ID XYLA_PSE14 Reviewed; 438 AA. AC Q48J73; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Xylose isomerase; DE EC=5.3.1.5; GN Name=xylA; OrderedLocusNames=PSPPH_2356; OS Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., RA Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., RA Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., RA Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., RA Mansfield J.W., Collmer A., Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. RT phaseolicola 1448A reveals divergence among pathovars in genes RT involved in virulence and transposition."; RL J. Bacteriol. 187:6488-6498(2005). 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; CP000058; AAZ36203.1; -; Genomic_DNA. DR RefSeq; YP_274557.1; -. DR GeneID; 3558817; -. DR GenomeReviews; CP000058_GR; PSPPH_2356. DR KEGG; psp:PSPPH_2356; -. DR NMPDR; fig|264730.3.peg.2447; -. DR HOGENOM; Q48J73; -. DR OMA; Q48J73; QFLIEPK. 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 1 438 Xylose isomerase. FT /FTId=PRO_0000236967. 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 438 AA; 49396 MW; FDADDF19F1C8CA04 CRC64; MPYFPAVDKV RYEGPDSDSP LAFRHYDADK LILGKPMREH LRMAACYWHT FVWPGADMFG VGTFKRPWQG SGDPLELAIG KAETAFEFFS KLGIDYYSFH DTDVAPEGSS LKEYRNNFAQ MIDQLERHQE QTGIKLLWGT ANCFSNPRFA AGAASNPDPE VFAYAATQVF SAMNATQRLK GANYVLWGGR EGYETLLNTD LRQEREQLGR FMRMVVEHKH KIGFKGDLLI EPKPQEPTKH QYDYDSATVF GFLQQYGLEK EIKVNIEANH ATLAGHSFHH EIATAVSLGI FGSIDANRGD PQNGWDTDQF PNSVEEMTLA TYEILKAGGF TNGGYNFDSK VRRQSLDEVD LFHGHVAAMD VLALALERAA AMVQNDKLQQ FKDQRYAGWQ QPFGKSLLAG EFSLESLAKH AFDKDLNPQA VSGRQELLEG VVNRFIYF //