ID XYLA_THEP3 Reviewed; 438 AA. AC P22842; B0K7B8; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 04-NOV-2026, entry version 146. DE RecName: Full=Xylose isomerase; DE EC=5.3.1.5; GN Name=xylA; OrderedLocusNames=Teth39_2060; OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium OS thermohydrosulfuricum). OC Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=340099; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1368665; DOI=10.1271/bbb1961.55.221; RA Dekker K., Yamagata H., Sakaguchi K., Udaka S.; RT "Xylose (glucose) isomerase gene from the thermophile Clostridium RT thermohydrosulfuricum; cloning, sequencing, and expression in Escherichia RT coli."; RL Agric. Biol. Chem. 55:221-227(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9495747; DOI=10.1128/jb.180.5.1103-1109.1998; RA Erbeznik M., Dawson K.A., Strobel H.J.; RT "Cloning and characterization of transcription of the xylAB operon in RT Thermoanaerobacter ethanolicus."; RL J. Bacteriol. 180:1103-1109(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33223 / DSM 2355 / 39E; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J., RA Richardson P.; RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E."; RL Submitted (JAN-2008) 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC46145.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=ABY95684.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; D00756; BAA00652.1; -; Genomic_DNA. DR EMBL; AF001974; AAC46145.1; ALT_INIT; Genomic_DNA. DR EMBL; CP000924; ABY95684.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_013570854.1; NC_010321.1. DR AlphaFoldDB; P22842; -. DR SMR; P22842; -. DR STRING; 340099.Teth39_2060; -. DR KEGG; tpd:Teth39_2060; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_037261_1_0_9; -. DR OMA; AAAICKC; -. DR Proteomes; UP000002156; 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 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; IPR013022; Xyl_isomerase-like_TIM-brl. 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; PF01261; AP_endonuc_2; 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 Reference proteome; Xylose metabolism. FT CHAIN 1..438 FT /note="Xylose isomerase" FT /id="PRO_0000195812" FT ACT_SITE 100 FT /evidence="ECO:0000250" FT ACT_SITE 103 FT /evidence="ECO:0000250" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 270 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 295 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 306 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 308 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 338 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" SQ SEQUENCE 438 AA; 50158 MW; 4B3B0BC1B7413DE7 CRC64; MEYFKNVPQI KYEGPKSNNP YAFKFYNPDE IIDGKPLKEH LRFSVAYWHT FTANGTDPFG APTMQRPWDH FTDPMDIAKA RVEAAFELFE KLDVPFFCFH DRDIAPEGET LRETNKNLDT IVAMIKDYLK TSKTKVLWGT ANLFSNPRFV HGAATSCNAD VFAYAAAQVK KALEITKELG GQNYVFWGGR EGYETLLNTD MELELDNLAR FLHMAVEYAQ EIGFEGQFLI EPKPKEPTKH QYDFDAASVH AFLKKYDLDK YFKLNIEANH ATLAGHDFQH ELRYARINNM LGSIDANMGD MLLGWDTDQY PTDIRMTTLA MYEVIKMGGF NKGGLNFDAK VRRASFEPED LFLGHIAGMD AFAKGFKVAY KLVKDGVFDR FIEERYKSYR EGIGAEIVSG KANFKTLEEY ALNNPKIENK SGKQELLESI LNQYLFSE //