ID   XYLA_BURTA              Reviewed;         440 AA.
AC   Q2SW40;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA; OrderedLocusNames=BTH_I2338;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000086; ABC39030.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_442859.2; -.
DR   GeneID; 3848180; -.
DR   GenomeReviews; CP000086_GR; BTH_I2338.
DR   KEGG; bte:BTH_I2338; -.
DR   TIGR; BTH_I2338; -.
DR   HOGENOM; Q2SW40; -.
DR   BioCyc; BTHA271848:BTH_I2338-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_0000236960.
FT   ACT_SITE    100    100       By similarity.
FT   ACT_SITE    103    103       By similarity.
FT   METAL       231    231       Magnesium 1 (By similarity).
FT   METAL       267    267       Magnesium 1 (By similarity).
FT   METAL       267    267       Magnesium 2 (By similarity).
FT   METAL       270    270       Magnesium 2 (By similarity).
FT   METAL       295    295       Magnesium 1 (By similarity).
FT   METAL       306    306       Magnesium 2 (By similarity).
FT   METAL       308    308       Magnesium 2 (By similarity).
FT   METAL       338    338       Magnesium 1 (By similarity).
SQ   SEQUENCE   440 AA;  49424 MW;  B5D02E609DD74C54 CRC64;
     MSYFEHIPAI RYEGPQSDNP LAYRHYDRTK RVLGKTLEEH LRIAVCYWHT FVWPGQDVFG
     QGALRRPWQQ PGEPLERARQ KADAAFAFFT KLGTPFYTFH DTDVAPEGAN LHEYVENFAR
     MVDYLGEHQQ ASGVRLLWGT ANLFSHPRFA AGAATSPNPD AFAWAATQVC HALDATHRLG
     GENYVLWGGR EGYETLLNTD LAREREQLAR FLAMVVEHKH RIGFTGALLI EPKPQEPTKH
     QYDYDVATVH GLLTQYGLQN EIRVNIEANH ATLAGHSFHH EIANAFALGV FGSVDANRGD
     PQNGWDTDQF PNSVEELTLA FYEILRHGGF TTGGMNFDAK VRRQSVDPED LFHGHIGAID
     VLALALERAA VLVENDRLDA LRRRRYAQWD SEFGRKILAG GYSLQSLAAD ALARGVNPQH
     ASGAQERLEN IVNQAIYALR
//