ID   XYLA_BACSW              Reviewed;         441 AA.
AC   P54272;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA;
OS   Bacillus sp. (strain LW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=72576;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=7663444;
RA   Liao W.X., Earnest L., Kok S.L., Jeyaseelan K.;
RT   "Molecular cloning and characterization of the xylose isomerase gene from a
RT   thermophilic Bacillus species.";
RL   Biochem. Mol. Biol. Int. 36:401-410(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Jeyaseelan K., Liao W.X., Earnest L., Kok S.L.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exhibits xylose isomerase activity.
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 magnesium ions per subunit.;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius. Active from 60 to 100
CC         degrees Celsius.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR   EMBL; L12967; AAA99461.1; -; Genomic_DNA.
DR   EMBL; L42008; AAB46621.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54272; -.
DR   SMR; P54272; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009045; F:xylose isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule.
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; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW   Xylose metabolism.
FT   CHAIN           1..441
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195765"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   441 AA;  50170 MW;  6B19B3BE2919D017 CRC64;
     MPYFDNISTI AYEGPASKNP LAFKFYNPEE KVGDKTMEEH LRFSVAYWHT FTGDGSDPFG
     AGNMIRPWNK YSGMDLAKAR VEAAFEFFEK LNIPFFCFHD VDIAPEGETL KETYKNLDII
     VDMIEEYMKT SKTKLLWNTA NLFTHPRFVH GAATSCNADV FAYAAAKVKK GLEIAKRLGA
     ENYVFWGGRE GYETLLNTDM KLELDNLARF LHMAVDYAKE IGFDGQFLIE PKPKEPTKHQ
     YDFDVATALA FLQTYGLKDY FKFNIEANHA TLAGHTFEHE LRVARIHGML GSVDANQGDM
     LLGWDTDEFP TDLYSTTLAM YEILKNGGLG RGGLNFDAKV RRGSFEPEDL FYAHIAGMDS
     FAVGLKVAHR LIEDRVFDEF IEERYKSYTE GIGREIVEGT VDFHKLEAHA LQLGEIQNQS
     GRQERLKTLL NQYLLEVCAA R