ID   XYLA_THESA              Reviewed;         439 AA.
AC   P30435;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA;
OS   Thermoanaerobacterium saccharolyticum.
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX   NCBI_TaxID=28896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49915 / DSM 7060 / B6A-RI;
RX   PubMed=8360616; DOI=10.1099/00221287-139-6-1227;
RA   Lee Y.-E., Ramesh M.V., Zeikus J.G.;
RT   "Cloning, sequencing and biochemical characterization of xylose isomerase
RT   from Thermoanaerobacterium saccharolyticum strain B6A-RI.";
RL   J. Gen. Microbiol. 139:1227-1234(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-7, AND SUBUNIT.
RC   STRAIN=ATCC 49915 / DSM 7060 / B6A-RI;
RX   PubMed=1996956; DOI=10.1042/bj2730565;
RA   Lee C.Y., Zeikus J.G.;
RT   "Purification and characterization of thermostable glucose isomerase from
RT   Clostridium thermosulfurogenes and Thermoanaerobacter strain B6A.";
RL   Biochem. J. 273:565-571(1991).
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:0000269|PubMed:1996956}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR   EMBL; L09699; AAA03088.1; -; mRNA.
DR   PIR; S17976; S17976.
DR   AlphaFoldDB; P30435; -.
DR   SMR; P30435; -.
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; Direct protein sequencing; Isomerase;
KW   Magnesium; Metal-binding; Xylose metabolism.
FT   CHAIN           1..439
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195815"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
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         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  50477 MW;  9ABD20005EBF6C0A CRC64;
     MNKYFENVSK IKYEGPKSNN PYSFKFYNPE EVIDGKTMEE HLRFSIAYWH TFTADGTDQF
     GKATMQRPWN HYTDPMDIAK RRVEAAFEFF DKINAPFFCF HDRDIAPEGD TLRETNKNLD
     TIVAMIKDYL KTSKTKVLWG TANLFSNPRF VHGASTSCNA DVFAYSAAQV KKALEITKEL
     GRENYVFWGG REGYETLLNT DMELELDNFA RFLHMAVDYA KEIGFEGQFL IEPKPKEPTK
     HQYDFDVANV LAFLRKYDLD KYFKVNIEAN HATLAFHDFQ HELRYARING VLGSIDANTG
     DMLLGWDTDQ FPTDIRMTTL AMYEVIKMGG FDKGGLNFDA KVRRASFEPE DLFLGHIAGM
     DAFAKGFKVA YKLVKDGVFD KFIEERYASY KEGIGADIVS GKADFKSLEK YALEHSQIVN
     KSGRQELLES ILNQYLFAE