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P24300 (XYLA_STRRU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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 rubiginosus
Taxonomic identifier1929 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length388 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.

Caution

According to the crystallographic study residue 40 could be Gln.

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 – 388387Xylose isomerase HAMAP-Rule MF_00455
PRO_0000195805

Sites

Active site541
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

................................................................. 388
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24300 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 4C675184B62C97FB

FASTA38843,227
        10         20         30         40         50         60 
MNYQPTPEDR FTFGLWTVGW QGRDPFGDAT RRALDPVESV RRLAELGAHG VTFHDDDLIP 

        70         80         90        100        110        120 
FGSSDSEREE HVKRFRQALD DTGMKVPMAT TNLFTHPVFK DGGFTANDRD VRRYALRKTI 

       130        140        150        160        170        180 
RNIDLAVELG AETYVAWGGR EGAESGGAKD VRDALDRMKE AFDLLGEYVT SQGYDIRFAI 

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

       250        260        270        280        290        300 
LFHIDLNGQN GIKYDQDLRF GAGDLRAAFW LVDLLESAGY SGPRHFDFKP PRTEDFDGVW 

       310        320        330        340        350        360 
ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAR PTAADGLQAL LDDRSAFEEF 

       370        380 
DVDAAAARGM AFERLDQLAM DHLLGARG 

« Hide

References

[1]"Genetic organization and regulation of the xylose degradation genes in Streptomyces rubiginosus."
Wong H.C., Ting Y., Lin H.C., Reichert F., Myambo K., Watt K.W., Toy P.L., Drummond R.J.
J. Bacteriol. 173:6849-6858(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator."
Carrell H.L., Glusker J.P., Burger V., Manfre F., Tritsch D., Biellmann J.-F.
Proc. Natl. Acad. Sci. U.S.A. 86:4440-4444(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[3]"A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 A Streptomyces rubiginosus structures with xylitol and D-xylose."
Whitlow M., Howard A.J., Finzel B.C., Poulos T.L., Winborne E., Gilliland G.L.
Proteins 9:153-173(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73789 Genomic DNA. Translation: AAA26838.1.
PIRB41339.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GW9X-ray1.55A1-387[»]
1MNZX-ray0.99A1-388[»]
1O1HX-ray1.40A/B2-388[»]
1OADX-ray1.50A/B2-388[»]
1XIBX-ray1.60A1-388[»]
1XICX-ray1.60A1-388[»]
1XIDX-ray1.70A1-388[»]
1XIEX-ray1.70A1-388[»]
1XIFX-ray1.60A1-388[»]
1XIGX-ray1.70A1-388[»]
1XIHX-ray1.70A1-388[»]
1XIIX-ray1.70A1-388[»]
1XIJX-ray1.70A1-388[»]
1XISX-ray1.60A2-388[»]
2G4JX-ray1.85A2-388[»]
2GLKX-ray0.94A1-388[»]
2GUBX-ray1.80A1-388[»]
2GVEneutron diffraction2.20A1-388[»]
2XISX-ray1.71A2-388[»]
3CWHneutron diffraction2.20A1-388[»]
3GNXX-ray2.00A/E2-388[»]
3KBJX-ray2.00A1-388[»]
3KBMX-ray2.00A1-388[»]
3KBNX-ray1.53A1-388[»]
3KBSX-ray1.80A1-388[»]
3KBVX-ray1.80A1-388[»]
3KBWX-ray1.60A1-388[»]
3KCJOther1.80A1-388[»]
3KCLOther2.00A1-388[»]
3KCOOther1.80A1-388[»]
3N4AX-ray1.94A2-388[»]
3QYSX-ray1.85A1-388[»]
3QZAOther2.00A1-388[»]
3U3HX-ray0.97A1-388[»]
3XISX-ray1.60A2-388[»]
4A8IX-ray0.95A1-388[»]
4A8LX-ray1.35A1-388[»]
4A8NX-ray1.20A1-388[»]
4A8RX-ray1.42A1-388[»]
4DUOX-ray2.00A1-388[»]
4DVOOther2.00A1-388[»]
4E3VX-ray1.50A1-388[»]
4J4KX-ray1.90A1-388[»]
4LNCOther2.19A1-388[»]
4XISX-ray1.60A2-388[»]
8XIAX-ray1.90A1-388[»]
9XIAX-ray1.90A1-388[»]
ProteinModelPortalP24300.
SMRP24300. Positions 1-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-58982N.

Chemistry

DrugBankDB00126. Vitamin C.

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

EvolutionaryTraceP24300.

Entry information

Entry nameXYLA_STRRU
AccessionPrimary (citable) accession number: P24300
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 107 of the entry and version 4 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