ID   XYLA_STROL              Reviewed;         387 AA.
AC   P15587;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA;
OS   Streptomyces olivochromogenes.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.81
RP   ANGSTROMS).
RX   PubMed=8180169; DOI=10.1021/bi00184a016;
RA   Lavie A., Allen K., Petsko G.A., Ringe D.;
RT   "X-ray crystallographic structures of D-xylose isomerase-substrate
RT   complexes position the substrate and provide evidence for metal movement
RT   during catalysis.";
RL   Biochemistry 33:5469-5480(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=2510821; DOI=10.1021/bi00444a022;
RA   Farber G.K., Glasfeld A., Tiraby G., Ringe D., Petsko G.A.;
RT   "Crystallographic studies of the mechanism of xylose isomerase.";
RL   Biochemistry 28:7289-7297(1989).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=3508293; DOI=10.1093/protein/1.6.459;
RA   Farber G.K., Petsko G.A., Ringe D.;
RT   "The 3.0 A crystal structure of xylose isomerase from Streptomyces
RT   olivochromogenes.";
RL   Protein Eng. 1:459-466(1987).
CC   -!- FUNCTION: Involved in D-xylose catabolism.
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   ---------------------------------------------------------------------------
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   PIR; S28986; S28986.
DR   PDB; 1MUW; X-ray; 0.86 A; A=2-387.
DR   PDB; 1S5M; X-ray; 0.98 A; A=2-387.
DR   PDB; 1S5N; X-ray; 0.95 A; A=2-387.
DR   PDB; 1XYA; X-ray; 1.81 A; A/B=2-387.
DR   PDB; 1XYB; X-ray; 1.96 A; A/B=2-387.
DR   PDB; 1XYC; X-ray; 2.19 A; A/B=2-387.
DR   PDB; 1XYL; X-ray; 1.80 A; A/B=2-387.
DR   PDB; 1XYM; X-ray; 1.80 A; A/B=2-387.
DR   PDB; 2GYI; X-ray; 1.60 A; A/B=2-387.
DR   PDBsum; 1MUW; -.
DR   PDBsum; 1S5M; -.
DR   PDBsum; 1S5N; -.
DR   PDBsum; 1XYA; -.
DR   PDBsum; 1XYB; -.
DR   PDBsum; 1XYC; -.
DR   PDBsum; 1XYL; -.
DR   PDBsum; 1XYM; -.
DR   PDBsum; 2GYI; -.
DR   AlphaFoldDB; P15587; -.
DR   SMR; P15587; -.
DR   STRING; 1963.AQJ27_24060; -.
DR   DrugBank; DB02438; 3-O-Methylfructose in Linear Form.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   DrugBank; DB11195; Xylitol.
DR   PRIDE; P15587; -.
DR   BRENDA; 5.3.1.5; 5943.
DR   EvolutionaryTrace; P15587; -.
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   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   Pfam; PF01261; AP_endonuc_2; 1.
DR   PRINTS; PR00688; XYLOSISMRASE.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR02631; xylA_Arthro; 1.
DR   PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium;
KW   Metal-binding; Xylose metabolism.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..387
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195803"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000250"
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         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          11..14
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           15..18
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           36..46
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           55..58
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           65..82
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           109..129
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:1XYM"
FT   HELIX           151..172
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          184..193
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           196..203
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           209..211
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           218..222
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           228..237
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          251..254
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          262..264
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           265..278
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           296..322
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           324..332
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           335..338
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           347..352
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           354..356
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   TURN            357..359
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           362..367
FT                   /evidence="ECO:0007829|PDB:1MUW"
FT   HELIX           372..383
FT                   /evidence="ECO:0007829|PDB:1MUW"
SQ   SEQUENCE   387 AA;  42923 MW;  83CCE206015B178D CRC64;
     MSYQPTPEDR FTFGLWTVGW QGRDPFGDAT RPALDPVETV QRLAELGAHG VTFHDDDLIP
     FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK DGGFTANDRD VRRYALRKTI
     RNIDLAVELG AKTYVAWGGR EGAESGAAKD VRVALDRMKE AFDLLGEYVT SQGYDTRFAI
     EPKPNEPRGD ILLPTVGHAL AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK
     LFHIDLNGQS GIKYDQDLRF GAGDLRAAFW LVDLLESAGY EGPRHFDFKP PRTEDIDGVW
     ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAQ PTAADGVQEL LADRTAFEDF
     DVDAAAARGM AFERLDQLAM DHLLGAR