ID   XYLA_STRVN              Reviewed;          12 AA.
AC   P14405;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
DE   Flags: Fragment;
GN   Name=xylA;
OS   Streptomyces violaceoruber.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1935;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=LMG 7183;
RX   PubMed=2604694; DOI=10.1042/bj2630195;
RA   Vangrysperre W., Ampe C., Kersters-Hilderson H., Tempst P.;
RT   "Single active-site histidine in D-xylose isomerase from Streptomyces
RT   violaceoruber. Identification by chemical derivatization and peptide
RT   mapping.";
RL   Biochem. J. 263:195-199(1989).
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:0000305};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000305};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR   SABIO-RK; P14405; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009045; F:xylose isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Magnesium; Metal-binding; Xylose metabolism.
FT   CHAIN           <1..>12
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195809"
FT   ACT_SITE        5
FT   ACT_SITE        8
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         12
SQ   SEQUENCE   12 AA;  1376 MW;  E749268EB1AAAAA1 CRC64;
     GVTFHDDDLI PF