XYLA_THET8
ID XYLA_THET8 Reviewed; 387 AA.
AC P26997;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2022613; DOI=10.1128/jb.173.10.3078-3083.1991;
RA Dekker K., Yamagata H., Sakaguchi K., Udaka S.;
RT "Xylose (glucose) isomerase gene from the thermophile Thermus thermophilus:
RT cloning, sequencing, and comparison with other thermostable xylose
RT isomerases.";
RL J. Bacteriol. 173:3078-3083(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=10329168; DOI=10.1006/jmbi.1999.2696;
RA Chang C., Park B.C., Lee D.-S., Suh S.W.;
RT "Crystal structures of thermostable xylose isomerases from Thermus
RT caldophilus and Thermus thermophilus: possible structural determinants of
RT thermostability.";
RL J. Mol. Biol. 288:623-634(1999).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D90256; BAA14301.1; -; Genomic_DNA.
DR RefSeq; WP_014677651.1; NC_017767.1.
DR RefSeq; YP_006250271.1; NC_017767.1.
DR PDB; 1BXB; X-ray; 2.20 A; A/B/C/D=1-387.
DR PDBsum; 1BXB; -.
DR AlphaFoldDB; P26997; -.
DR SMR; P26997; -.
DR BRENDA; 5.3.1.5; 2305.
DR SABIO-RK; P26997; -.
DR EvolutionaryTrace; P26997; -.
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; IPR013453; XylA_actinobac.
DR InterPro; IPR001998; Xylose_isomerase.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR02631; xylA_Arthro; 1.
DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium;
KW Metal-binding; Xylose metabolism.
FT CHAIN 1..387
FT /note="Xylose isomerase"
FT /id="PRO_0000195816"
FT ACT_SITE 53
FT /evidence="ECO:0000250"
FT ACT_SITE 56
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 108..128
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 153..171
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 295..320
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:1BXB"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 349..356
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:1BXB"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:1BXB"
SQ SEQUENCE 387 AA; 43907 MW; B2ED05466E4C88CE CRC64;
MYEPKPEHRF TFGLWTVGNV GRDPFGDAVR ERLDPVYVVH KLAELGAYGV NLHDEDLIPR
GTPPQERDQI VRRFKKALDE TGLKVPMVTA NLFSDPAFKD GAFTSPDPWV RAYALRKSLE
TMDLGAELGA EIYVVWPGRE GAEVEATGKA RKVWDWVREA LNFMAAYAED QGYGYRFALE
PKPNEPRGDI YFATVGSMLA FIHTLDRPER FGLNPEFAHE TMAGLNFVHA VAQALDAGKL
FHIDLNDQRM SRFDQDLRFG SENLKAAFFL VDLLESSGYQ GPRHFDAHAL RTEDEEGVWA
FARGCMRTYL ILKERAEAFR EDPEVKELLA AYYQEDPAAL ALLGPYSREK AEALKRAELP
LEAKRRRGYA LERLDQLAVE YLLGVRG
