XYLA_THECA
ID XYLA_THECA Reviewed; 387 AA.
AC P56681;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Thermus caldophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=272;
RN [1]
RP CRYSTALLIZATION, AND CHARACTERIZATION.
RC STRAIN=GK24;
RX PubMed=10089429; DOI=10.1107/s0907444998009019;
RA Chang C., Song H.K., Park B.C., Lee D.-S., Suh S.W.;
RT "A thermostable xylose isomerase from Thermus caldophilus: biochemical
RT characterization, crystallization and preliminary X-ray analysis.";
RL Acta Crystallogr. D 55:294-296(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC STRAIN=GK24;
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}.
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DR PDB; 1BXC; X-ray; 2.30 A; A/B/C/D=1-387.
DR PDBsum; 1BXC; -.
DR AlphaFoldDB; P56681; -.
DR SMR; P56681; -.
DR EvolutionaryTrace; P56681; -.
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_0000195811"
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:1BXC"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 64..81
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 108..127
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 153..171
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:1BXC"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 295..321
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:1BXC"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:1BXC"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:1BXC"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:1BXC"
SQ SEQUENCE 387 AA; 43860 MW; 28FB6568BA758065 CRC64;
MYEPKPEHRF TFGLWTVGNV GRDPFGDAVR ERLDPVYVGH KLAELGVHGV NLHDEDLIPR
GTPPAERDQI VRRFKRALDE TGLKVPMVTG NLFSDPGFKD GGFTSRDPWV RAYAFRKSLE
TMDLGAELGA EIYVVWPGRE GAEVEATGKA RKVWDWVREP LNFMAAYAED QGYGYRFALE
PKPNEPRGDI YFATVGSMLA LIHTLERPER FGLNPEFAHE TMAGLNFVHA VAQALDAGKL
LHIDLNGQRM NRFDQDLRFG SENLKAAFLL VDLLESSGYQ GPRHFDAHAL RTEDEEGVWA
FARGCMRTYL ILKERAEAFR EDPEVKELLA AYYQEDPAAL PLMDPYSHEK AEALKRAELP
LEAKRHRGYA LERLDQLAVE YLLGVRG
