ID   XYLA_LACBR              Reviewed;         449 AA.
AC   P29443;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA;
OS   Lactobacillus brevis.
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92267372; 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].
RA   Bor Y.-C., Batt C.A.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: D-xylose = D-xylulose.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the xylose isomerase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M84564; AAA25256.1; -; Genomic_DNA.
DR   EMBL; AF045552; AAC95125.1; -; Genomic_DNA.
DR   PIR; JC1137; JC1137.
DR   HSSP; P19148; 1A0C.
DR   BRENDA; 5.3.1.5; 1167.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0009045; F:xylose isomerase activity; IEA:HAMAP.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP.
DR   HAMAP; MF_00455; -; 1.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR012307; Xyl_isomerase-typ_TIM-brl.
DR   InterPro; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   InterPro; IPR018115; Xylose_isomerase_AS.
DR   Gene3D; G3DSA:3.20.20.150; Xyl_isomerase-like_TIM-brl; 1.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   PRINTS; PR00688; XYLOSISMRASE.
DR   TIGRFAMs; TIGR02630; xylose_isom_A; 1.
DR   PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium;
KW   Metal-binding; Pentose shunt; Xylose metabolism.
FT   CHAIN         1    449       Xylose isomerase.
FT                                /FTId=PRO_0000195781.
FT   ACT_SITE    103    103       By similarity.
FT   ACT_SITE    106    106       By similarity.
FT   METAL       234    234       Magnesium 1 (By similarity).
FT   METAL       270    270       Magnesium 1 (By similarity).
FT   METAL       270    270       Magnesium 2 (By similarity).
FT   METAL       273    273       Magnesium 2 (By similarity).
FT   METAL       298    298       Magnesium 1 (By similarity).
FT   METAL       309    309       Magnesium 2 (By similarity).
FT   METAL       311    311       Magnesium 2 (By similarity).
FT   METAL       342    342       Magnesium 1 (By similarity).
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
//