ID XYLA_THETU Reviewed; 439 AA. AC P19148; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Xylose isomerase; DE EC=5.3.1.5; GN Name=xylA; OS Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacterium. OX NCBI_TaxID=33950; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 33743 / DSM 2229 / 4B; RX PubMed=2229064; DOI=10.1016/s0021-9258(17)30628-2; RA Lee C.Y., Bagdasarian M., Meng M.H., Zeikus J.G.; RT "Catalytic mechanism of xylose (glucose) isomerase from Clostridium RT thermosulfurogenes. Characterization of the structural gene and function of RT active site histidine."; RL J. Biol. Chem. 265:19082-19090(1990). RN [2] RP PROTEIN SEQUENCE OF 1-7. RX PubMed=1996956; DOI=10.1042/bj2730565; RA Lee C.Y., Zeikus J.G.; RT "Purification and characterization of thermostable glucose isomerase from RT Clostridium thermosulfurogenes and Thermoanaerobacter strain B6A."; RL Biochem. J. 273:565-571(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RC STRAIN=ATCC 33743 / DSM 2229 / 4B; RA Gallay O., Chopra R., Conti E., Brick P., Jackson R., Hartley B., RA Vieille C., Zeikus J.G., Blow D.; RL Submitted (NOV-1997) to the PDB data bank. 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=Co(2+); Xref=ChEBI:CHEBI:48828; CC Note=Binds 2 cobalt ions per subunit.; CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the xylose isomerase family. {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; J05650; AAA23285.1; -; Genomic_DNA. DR PIR; A36598; ISCLXM. DR PDB; 1A0C; X-ray; 2.50 A; A/B/C/D=2-439. DR PDBsum; 1A0C; -. DR AlphaFoldDB; P19148; -. DR SMR; P19148; -. DR SABIO-RK; P19148; -. DR EvolutionaryTrace; P19148; -. 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 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cobalt; Cytoplasm; KW Direct protein sequencing; Isomerase; Metal-binding; Xylose metabolism. FT CHAIN 1..439 FT /note="Xylose isomerase" FT /id="PRO_0000195817" FT ACT_SITE 101 FT ACT_SITE 104 FT /evidence="ECO:0000250" FT BINDING 232 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT /ligand_label="1" FT BINDING 268 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT /ligand_label="1" FT BINDING 268 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT /ligand_label="2" FT BINDING 271 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT /ligand_label="2" FT BINDING 296 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT /ligand_label="1" FT BINDING 307 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT /ligand_label="2" FT BINDING 309 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT /ligand_label="2" FT BINDING 339 FT /ligand="Co(2+)" FT /ligand_id="ChEBI:CHEBI:48828" FT /ligand_label="1" FT MUTAGEN 101 FT /note="H->F: Abolishes activity." FT STRAND 21..26 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 38..42 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 48..52 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 68..71 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 75..93 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 102..105 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 112..130 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 136..141 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 160..179 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 192..195 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 202..222 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 227..231 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 237..244 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 247..256 FT /evidence="ECO:0007829|PDB:1A0C" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 269..274 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 279..288 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 315..327 FT /evidence="ECO:0007829|PDB:1A0C" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 350..375 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 378..386 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 393..399 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 405..414 FT /evidence="ECO:0007829|PDB:1A0C" FT HELIX 425..436 FT /evidence="ECO:0007829|PDB:1A0C" SQ SEQUENCE 439 AA; 50475 MW; 55A227DBDD0EECB9 CRC64; MNKYFENVSK IKYEGPKSNN PYSFKFYNPE EVIDGKTMEE HLRFSIAYWH TFTADGTDQF GKATMQRPWN HYTDPMDIAK ARVEAAFEFF DKINAPYFCF HDRDIAPEGD TLRETNKNLD TIVAMIKDYL KTSKTKVLWG TANLFSNPRF VHGASTSCNA DVFAYSAAQV KKALEITKEL GGENYVFWGG REGYETLLNT DMEFELDNFA RFLHMAVDYA KEIGFEGQFL IEPKPKEPTK HQYDFDVANV LAFLRKYDLD KYFKVNIEAN HATLAFHDFQ HELRYARING VLGSIDANTG DMLLGWDTDQ FPTDIRMTTL AMYEVIKMGG FDKGGLNFDA KVRRASFEPE DLFLGHIAGM DAFAKGFKVA YKLVKDRVFD KFIEERYASY KDGIGADIVS GKADFRSLEK YALERSQIVN KSGRQELLES ILNQYLFAE //