ID XYLA_STROI Reviewed; 388 AA. AC Q93RJ9; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 06-FEB-2007, entry version 25. DE Xylose isomerase (EC 5.3.1.5). GN Name=xylA; OS Streptomyces olivaceoviridis (Streptomyces corchorusii). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1921; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kaneko T.; RT "Streptomyces olivaceoviridis D-xylose isomerase (xylA) gene."; RL Submitted (FEB-2000) 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB038265; BAB62014.1; -; Genomic_DNA. DR PIR; JC7663; JC7663. DR HSSP; P15587; 1XYA. DR SMR; Q93RJ9; 2-387. DR GO; GO:0000287; F:magnesium ion binding; 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; IPR013453; XylA_actinobac. DR InterPro; IPR012307; Xylisom_TIMbarrl. DR InterPro; IPR001998; Xylose_isom. DR Pfam; PF01261; AP_endonuc_2; 1. DR PRINTS; PR00688; XYLOSISMRASE. DR TIGRFAMs; TIGR02631; xylA_Arthro; 1. DR PROSITE; PS00172; XYLOSE_ISOMERASE_1; 1. DR PROSITE; PS00173; XYLOSE_ISOMERASE_2; 1. KW Carbohydrate metabolism; Isomerase; Magnesium; Metal-binding; KW Pentose shunt; Xylose metabolism. FT CHAIN 1 388 Xylose isomerase. FT /FTId=PRO_0000195802. FT ACT_SITE 54 54 By similarity. FT ACT_SITE 57 57 By similarity. FT METAL 181 181 Magnesium 1 (By similarity). FT METAL 217 217 Magnesium 1 (By similarity). FT METAL 217 217 Magnesium 2 (By similarity). FT METAL 220 220 Magnesium 2 (By similarity). FT METAL 245 245 Magnesium 1 (By similarity). FT METAL 255 255 Magnesium 2 (By similarity). FT METAL 257 257 Magnesium 2 (By similarity). FT METAL 287 287 Magnesium 1 (By similarity). SQ SEQUENCE 388 AA; 42993 MW; C13A578836CD996C CRC64; MSYQPTPEDR FTFGLWTVGW QGRDPFGDAT RRALDPVETV QRLAELGAHG VTFHDDDLIP FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK DGAFTANDRD VRRYALRKTI RNIDLAAELG AKTYVAWGGR EGAESGAAKD VRSALDRMKE AFDLLGEYVT SQGYVLRFAI EPKPNEPRGD ILLPTVGHAL AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQS GIKYDQDLRF GAGDLRSALW MVDLLESAGY EGPRHFDFKP PRTEDLDGVW ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDQLAQ PTAADGLEDL LADRAAFEDF DVEAAAARGM AFERLDQLAM DHLLGARG //