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   03-AUG-2022, entry version 105.
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; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RC   STRAIN=cv. Himalaya;
RX   PubMed=8620879; 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 and
RT   gene for xylose isomerase of barley.";
RL   Eur. J. Biochem. 237:240-246(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-xylose = alpha-D-xylulofuranose; Xref=Rhea:RHEA:22816,
CC         ChEBI:CHEBI:28518, ChEBI:CHEBI:188998; EC=5.3.1.5;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=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. {ECO:0000305}.
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DR   EMBL; X95257; CAA64545.1; -; mRNA.
DR   EMBL; X95256; CAA64544.1; -; Genomic_DNA.
DR   PIR; S65466; S65466.
DR   AlphaFoldDB; Q40082; -.
DR   SMR; Q40082; -.
DR   ExpressionAtlas; Q40082; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009045; F:xylose isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00455; Xylose_isom_A; 1.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   PRINTS; PR00688; XYLOSISMRASE.
DR   SUPFAM; SSF51658; SSF51658; 1.
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; Magnesium;
KW   Manganese; Metal-binding; Xylose metabolism.
FT   CHAIN           1..479
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195825"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         382
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        443..468
FT                   /note="AGKGDFETLEKKALEWGEPTVPSGKQ -> GSSSFTAQCKYISAPMIVPYDL
FT                   LLPA (in Ref. 1; CAA64544)"
FT                   /evidence="ECO:0000305"
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