ID   XYLA_STRS8              Reviewed;           9 AA.
AC   P19149;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
DE   Flags: Fragment;
GN   Name=xylA;
OS   Streptomyces sp. (strain NCL 82-5-1).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=72593;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3415697; DOI=10.1016/s0006-291x(88)81101-x;
RA   Pawar H.S., Kannan K., Srinivasan M.C., Vartak H.G.;
RT   "Purification and characterisation of glucose (xylose) isomerase from
RT   Chainia sp. (NCL 82-5-1).";
RL   Biochem. Biophys. Res. Commun. 155:411-417(1988).
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: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   PIR; A31576; A31576.
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..>9
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195806"
FT   NON_TER         9
SQ   SEQUENCE   9 AA;  983 MW;  F64BA1EDC5B87DD1 CRC64;
     RHAGSAHTF