XYLA_THEP3
ID XYLA_THEP3 Reviewed; 438 AA.
AC P22842; B0K7B8;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA; OrderedLocusNames=Teth39_2060;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1368665; DOI=10.1271/bbb1961.55.221;
RA Dekker K., Yamagata H., Sakaguchi K., Udaka S.;
RT "Xylose (glucose) isomerase gene from the thermophile Clostridium
RT thermohydrosulfuricum; cloning, sequencing, and expression in Escherichia
RT coli.";
RL Agric. Biol. Chem. 55:221-227(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9495747; DOI=10.1128/jb.180.5.1103-1109.1998;
RA Erbeznik M., Dawson K.A., Strobel H.J.;
RT "Cloning and characterization of transcription of the xylAB operon in
RT Thermoanaerobacter ethanolicus.";
RL J. Bacteriol. 180:1103-1109(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) 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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC46145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABY95684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D00756; BAA00652.1; -; Genomic_DNA.
DR EMBL; AF001974; AAC46145.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000924; ABY95684.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_013570854.1; NC_010321.1.
DR AlphaFoldDB; P22842; -.
DR SMR; P22842; -.
DR STRING; 340099.Teth39_2060; -.
DR EnsemblBacteria; ABY95684; ABY95684; Teth39_2060.
DR KEGG; tpd:Teth39_2060; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_9; -.
DR OMA; TLAMYEI; -.
DR Proteomes; UP000002156; 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 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 Reference proteome; Xylose metabolism.
FT CHAIN 1..438
FT /note="Xylose isomerase"
FT /id="PRO_0000195812"
FT ACT_SITE 100
FT /evidence="ECO:0000250"
FT ACT_SITE 103
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 438 AA; 50158 MW; 4B3B0BC1B7413DE7 CRC64;
MEYFKNVPQI KYEGPKSNNP YAFKFYNPDE IIDGKPLKEH LRFSVAYWHT FTANGTDPFG
APTMQRPWDH FTDPMDIAKA RVEAAFELFE KLDVPFFCFH DRDIAPEGET LRETNKNLDT
IVAMIKDYLK TSKTKVLWGT ANLFSNPRFV HGAATSCNAD VFAYAAAQVK KALEITKELG
GQNYVFWGGR EGYETLLNTD MELELDNLAR FLHMAVEYAQ EIGFEGQFLI EPKPKEPTKH
QYDFDAASVH AFLKKYDLDK YFKLNIEANH ATLAGHDFQH ELRYARINNM LGSIDANMGD
MLLGWDTDQY PTDIRMTTLA MYEVIKMGGF NKGGLNFDAK VRRASFEPED LFLGHIAGMD
AFAKGFKVAY KLVKDGVFDR FIEERYKSYR EGIGAEIVSG KANFKTLEEY ALNNPKIENK
SGKQELLESI LNQYLFSE
