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P26997 (XYLA_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xylose isomerase

EC=5.3.1.5
Gene names
Name:xylA
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-xylopyranose = D-xylulose. HAMAP-Rule MF_00455

Cofactor

Binds 2 magnesium ions per subunit By similarity. HAMAP-Rule MF_00455

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00455.

Sequence similarities

Belongs to the xylose isomerase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Pentose shunt
Xylose metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processD-xylose metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

xylose isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Xylose isomerase HAMAP-Rule MF_00455
PRO_0000195816

Sites

Active site531 By similarity
Active site561 By similarity
Metal binding1801Magnesium 1 By similarity
Metal binding2161Magnesium 1 By similarity
Metal binding2161Magnesium 2 By similarity
Metal binding2191Magnesium 2 By similarity
Metal binding2441Magnesium 1 By similarity
Metal binding2541Magnesium 2 By similarity
Metal binding2561Magnesium 2 By similarity
Metal binding2861Magnesium 1 By similarity

Secondary structure

.............................................................. 387
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26997 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: B2ED05466E4C88CE

FASTA38743,907
        10         20         30         40         50         60 
MYEPKPEHRF TFGLWTVGNV GRDPFGDAVR ERLDPVYVVH KLAELGAYGV NLHDEDLIPR 

        70         80         90        100        110        120 
GTPPQERDQI VRRFKKALDE TGLKVPMVTA NLFSDPAFKD GAFTSPDPWV RAYALRKSLE 

       130        140        150        160        170        180 
TMDLGAELGA EIYVVWPGRE GAEVEATGKA RKVWDWVREA LNFMAAYAED QGYGYRFALE 

       190        200        210        220        230        240 
PKPNEPRGDI YFATVGSMLA FIHTLDRPER FGLNPEFAHE TMAGLNFVHA VAQALDAGKL 

       250        260        270        280        290        300 
FHIDLNDQRM SRFDQDLRFG SENLKAAFFL VDLLESSGYQ GPRHFDAHAL RTEDEEGVWA 

       310        320        330        340        350        360 
FARGCMRTYL ILKERAEAFR EDPEVKELLA AYYQEDPAAL ALLGPYSREK AEALKRAELP 

       370        380 
LEAKRRRGYA LERLDQLAVE YLLGVRG 

« Hide

References

[1]"Xylose (glucose) isomerase gene from the thermophile Thermus thermophilus: cloning, sequencing, and comparison with other thermostable xylose isomerases."
Dekker K., Yamagata H., Sakaguchi K., Udaka S.
J. Bacteriol. 173:3078-3083(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Crystal structures of thermostable xylose isomerases from Thermus caldophilus and Thermus thermophilus: possible structural determinants of thermostability."
Chang C., Park B.C., Lee D.-S., Suh S.W.
J. Mol. Biol. 288:623-634(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90256 Genomic DNA. Translation: BAA14301.1.
RefSeqYP_006250271.1. NC_017767.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXBX-ray2.20A/B/C/D1-387[»]
ProteinModelPortalP26997.
SMRP26997. Positions 1-387.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP26997.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00455. Xylose_isom_A.
InterProIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSPR00688. XYLOSISMRASE.
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR02631. xylA_Arthro. 1 hit.
PROSITEPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26997.

Entry information

Entry nameXYLA_THET8
AccessionPrimary (citable) accession number: P26997
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references