ID   XYLA_LACPE              Reviewed;         449 AA.
AC   P21938;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA;
OS   Lactiplantibacillus pentosus (Lactobacillus pentosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MD353;
RX   PubMed=1660563; DOI=10.1007/bf00290664;
RA   Lokman B.C., van Santen P., Verdoes J.C., Kruese J., Leer R.J., Posno M.,
RA   Pouwels P.H.;
RT   "Organization and characterization of three genes involved in D-xylose
RT   catabolism in Lactobacillus pentosus.";
RL   Mol. Gen. Genet. 230:161-169(1991).
CC   -!- FUNCTION: Involved in D-xylose catabolism.
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; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR   EMBL; M57384; AAA25258.1; -; Genomic_DNA.
DR   PIR; S18561; S18561.
DR   AlphaFoldDB; P21938; -.
DR   SMR; P21938; -.
DR   STRING; 1589.GCA_001188985_00558; -.
DR   PRIDE; P21938; -.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW   Xylose metabolism.
FT   CHAIN           1..449
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195783"
FT   ACT_SITE        103
FT   ACT_SITE        106
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  50705 MW;  A3FF82EB7B34C872 CRC64;
     MTNEYWQGVD QIKYIGHQDK KSGLGFQYYN PDEVIGGKKM RDWLRFSVAY WHTFDQRLVD
     PFGDGTAQRP YDHITDPMDL ALAKVDAAFE FYHKLGVDYL CFHDRDLAPE GDTLRETNRN
     LDKVIDKIVD YQKQTGMKVL WNTSNMFTNP RFVAGAATSP DADVFAYAAA QLKHSLEIGK
     RVGAENYVFW GGREGYESLW NTNMKLEQEH AAKFFHMAKD YANEIGFDAQ MLLEPKPKEP
     STHQYDFDAA TTIAFMKEYD LDKDFKLNLE GNHANLAGHT YQHEIRVARE ANLLGSLDAN
     QGDKLIGWDI DEFPSDLYEA TAAMYEVVEN GSIGPRGGLN FDAKPRRSSF AANDLFYGHI
     VGIDTFAAGL RVALKMKQDG FLEKLVADRY SSYQSGVGAE IEAGTADFKS LESYAIDKPQ
     SELIAATSSD PLEEVKDTIN HYIIETLSK