ID   XYLA_PHOLL              Reviewed;         439 AA.
AC   Q7N4P7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=plu2275;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01) (Photorhabdus luminescens subsp. laumondii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571866; CAE14568.1; -; Genomic_DNA.
DR   RefSeq; WP_011146524.1; NC_005126.1.
DR   AlphaFoldDB; Q7N4P7; -.
DR   SMR; Q7N4P7; -.
DR   STRING; 243265.plu2275; -.
DR   GeneID; 24166365; -.
DR   KEGG; plu:plu2275; -.
DR   eggNOG; COG2115; Bacteria.
DR   HOGENOM; CLU_037261_1_0_6; -.
DR   OrthoDB; 9763981at2; -.
DR   Proteomes; UP000002514; 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   Reference proteome; Xylose metabolism.
FT   CHAIN           1..439
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195785"
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;  49984 MW;  C850623FD48E4BE5 CRC64;
     MHRYFERVNR ISYEGRQSNN PLAFRHYNPE EIILGKKMKD HLRFAVCYWH NFCWDGTDMF
     GSGAFERFWQ KGGDALELAK LKADVAFEFF YKLNIPFYCF HDIDVAPEGC SLKEYIYNLG
     VMSDILADKQ AETGVKLLWG TANCFTHPRY AAGASTNPDL NIFAYASAQV CQVMQMTKKL
     GGENYVLWGG REGYESLLNT DLRQEREQIG RFMQMVVDYK YKIGFQGTLL IEPKPQEPTK
     HQYDYDVATV YGFLKQFGLE NEIKVNIEAN HATLAGHSFQ HEVATAIALG ILGSIDANRG
     DAQLGWDTDQ FPNSVEENSL VMYEILKAGG FTTGGLNFDA KVRRQSIDID DLFYGHIGAI
     DTMALSLKSA VKILVDGKLD EYVAQRYSGW NSELGRDILE GKMTLDEVAH YAETLVQEPK
     HRSGQQELLE NLINRYIYD
//