ID   XYLA_FERGO              Reviewed;         433 AA.
AC   Q6T6K9;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455};
DE            EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455};
GN   Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455};
OS   Fervidobacterium gondwanense.
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=44754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kluskens L., Geerling A.C.M., Zeilstra J., de Vos W.M., van der Oost J. IV;
RT   "Isolation, expression and characterization of a glucose isomerase produced
RT   by the thermophilic bacterium Fervidobacterium gondwanense.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00455}.
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DR   EMBL; AY431100; AAR07504.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6T6K9; -.
DR   SMR; Q6T6K9; -.
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..433
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195778"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         334
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   433 AA;  49696 MW;  DA371167297A475C CRC64;
     MYFNVEKVVY EGPSSKNLLA YKFYNPEEEI AGKKMRDWFR FAVAYWHTFN SRGEDPFGSA
     TFERPWFKKD PMDTAFAKVD ALFEFCEKTG VEYFTFHDRD LAHEGLTLRE SNKILDKVVE
     KIKEYMKSSN VKLLWGTANL FSHPRYAQGA ATSPNPLVFS YAASQVKKML DVTKELGGLG
     YVLWGGREGY DNLLLTDSAL EEKLFARFLE MVVEYKERIG FNGVLMIEPK PKEPTKHQYD
     FDASTVLYFL KKHNLFEHFK LNIEANHATL AGHTFAHELR VARLNGKLGS IDANRGDLLL
     GWDTDQFPTD VYETTFAMYE VLENNGLDCG FNFDAKVRRA SIDPEDIVYA HVSSMDAFAL
     GLKLAVKLRE KVKPMIEERY SEYNSEIGMK ILEGKTTLDE LSSYVEDLTD VRVKSLKQEL
     LEMVINDVIF GGR