ID   XYLA_BACSH              Reviewed;         445 AA.
AC   E0TVS5; P04788; P94491;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA; OrderedLocusNames=BSUW23_09025;
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=6096130; DOI=10.1002/j.1460-2075.1984.tb02173.x;
RA   Wilhelm M., Hollenberg C.P.;
RT   "Selective cloning of Bacillus subtilis xylose isomerase and xylulokinase
RT   in Escherichia coli genes by IS5-mediated expression.";
RL   EMBO J. 3:2555-2560(1984).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR   EMBL; CP002183; ADM37851.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0TVS5; -.
DR   SMR; E0TVS5; -.
DR   EnsemblBacteria; ADM37851; ADM37851; BSUW23_09025.
DR   KEGG; bss:BSUW23_09025; -.
DR   HOGENOM; CLU_037261_1_0_9; -.
DR   OMA; TLAMYEI; -.
DR   Proteomes; UP000002233; Chromosome.
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..445
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000403666"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  50295 MW;  F965E52CC02311D1 CRC64;
     MAQSHSSSVN YFGSVNKVVF EGKASTNPLA FKYYNPQEVI GGKTMKEHLR FSIAYWHTFT
     ADGTDVFGAA TMQRPWDHYK GMDLARARVE AAFEMFEKLD APFFAFHDRD IAPEGSTLKE
     TNQNLDIIVG MIKDYMRDSN VKLLWNTANM FTNPRFVHGA ATSCNADVFA YAAAQVKKGL
     ETAKELGAEN YVFWGGREGY ETLLNTDLKF ELDNLARFMH MAVDYAKEIE YTGQFLIEPK
     PKEPTTHQYD TDAATTIAFL KQYGLDNHFK LNLEANHATL AGHTFEHELR MARVHGLLGS
     VDANQGHPLL GWDTDEFPTD LYSTTLAMYE ILQNGGLGSG GLNFDAKVRR SSFEPDDLVY
     AHIAGMDAFA RGLKVAHKLI EDRVFEDVIQ HRYRSFTEGI GLEITEGRAN FHTLEQYALN
     NKTIKNESGR QERLKAILNQ YILEV