ID   E1TFK5_BURSG            Unreviewed;       440 AA.
AC   E1TFK5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|HAMAP-Rule:MF_00455};
DE            EC=5.3.1.5 {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|HAMAP-Rule:MF_00455};
GN   Name=xylA {ECO:0000256|HAMAP-Rule:MF_00455};
GN   OrderedLocusNames=BC1003_4427 {ECO:0000313|EMBL:ADN60359.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN60359.1};
RN   [1] {ECO:0000313|EMBL:ADN60359.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN60359.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) 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:0000256|ARBA:ARBA00033659, ECO:0000256|HAMAP-
CC         Rule:MF_00455, ECO:0000256|RuleBase:RU000609};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00455};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00455};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00455,
CC       ECO:0000256|RuleBase:RU000610}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00455,
CC       ECO:0000256|RuleBase:RU000610}.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|HAMAP-Rule:MF_00455,
CC       ECO:0000256|RuleBase:RU000609}.
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DR   EMBL; CP002218; ADN60359.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1TFK5; -.
DR   STRING; 640512.BC1003_4427; -.
DR   KEGG; bgf:BC1003_4427; -.
DR   eggNOG; COG2115; Bacteria.
DR   HOGENOM; CLU_037261_1_0_4; -.
DR   OrthoDB; 9763981at2; -.
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   Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
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   NCBIfam; TIGR02630; xylose_isom_A; 1.
DR   PANTHER; PTHR48320; -; 1.
DR   PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 1.
DR   PRINTS; PR00688; XYLOSISMRASE.
DR   SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR   PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00455}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00455};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00455};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00455};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00455};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW   Rule:MF_00455}.
FT   ACT_SITE        100
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         338
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   440 AA;  49831 MW;  DFB53EA91024B787 CRC64;
     MSYFEHIPEI RYEGPQSDNP LAYRHYDKSK KVLGKTLEEH LRIAVCYWHT FVWPGVDIFG
     QGTFRRPWQQ PGDAMEMAHL KADAAFEFFS KLGTPYYTFH DTDVAPEGTN LHEYSENFSR
     IVDYLERKQH DTGVKLLWGT ANLFSHPRYA AGAATSPDPE IFAYAATQVR HALDATQRLG
     GENYVLWGGR EGYDTLLNTD LVRERDQLAR FLHMVVEHAH KIGFKGALLI EPKPQEPTKH
     QYDYDVATVH GFLLQYGLEK EIRVNIEANH ATLAGHSFHH EIATAYALGV FGSVDANRGD
     PQNGWDTDQF PNSVEELTLA FYEILRHGGF TTGGMNFDSK VRRQSVDAED LFHGHIGAID
     NLALALERAA VLIGNDRLGE FRRQRYAGWD ADFGRKILSG DYSLSTLAAE AVSRDLNPQH
     KSGQQERMEN IVNQAIYSGR
//