ID   XYLA_YERPS              Reviewed;         439 AA.
AC   Q663Y3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455};
DE            EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455};
GN   Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455};
GN   OrderedLocusNames=YPTB3891;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00455};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00455};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00455};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00455}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00455}.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00455}.
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DR   EMBL; BX936398; CAH23129.1; -; Genomic_DNA.
DR   RefSeq; WP_002209593.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q663Y3; -.
DR   SMR; Q663Y3; -.
DR   GeneID; 66843688; -.
DR   KEGG; ypo:BZ17_2690; -.
DR   KEGG; yps:YPTB3891; -.
DR   PATRIC; fig|273123.14.peg.2821; -.
DR   Proteomes; UP000001011; 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; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   NCBIfam; TIGR02630; xylose_isom_A; 1.
DR   PANTHER; PTHR48320; -; 1.
DR   PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 1.
DR   PRINTS; PR00688; XYLOSISMRASE.
DR   SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR   PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW   Xylose metabolism.
FT   CHAIN           1..439
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000236981"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   439 AA;  49550 MW;  AC04F2193088D5C2 CRC64;
     MQSYFNELEQ VRYEGSQSTN PLAFHHYNPD EMILGKRMAD HLRFAACYWH TFCWGGADMF
     GANAFDRPWQ QPGDALALAK RKAEVAFEFF HKLNVPYYCF HDVDVSPEGA SLQEYLNNFA
     VMTDVLAEKQ AASGVKLLWG TANCFTHPRY GAGAATNPDP EVFSWAATQV FTAMNATRQL
     GGENYVLWGG REGYETLLNT DLRQEREQIG RFMQMVVEHK HKTGFQGTLL IEPKPQEPTK
     HQYDYDVATV YGFLKQFGLE KEIKVNIEAN HATLAGHSFH HEIASAIALG IFGSVDANRG
     DPQLGWDTDQ FPNSVEENTL VMFEILKAGG FTTGGLNFDA KVRRQSTDKY DLFYGHIGAM
     DTMALALKFA AKMIEDGQLD QIVAKRYAGW NSELGQQILQ GKMSLEELSR YASQHNLNPQ
     HQSGHQELLE NKVNRYLFG
//