ID   XYLA_LEVBR              Reviewed;         449 AA.
AC   P29443;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455, ECO:0000303|PubMed:1587475};
DE            EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455};
GN   Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455, ECO:0000303|PubMed:1587475};
OS   Levilactobacillus brevis (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=1580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-26.
RX   PubMed=1587475; DOI=10.1016/0378-1119(92)90718-5;
RA   Bor Y.-C., Moraes C., Lee S.-P., Crosby W.L., Sinskey A.J., Batt C.A.;
RT   "Cloning and sequencing the Lactobacillus brevis gene encoding xylose
RT   isomerase.";
RL   Gene 114:127-131(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=9835554; DOI=10.1128/aem.64.12.4720-4728.1998;
RA   Chaillou S., Bor Y.-C., Batt C.A., Postma P.W., Pouwels P.H.;
RT   "Molecular cloning and functional expression in Lactobacillus plantarum 80
RT   of xylT, encoding the D-xylose-H+ symporter of Lactobacillus brevis.";
RL   Appl. Environ. Microbiol. 64:4720-4728(1998).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00455};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00455};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00455};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00455}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00455}.
CC   -!- INDUCTION: By D-xylose. {ECO:0000269|PubMed:9835554}.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00455}.
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DR   EMBL; M84564; AAA25256.1; -; Genomic_DNA.
DR   EMBL; AF045552; AAC95125.1; -; Genomic_DNA.
DR   PIR; JC1137; JC1137.
DR   AlphaFoldDB; P29443; -.
DR   SMR; P29443; -.
DR   SABIO-RK; P29443; -.
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; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
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; Direct protein sequencing; Isomerase;
KW   Magnesium; Metal-binding; Xylose metabolism.
FT   CHAIN           1..449
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195781"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         342
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   449 AA;  50757 MW;  37170CFB5C435E4E CRC64;
     MTEEYWKGVD KIQYVGHQDK KSGLGFQYYN PEEEIMGKKM KDWLRFAVAY WHTFDQRLVD
     PFGDGTAQRP YDKYTDPMDL ALAKVDAAFE FYQKLGVDYL CFHDRDLAPE GDTLRETNAN
     LDKVVDKIVE YQKTSGMKVL WNTSNMFTNP RFVEGAATSP YADVFAYSAA QLKHSLEIGK
     RVGSENYVFW GGREGYESLW NTNMKQEQEH AAKIFHMAKD YANEIGFDAQ MLLEPKPKEP
     TTHQYDFDAA TTIAFMKEYD LDKDFKLNLE GNHANLAGHT YQHEIRVARE AGLLGSLDAN
     QGDKLIGWDI DEYPSNLYET TAAMYEVVEN GSIGPRGGLN FDAKPRRSAF APEDLFLGHI
     VGMDSFAAGL RVAAAMKQDG FLDNLKADRY SSYKSGVGAD IESGKADLKS LEAYAIDKPQ
     SELIAATHSD HLEEIKDTIN HYIIDTLSK