ID   XYLA_ECOL5              Reviewed;         440 AA.
AC   Q0TBN7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA; OrderedLocusNames=ECP_3668;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- CATALYTIC ACTIVITY: D-xylose = D-xylulose.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the xylose isomerase family.
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DR   EMBL; CP000247; ABG71642.1; -; Genomic_DNA.
DR   RefSeq; YP_671543.1; -.
DR   GeneID; 4188059; -.
DR   GenomeReviews; CP000247_GR; ECP_3668.
DR   KEGG; ecp:ECP_3668; -.
DR   HOGENOM; Q0TBN7; -.
DR   OMA; Q0TBN7; QFLIEPK.
DR   BioCyc; ECOL362663:ECP_3668-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0009045; F:xylose isomerase activity; IEA:HAMAP.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP.
DR   HAMAP; MF_00455; -; 1.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR012307; Xyl_isomerase-typ_TIM-brl.
DR   InterPro; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   InterPro; IPR018115; Xylose_isomerase_AS.
DR   Gene3D; G3DSA:3.20.20.150; Xyl_isomerase-like_TIM-brl; 1.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   PRINTS; PR00688; XYLOSISMRASE.
DR   TIGRFAMs; TIGR02630; xylose_isom_A; 1.
DR   PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase;
KW   Magnesium; Metal-binding; Pentose shunt; Xylose metabolism.
FT   CHAIN         1    440       Xylose isomerase.
FT                                /FTId=PRO_1000026439.
FT   ACT_SITE    101    101       By similarity.
FT   ACT_SITE    104    104       By similarity.
FT   METAL       232    232       Magnesium 1 (By similarity).
FT   METAL       268    268       Magnesium 1 (By similarity).
FT   METAL       268    268       Magnesium 2 (By similarity).
FT   METAL       271    271       Magnesium 2 (By similarity).
FT   METAL       296    296       Magnesium 1 (By similarity).
FT   METAL       307    307       Magnesium 2 (By similarity).
FT   METAL       309    309       Magnesium 2 (By similarity).
FT   METAL       339    339       Magnesium 1 (By similarity).
SQ   SEQUENCE   440 AA;  49719 MW;  6E21039B6EC0561F CRC64;
     MQAYFDQLDR VRYEGSKSSN PLAFRHYNPD ELVLGKRMEE HLRFAACYWH TFCWNGADMF
     GVGAFNRPWQ QPGEALALAK RKADVAFEFF HKLHVPFYCF HDVDVSPEGA SLKEYINNFA
     QMVDVLAGKQ EESGVKLLWG TANCFTNPRY GAGAATNPDP EVFSWAATQV VTAMEATHKL
     GGENYVLWGG REGYETLLNT DLRQEREQLG RFMQMVVEHK HKIGFQGTLL IEPKPQEPTK
     HQYDYDAATV YGFLKQFGLE KEIKLNIEAN HATLAGHSFH HEIATAIALG LFGSVDANRG
     DAQLGWDTDQ FPNSVEENAL VMYEILKAGG FTTGGLNFDA KVRRQSTDKY DLFYGHIGAM
     DTMALALKIA ARMIEDGELD KRIAQRYSGW NSELGQQILK GQMSLADLAK YAQEHNLSPV
     HQSGRQEQLE NLVNHYLFDK
//