ID XYLA_ARTS7 Reviewed; 395 AA. AC P12070; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 134. DE RecName: Full=Xylose isomerase; DE EC=5.3.1.5; GN Name=xylA; OS Arthrobacter sp. (strain NRRL B3728). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Arthrobacter. OX NCBI_TaxID=1669; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1854339; DOI=10.1042/bj2770263; RA Loviny-Anderton T., Shaw P.C., Shin M.K., Hartley B.S.; RT "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. RT Gene cloning, sequence and expression."; RL Biochem. J. 277:263-271(1991). RN [2] RP PROTEIN SEQUENCE OF 2-21, AND CHARACTERIZATION. RX PubMed=1854338; DOI=10.1042/bj2770255; RA Smith C.A., Rangarajan M., Hartley B.S.; RT "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. RT Purification and properties."; RL Biochem. J. 277:255-261(1991). RN [3] RP ACTIVE SITES HIS-54 AND ASP-57. RX PubMed=2319597; DOI=10.1016/0022-2836(90)90316-e; RA Collyer C.A., Henrick K., Blow D.M.; RT "Mechanism for aldose-ketose interconversion by D-xylose isomerase RT involving ring opening followed by a 1,2-hydride shift."; RL J. Mol. Biol. 212:211-235(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=2769749; DOI=10.1016/0022-2836(89)90092-2; RA Henrick K., Collyer C.A., Blow D.M.; RT "Structures of D-xylose isomerase from Arthrobacter strain B3728 containing RT the inhibitors xylitol and D-sorbitol at 2.5-A and 2.3-A resolution, RT respectively."; RL J. Mol. Biol. 208:129-157(1989). RN [5] RP COMPARISON OF X-RAY STRUCTURES. RX PubMed=3508294; DOI=10.1093/protein/1.6.467; RA Henrick K., Blow D.M., Carell H.L., Glusker J.P.; RT "Comparison of backbone structures of glucose isomerase from Streptomyces RT and Arthrobacter."; RL Protein Eng. 1:467-469(1987). 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; CC Note=Binds 2 magnesium 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; X59466; CAA42073.1; -; Genomic_DNA. DR PIR; S16214; S16214. DR PDB; 1DID; X-ray; 2.50 A; A/B=2-395. DR PDB; 1DIE; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLA; X-ray; 2.30 A; A/B=2-395. DR PDB; 1XLB; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLC; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLD; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLE; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLF; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLG; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLH; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLI; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLJ; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLK; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLL; X-ray; 2.50 A; A/B=2-395. DR PDB; 1XLM; X-ray; 2.40 A; A/B=2-395. DR PDB; 4XIA; X-ray; 2.30 A; A/B=3-395. DR PDB; 5XIA; X-ray; 2.50 A; A/B=3-395. DR PDBsum; 1DID; -. DR PDBsum; 1DIE; -. DR PDBsum; 1XLA; -. DR PDBsum; 1XLB; -. DR PDBsum; 1XLC; -. DR PDBsum; 1XLD; -. DR PDBsum; 1XLE; -. DR PDBsum; 1XLF; -. DR PDBsum; 1XLG; -. DR PDBsum; 1XLH; -. DR PDBsum; 1XLI; -. DR PDBsum; 1XLJ; -. DR PDBsum; 1XLK; -. DR PDBsum; 1XLL; -. DR PDBsum; 1XLM; -. DR PDBsum; 4XIA; -. DR PDBsum; 5XIA; -. DR AlphaFoldDB; P12070; -. DR SMR; P12070; -. DR DrugBank; DB02172; 2,5-Dideoxy-2,5-Imino-D-Glucitol. DR DrugBank; DB03206; Duvoglustat. DR DrugBank; DB11195; Xylitol. DR SABIO-RK; P12070; -. DR EvolutionaryTrace; P12070; -. 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; IPR013453; XylA_actinobac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; TIGR02631; xylA_Arthro; 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 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cytoplasm; KW Direct protein sequencing; Isomerase; Magnesium; Metal-binding; KW Xylose metabolism. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1854338" FT CHAIN 2..395 FT /note="Xylose isomerase" FT /id="PRO_0000195760" FT ACT_SITE 54 FT /evidence="ECO:0000269|PubMed:2319597" FT ACT_SITE 57 FT /evidence="ECO:0000269|PubMed:2319597" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 220 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 255 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 257 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT HELIX 7..9 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 36..46 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 55..58 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 65..82 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 109..128 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 151..172 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 184..193 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 196..203 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 218..222 FT /evidence="ECO:0007829|PDB:1XLA" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 228..237 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 265..277 FT /evidence="ECO:0007829|PDB:1XLA" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 302..328 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 330..338 FT /evidence="ECO:0007829|PDB:1XLA" FT TURN 339..342 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 355..360 FT /evidence="ECO:0007829|PDB:1XLA" FT TURN 362..367 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 370..373 FT /evidence="ECO:0007829|PDB:1XLA" FT HELIX 380..391 FT /evidence="ECO:0007829|PDB:1XLA" SQ SEQUENCE 395 AA; 43292 MW; EA7A21FC47726369 CRC64; MSVQPTPADH FTFGLWTVGW TGADPFGVAT RKNLDPVEAV HKLAELGAYG ITFHDNDLIP FDATEAEREK ILGDFNQALK DTGLKVPMVT TNLFSHPVFK DGGFTSNDRS IRRFALAKVL HNIDLAAEMG AETFVMWGGR EGSEYDGSKD LAAALDRMRE GVDTAAGYIK DKGYNLRIAL EPKPNEPRGD IFLPTVGHGL AFIEQLEHGD IVGLNPETGH EQMAGLNFTH GIAQALWAEK LFHIDLNGQR GIKYDQDLVF GHGDLTSAFF TVDLLENGFP NGGPKYTGPR HFDYKPSRTD GYDGVWDSAK ANMSMYLLLK ERALAFRADP EVQEAMKTSG VFELGETTLN AGESAADLMN DSASFAGFDA EAAAERNFAF IRLNQLAIEH LLGSR //