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Database: UniProt/TrEMBL
Entry: L0EB30_THECK
LinkDB: L0EB30_THECK
Original site: L0EB30_THECK 
ID   L0EB30_THECK            Unreviewed;       437 AA.
AC   L0EB30;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00018232, 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=Theco_1313 {ECO:0000313|EMBL:AGA57478.1};
OS   Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX   NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA57478.1, ECO:0000313|Proteomes:UP000010795};
RN   [1] {ECO:0000313|Proteomes:UP000010795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18247 / JCM 13945 / KWC4
RC   {ECO:0000313|Proteomes:UP000010795};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL   Submitted (JAN-2012) 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;
CC         Evidence={ECO:0000256|HAMAP-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|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00455, 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; CP003255; AGA57478.1; -; Genomic_DNA.
DR   RefSeq; WP_015254235.1; NC_019897.1.
DR   AlphaFoldDB; L0EB30; -.
DR   STRING; 717605.Theco_1313; -.
DR   KEGG; tco:Theco_1313; -.
DR   eggNOG; COG2115; Bacteria.
DR   HOGENOM; CLU_037261_1_0_9; -.
DR   OMA; TLAMYEI; -.
DR   OrthoDB; 9763981at2; -.
DR   Proteomes; UP000010795; 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   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; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   NCBIfam; TIGR02630; xylose_isom_A; 1.
DR   PANTHER; PTHR48306; XYLOSE ISOMERASE; 1.
DR   PANTHER; PTHR48306:SF1; XYLOSE ISOMERASE; 1.
DR   Pfam; PF01261; AP_endonuc_2; 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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}; Reference proteome {ECO:0000313|Proteomes:UP000010795};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW   Rule:MF_00455}.
FT   DOMAIN          154..285
FT                   /note="Xylose isomerase-like TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         294
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         337
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   437 AA;  49298 MW;  AC23D6550553C9A3 CRC64;
     MAYFENVGKI QFEGKGSDNP FAYKHYNPQE KVLGKTMEEH LRFAVAYWHT FTGTGADPFG
     VGTAIRSWDK FDGMDRAKAR VEANFEFLEK TGIDYYCFHD VDIAPEGDTL QETHKNLDTI
     VAMLKEFQKS TGKKLLWNTA NMFTNPRYVF GAATTCNADV YAHAAAQVKK MLEVGKELGA
     ENYVFWGGRE GYETLLNTDM ALELDNLARF YHMAIEYAKE IGFNAQFLIE PKPKEPTKHQ
     YDFDAATTIA FLQKYGLKDH FKLNLEANHA TLAGHTFEHE LRVAAINDML GSIDANQGDL
     LLGWDTDEFP TDLYSVTLTM YEILKAGGFK TGGINFDAKV RRGSFEPEDL FLAHIAGVDT
     FAWGLKAAAK IIEERVLDSV IEERYASFRE GIGKEIVEGK ATLKSLEAYA LQNKPIVNRS
     GRQERIKLVL NEIIYSV
//
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