ID XYLA_ACTM4 Reviewed; 394 AA. AC P12851; I0GZR8; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 156. DE RecName: Full=Xylose isomerase; DE EC=5.3.1.5; GN Name=xylA; Synonyms=XI; OrderedLocusNames=AMIS_10350; OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Actinoplanes. OX NCBI_TaxID=512565; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 / RC NCIMB 12654 / NRRL B-3342 / UNCC 431; RX PubMed=2798103; DOI=10.1093/nar/17.18.7515; RA Amore R., Hollenberg C.P.; RT "Xylose isomerase from Actinoplanes missouriensis: primary structure of the RT gene and the protein."; RL Nucleic Acids Res. 17:7515-7515(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 / RC NCIMB 12654 / NRRL B-3342 / UNCC 431; RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H., RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.; RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC RT 102363)."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=3237716; DOI=10.1002/prot.340040303; RA Rey F., Jenkins J., Janin J., Lasters I., Alard P., Claessens M., RA Matthyssens G., Wodak S.J.; RT "Structural analysis of the 2.8 A model of Xylose isomerase from RT Actinoplanes missouriensis."; RL Proteins 4:165-172(1988). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=1610791; DOI=10.1021/bi00139a005; RA Jenkins J., Janin J., Rey F., Chiadmi M., van Tilbeurgh H., Lasters I., RA de Maeyer M., van Belle D., Wodak S.J., Lauwereys M., Stanssens P., RA Mrabet N.T., Snauwaert J., Matthyssens G., Lambeir A.-M.; RT "Protein engineering of xylose (glucose) isomerase from Actinoplanes RT missouriensis. 1. Crystallography and site-directed mutagenesis of metal RT binding sites."; RL Biochemistry 31:5449-5458(1992). RN [5] RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS). RX PubMed=10089406; DOI=10.1107/s090744499800626x; RA Ramin M., Shepard W., Fourme R., Kahn R.; RT "Multiwavelength anomalous solvent contrast (MASC): derivation of envelope RT structure-factor amplitudes and comparison with model values."; RL Acta Crystallogr. D 55:157-167(1999). RN [6] RP MUTAGENESIS. RX PubMed=1610792; DOI=10.1021/bi00139a006; RA Lambeir A.-M., Lauwereys M., Stanssens P., Mrabet N.T., Snauwaert J., RA van Tilbeurgh H., Matthyssens G., Lasters I., de Maeyer M., Wodak S.J., RA Jenkins J., Chiadmi M., Janin J.; RT "Protein engineering of xylose (glucose) isomerase from Actinoplanes RT missouriensis. 2. Site-directed mutagenesis of the xylose binding site."; RL Biochemistry 31:5459-5466(1992). RN [7] RP MUTAGENESIS. RX PubMed=1610793; DOI=10.1021/bi00139a007; RA van Tilbeurgh H., Jenkins J., Chiadmi M., Janin J., Wodak S.J., RA Mrabet N.T., Lambeir A.-M.; RT "Protein engineering of xylose (glucose) isomerase from Actinoplanes RT missouriensis. 3. Changing metal specificity and the pH profile by site- RT directed mutagenesis."; RL Biochemistry 31:5467-5472(1992). 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; X16042; CAA34164.1; -; Genomic_DNA. DR EMBL; AP012319; BAL86255.1; -; Genomic_DNA. DR PIR; S05998; ISMAXM. DR RefSeq; WP_014441152.1; NC_017093.1. DR PDB; 1BHW; X-ray; 4.10 A; A/B/C/D=2-394. DR PDB; 1XIM; X-ray; 2.20 A; A/B/C/D=2-394. DR PDB; 1XIN; X-ray; 2.40 A; A/B/C/D=2-394. DR PDB; 2XIM; X-ray; 2.30 A; A/B/C/D=2-394. DR PDB; 2XIN; X-ray; 2.30 A; A/B/C/D=2-394. DR PDB; 3XIM; X-ray; 2.30 A; A/B/C/D=2-394. DR PDB; 3XIN; X-ray; 2.30 A; A/B/C/D=2-394. DR PDB; 4XIM; X-ray; 2.30 A; A/B/C/D=2-394. DR PDB; 5XIM; X-ray; 2.60 A; A/B/C/D=2-394. DR PDB; 5XIN; X-ray; 2.30 A; A/B/C/D=2-394. DR PDB; 6XIM; X-ray; 2.50 A; A/B/C/D=2-394. DR PDB; 7XIM; X-ray; 2.40 A; A/B/C/D=2-394. DR PDB; 8XIM; X-ray; 2.40 A; A/B/C/D=2-394. DR PDB; 9XIM; X-ray; 2.40 A; A/B/C/D=2-394. DR PDBsum; 1BHW; -. DR PDBsum; 1XIM; -. DR PDBsum; 1XIN; -. DR PDBsum; 2XIM; -. DR PDBsum; 2XIN; -. DR PDBsum; 3XIM; -. DR PDBsum; 3XIN; -. DR PDBsum; 4XIM; -. DR PDBsum; 5XIM; -. DR PDBsum; 5XIN; -. DR PDBsum; 6XIM; -. DR PDBsum; 7XIM; -. DR PDBsum; 8XIM; -. DR PDBsum; 9XIM; -. DR AlphaFoldDB; P12851; -. DR SMR; P12851; -. DR STRING; 512565.AMIS_10350; -. DR DrugBank; DB11195; Xylitol. DR KEGG; ams:AMIS_10350; -. DR PATRIC; fig|512565.3.peg.1041; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_060750_0_0_11; -. DR OrthoDB; 9763981at2; -. DR BRENDA; 5.3.1.5; 141. DR SABIO-RK; P12851; -. DR EvolutionaryTrace; P12851; -. DR Proteomes; UP000007882; 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; IPR013453; XylA_actinobac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; TIGR02631; xylA_Arthro; 1. DR PANTHER; PTHR12110; HYDROXYPYRUVATE ISOMERASE; 1. DR PANTHER; PTHR12110:SF59; 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; Isomerase; Magnesium; KW Metal-binding; Reference proteome; Xylose metabolism. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..394 FT /note="Xylose isomerase" FT /id="PRO_0000195757" FT ACT_SITE 54 FT ACT_SITE 57 FT /evidence="ECO:0000250" 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 292 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT HELIX 7..9 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 36..46 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 55..58 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 65..82 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 109..129 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 133..137 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 141..145 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 151..172 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 184..193 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 196..203 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 218..222 FT /evidence="ECO:0007829|PDB:1XIM" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 228..238 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:2XIN" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 265..276 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:1XIM" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 301..327 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 329..337 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 341..344 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 354..359 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 361..363 FT /evidence="ECO:0007829|PDB:1XIM" FT TURN 364..366 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 369..373 FT /evidence="ECO:0007829|PDB:1XIM" FT HELIX 379..390 FT /evidence="ECO:0007829|PDB:1XIM" SQ SEQUENCE 394 AA; 43499 MW; 764B1FC35AE7A780 CRC64; MSVQATREDK FSFGLWTVGW QARDAFGDAT RTALDPVEAV HKLAEIGAYG ITFHDDDLVP FGSDAQTRDG IIAGFKKALD ETGLIVPMVT TNLFTHPVFK DGGFTSNDRS VRRYAIRKVL RQMDLGAELG AKTLVLWGGR EGAEYDSAKD VSAALDRYRE ALNLLAQYSE DRGYGLRFAI EPKPNEPRGD ILLPTAGHAI AFVQELERPE LFGINPETGH EQMSNLNFTQ GIAQALWHKK LFHIDLNGQH GPKFDQDLVF GHGDLLNAFS LVDLLENGPD GAPAYDGPRH FDYKPSRTED YDGVWESAKA NIRMYLLLKE RAKAFRADPE VQEALAASKV AELKTPTLNP GEGYAELLAD RSAFEDYDAD AVGAKGFGFV KLNQLAIEHL LGAR //