455, CC ECO:0000256|RuleBase:RU000610}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00455, ECO:0000256|RuleBase:RU000610}. CC -!- SIMILARITY: Belongs to the xylose isomerase family. CC {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|HAMAP-Rule:MF_00455, CC ECO:0000256|RuleBase:RU000609}. 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; CP002271; ADO70176.1; -; Genomic_DNA. DR EMBL; AAMD01000080; EAU65496.1; -; Genomic_DNA. DR RefSeq; WP_002615196.1; NZ_AAMD01000080.1. DR STRING; 378806.STAUR_2372; -. DR KEGG; sur:STAUR_2372; -. DR PATRIC; fig|378806.16.peg.4541; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_037261_1_0_7; -. DR OrthoDB; 9763981at2; -. DR Proteomes; UP000001351; Chromosome. DR Proteomes; UP000032702; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00455}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00455}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00455}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00455}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00455}; KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP- KW Rule:MF_00455}. FT DOMAIN 91..282 FT /note="Xylose isomerase-like TIM barrel" FT /evidence="ECO:0000259|Pfam:PF01261" FT ACT_SITE 102 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT ACT_SITE 105 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 269 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 269 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 272 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 297 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 308 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 310 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 340 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" SQ SEQUENCE 438 AA; 48793 MW; D79D3CE090618302 CRC64; MREPFFADIA PVRYEGLKST HPLAYRWYEP NRLVLGRSMA EHLRLAVCYW HTFCWAGSDP FGPATMPRPW MQPGDAMALA EQKLSVAFEL FEKLGVPFFT FHDRDLAPEL GSLRASQHAL KVMLDKAQVM MERTGVKLLW GTANLFSHPR YMAGAATNPD PEVFAHAAAQ VRDALEATHR LGGANYVLWG GREGYDTLLN THLKREIDQL GRFLNLVVEH KHKLGFKGTI LIEPKPMEPT KHQYDYDVST VYGFLERSGL AKEVKVNIEV NHATLAGHTF DHEVATAIAL GIFGSIDMNR GDPQNGWDTD QFPNNAPELV LPLYRILQAG GFTTGGINFD AKVRRQSIEP VDLLHAHVGA IDVLARALLA AAAMLEEGAL SRHIDQRYAG WEGELGRKIT EGQIDLAGLA NLAVDADLAP KPRSGRQEML ENLVNRYI //