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P15587 (XYLA_STROL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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
OrganismStreptomyces olivochromogenes
Taxonomic identifier1963 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in D-xylose catabolism. HAMAP-Rule MF_00455

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

Initiator methionine11Removed HAMAP-Rule MF_00455
Chain2 – 387386Xylose isomerase HAMAP-Rule MF_00455
PRO_0000195803

Sites

Active site541 By similarity
Active site571 By similarity
Metal binding1811Magnesium 1
Metal binding2171Magnesium 1
Metal binding2171Magnesium 2
Metal binding2201Magnesium 2
Metal binding2451Magnesium 1
Metal binding2551Magnesium 2
Metal binding2571Magnesium 2
Metal binding2871Magnesium 1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P15587 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 83CCE206015B178D

FASTA38742,923
        10         20         30         40         50         60 
MSYQPTPEDR FTFGLWTVGW QGRDPFGDAT RPALDPVETV QRLAELGAHG VTFHDDDLIP 

        70         80         90        100        110        120 
FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK DGGFTANDRD VRRYALRKTI 

       130        140        150        160        170        180 
RNIDLAVELG AKTYVAWGGR EGAESGAAKD VRVALDRMKE AFDLLGEYVT SQGYDTRFAI 

       190        200        210        220        230        240 
EPKPNEPRGD ILLPTVGHAL AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK 

       250        260        270        280        290        300 
LFHIDLNGQS GIKYDQDLRF GAGDLRAAFW LVDLLESAGY EGPRHFDFKP PRTEDIDGVW 

       310        320        330        340        350        360 
ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAQ PTAADGVQEL LADRTAFEDF 

       370        380 
DVDAAAARGM AFERLDQLAM DHLLGAR 

« Hide

References

[1]"X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis."
Lavie A., Allen K., Petsko G.A., Ringe D.
Biochemistry 33:5469-5480(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS).
[2]"Crystallographic studies of the mechanism of xylose isomerase."
Farber G.K., Glasfeld A., Tiraby G., Ringe D., Petsko G.A.
Biochemistry 28:7289-7297(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[3]"The 3.0 A crystal structure of xylose isomerase from Streptomyces olivochromogenes."
Farber G.K., Petsko G.A., Ringe D.
Protein Eng. 1:459-466(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRS28986.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MUWX-ray0.86A2-387[»]
1S5MX-ray0.98A2-387[»]
1S5NX-ray0.95A2-387[»]
1XYAX-ray1.81A/B2-387[»]
1XYBX-ray1.96A/B2-387[»]
1XYCX-ray2.19A/B2-387[»]
1XYLX-ray1.80A/B2-387[»]
1XYMX-ray1.80A/B2-387[»]
2GYIX-ray1.60A/B2-387[»]
ProteinModelPortalP15587.
SMRP15587. Positions 2-387.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

EvolutionaryTraceP15587.

Entry information

Entry nameXYLA_STROL
AccessionPrimary (citable) accession number: P15587
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 99 of the entry and version 3 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