ID   XYLA_XANC5              Reviewed;         445 AA.
AC   Q3BMF2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=xylA1 {ECO:0000255|HAMAP-Rule:MF_00455};
GN   OrderedLocusNames=XCV1808, XCV4330;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ26061.1; -; Genomic_DNA.
DR   EMBL; AM039952; CAJ23485.1; -; Genomic_DNA.
DR   RefSeq; WP_011347136.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BMF2; -.
DR   SMR; Q3BMF2; -.
DR   STRING; 456327.BJD11_13480; -.
DR   GeneID; 79907321; -.
DR   KEGG; xcv:XCV1808; -.
DR   KEGG; xcv:XCV4330; -.
DR   eggNOG; COG2115; Bacteria.
DR   HOGENOM; CLU_037261_1_0_6; -.
DR   Proteomes; UP000007069; 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..445
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000236977"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         347
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   445 AA;  48791 MW;  4249F0C771C88ECD CRC64;
     MSNTVYIGAK EYFPGIGKIG FEGRDSDNPL AFKVYDANKT IGDKTMAEHL RFAVAYWHSF
     CGNGADPFGP GTRAYPWDAG TTALNRAEAK ADAAFEFFTK LGVPYYCFHD IDLAPDADDI
     GEYEKNLKHM VGIAKQRQAD TGIKLLWGTA NLFSHPRYMN GASTNPDFNV VARAAVQVKA
     AIDATVELGG ENYVFWGGRE GYACLHNTQM KREQDNMARF LTLARDYGRA IGFKGNFLIE
     PKPMEPMKHQ YDFDSATVIG FLRQHGLDQD FKLNIEANHA TLSGHSFEHD LQVASDAGLL
     GSIDANRGNP QNGWDTDQFP TDLYDTVGAM LVVLRQGGLA PGGLNFDAKV RRESSDPQDL
     FLAHIGGMDA FARGLEVANA LLTASPLEQW RAERYASFDS GAGADFAAGK TTLADLAKHA
     ASNAPQQLSG RQEAYENLIN QYLTR
//