XYLA_THETC
ID XYLA_THETC Reviewed; 439 AA.
AC P29441; D9TTQ8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA; OrderedLocusNames=Tthe_2492;
OS Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS thermosaccharolyticum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX NCBI_TaxID=580327;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC 00135 / 2032;
RX PubMed=8163183; DOI=10.1016/0378-1119(94)90134-1;
RA Meaden P.G., Aduse-Opoku J., Reizer J., Reizer A., Lanceman Y.A.,
RA Martin M.F., Mitchell W.J.;
RT "The xylose isomerase-encoding gene (xylA) of Clostridium
RT thermosaccharolyticum: cloning, sequencing and phylogeny of XylA enzymes.";
RL Gene 141:97-101(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC 00135 / 2032;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT 571.";
RL Submitted (AUG-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 -!- 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}.
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DR EMBL; M91248; AAA79035.1; -; Genomic_DNA.
DR EMBL; CP002171; ADL69948.1; -; Genomic_DNA.
DR PIR; I40806; I40806.
DR RefSeq; WP_013298905.1; NC_014410.1.
DR AlphaFoldDB; P29441; -.
DR SMR; P29441; -.
DR STRING; 580327.Tthe_2492; -.
DR EnsemblBacteria; ADL69948; ADL69948; Tthe_2492.
DR KEGG; ttm:Tthe_2492; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_9; -.
DR OMA; TLAMYEI; -.
DR OrthoDB; 481478at2; -.
DR Proteomes; UP000001626; 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..439
FT /note="Xylose isomerase"
FT /id="PRO_0000195773"
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"
FT CONFLICT 263
FT /note="F -> L (in Ref. 1; AAA79035)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..378
FT /note="GV -> AE (in Ref. 1; AAA79035)"
FT /evidence="ECO:0000305"
FT CONFLICT 420..433
FT /note="NKSGRQEMLESILN -> TNQVDKKCLNQYSI (in Ref. 1;
FT AAA79035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 50184 MW; 983515ED3EC5FEEB CRC64;
MSKYFEKVSK IKYEGPKSNN PYAFKFYNPE EVIDGKTMEE HLRFSIAYWH TFTADGTDQF
GKATMQRPWN HLTDPMDIAK ARVEAAFEFF DKINAPFFCF HDRDIAPEGD TLRETNKNLD
IIVAMIKDYL KTSKTKVLWG TANLFSNPRF VHGASTSCNA DVFAYSAAQV KKALEITKEL
GGQNYVFWGG REGYETLLNT DMELELDNFA RFLHMAVDYA KEIGFEGQFL IEPKPKEPTK
HQYDFDVANV LAFLRKYDLD KYFKVNIEAN HATLAAHDFQ HELRYARING VLGSIDANTG
DMLLGWDTDQ FPTDIRMTTL AMYEVIKMGG FDKGGLNFDA KVRRASFEPE DLFLGHIAGM
DAFAKGFKVA YKLVKDGVFD KFIEERYASY KDGIGADIVS GKADFKSLEK YALEHSEIVN
KSGRQEMLES ILNQYLFTE
