XYLA_THENE
ID XYLA_THENE Reviewed; 444 AA.
AC P45687;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Thermotoga neapolitana.
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=2337;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 5068 / LA4;
RX PubMed=7646024; DOI=10.1128/aem.61.5.1867-1875.1995;
RA Vieille C., Hess J.M.J., Kelly R.M., Zeikus J.G.J.;
RT "xylA cloning and sequencing and biochemical characterization of xylose
RT isomerase from Thermotoga neapolitana.";
RL Appl. Environ. Microbiol. 61:1867-1875(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RC STRAIN=DSM 5068 / LA4;
RA Gallay O., Chopra R., Conti E., Brick P., Jackson R., Hartley B.,
RA Vieille C., Zeikus J.G., Blow D.;
RL Submitted (NOV-1997) to the PDB data bank.
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=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Note=Binds 2 cobalt ions per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.1.;
CC Temperature dependence:
CC Optimum temperature is above 95 degrees Celsius. Extremely
CC thermostable.;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR EMBL; L38994; AAB06798.1; -; Genomic_DNA.
DR PDB; 1A0E; X-ray; 2.70 A; A/D=2-444.
DR PDBsum; 1A0E; -.
DR AlphaFoldDB; P45687; -.
DR SMR; P45687; -.
DR BRENDA; 5.3.1.5; 6332.
DR EvolutionaryTrace; P45687; -.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cobalt; Cytoplasm; Isomerase;
KW Metal-binding; Xylose metabolism.
FT CHAIN 1..444
FT /note="Xylose isomerase"
FT /id="PRO_0000195814"
FT ACT_SITE 101
FT ACT_SITE 104
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 268
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 268
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 271
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 296
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 307
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 309
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 339
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 75..93
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 160..179
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 202..222
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:1A0E"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 349..376
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 393..400
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:1A0E"
FT HELIX 425..441
FT /evidence="ECO:0007829|PDB:1A0E"
SQ SEQUENCE 444 AA; 50893 MW; 21F606C4D5F68D0B CRC64;
MAEFFPEIPK VQFEGKESTN PLAFKFYDPE EIIDGKPLKD HLKFSVAFWH TFVNEGRDPF
GDPTADRPWN RYTDPMDKAF ARVDALFEFC EKLNIEYFCF HDRDIAPEGK TLRETNKILD
KVVERIKERM KDSNVKLLWG TANLFSHPRY MHGAATTCSA DVFAYAAAQV KKALEITKEL
GGEGYVFWGG REGYETLLNT DLGFELENLA RFLRMAVDYA KRIGFTGQFL IEPKPKEPTK
HQYDFDVATA YAFLKSHGLD EYFKFNIEAN HATLAGHTFQ HELRMARILG KLGSIDANQG
DLLLGWDTDQ FPTNVYDTTL AMYEVIKAGG FTKGGLNFDA KVRRASYKVE DLFIGHIAGM
DTFALGFKVA YKLVKDGVLD KFIEEKYRSF REGIGRDIVE GKVDFEKLEE YIIDKETIEL
PSGKQEYLES LINSYIVKTI LELR
