ID   XYLA_HORVU              Reviewed;         479 AA.
AC   Q40082; Q40081;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=XYLA;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE,
RP   AND CHARACTERIZATION.
RC   STRAIN=cv. Himalaya;
RX   MEDLINE=96203931; PubMed=8620879;
RX   DOI=10.1111/j.1432-1033.1996.0240n.x;
RA   Kristo P.A., Saarelainen R., Fagerstroem R., Aho S., Korhola M.;
RT   "Protein purification, and cloning and characterization of the cDNA
RT   and gene for xylose isomerase of barley.";
RL   Eur. J. Biochem. 237:240-246(1996).
CC   -!- CATALYTIC ACTIVITY: D-xylose = D-xylulose.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0-9.0;
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family.
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DR   EMBL; X95257; CAA64545.1; -; mRNA.
DR   EMBL; X95256; CAA64544.1; -; Genomic_DNA.
DR   PIR; S65466; S65466.
DR   HSSP; P45687; 1A0E.
DR   Gramene; Q40082; -.
DR   BRENDA; 5.3.1.5; 283.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009045; F:xylose isomerase activity; IEA:EC.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Isomerase;
KW   Magnesium; Manganese; Metal-binding; Pentose shunt; Xylose metabolism.
FT   CHAIN         1    479       Xylose isomerase.
FT                                /FTId=PRO_0000195825.
FT   ACT_SITE    144    144       By similarity.
FT   METAL       275    275       Manganese 1 (By similarity).
FT   METAL       311    311       Manganese 1 (By similarity).
FT   METAL       311    311       Manganese 2 (By similarity).
FT   METAL       314    314       Manganese 2 (By similarity).
FT   METAL       339    339       Manganese 1 (By similarity).
FT   METAL       350    350       Manganese 2 (By similarity).
FT   METAL       352    352       Manganese 2 (By similarity).
FT   METAL       382    382       Manganese 1 (By similarity).
FT   CONFLICT    443    468       AGKGDFETLEKKALEWGEPTVPSGKQ -> GSSSFTAQCKY
FT                                ISAPMIVPYDLLLPA (in Ref. 1; CAA64544).
SQ   SEQUENCE   479 AA;  53614 MW;  57E6033AFD77A33F CRC64;
     MKGGELLVLL LASSLCLSAA VAAQETCPAD IGAKCTDAAS DDWEGEFFPG IDKINYEGPT
     SKKPLSYKWY NAEEVILGKK MKDWFRFSVA FWHTFRGTGG DPFGAPTKNW PWEDGTNSLA
     MAKRRMKAHF EFMEKLGVER WCFHDRDIAP DGKTLAETNA NLDEIVELAK QLQSETNIKP
     LWGTAQLFMH PRYMHGAATS PEVKVYAYAA AQVKKALEVT HYLGGENYVF WGGREGYQTL
     LNTDMKRELE HLANFLQAAV NHKKKIGFNG TLLIEPKPQE PTKHQYDWDV ATTFSFLQKF
     GLTGEFKINV ECNHATLSGH SCHHELETAR INDILGNIDA NTGDPQVGWD TDEFLTDISE
     ATLIMSSVVK NDGLAPGGFN FYAKLRREST DVEDLFIAHI SGMDTMARGR RNVVKLIEDG
     SLDELVRKRY QSFDTEIGAM IEAGKGDFET LEKKALEWGE PTVPSGKQEL AEMLFQSAL
//