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P12070 (XYLA_ARTS7) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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
OrganismArthrobacter sp. (strain NRRL B3728)
Taxonomic identifier1669 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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
Direct protein sequencing
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 Ref.2
Chain2 – 395394Xylose isomerase HAMAP-Rule MF_00455
PRO_0000195760

Sites

Active site541 Ref.3
Active site571 Ref.3
Metal binding1811Magnesium 1
Metal binding2171Magnesium 1
Metal binding2171Magnesium 2
Metal binding2201Magnesium 2
Metal binding2451Magnesium 1
Metal binding2551Magnesium 2
Metal binding2571Magnesium 2
Metal binding2931Magnesium 1

Secondary structure

............................................................. 395
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12070 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EA7A21FC47726369

FASTA39543,292
        10         20         30         40         50         60 
MSVQPTPADH FTFGLWTVGW TGADPFGVAT RKNLDPVEAV HKLAELGAYG ITFHDNDLIP 

        70         80         90        100        110        120 
FDATEAEREK ILGDFNQALK DTGLKVPMVT TNLFSHPVFK DGGFTSNDRS IRRFALAKVL 

       130        140        150        160        170        180 
HNIDLAAEMG AETFVMWGGR EGSEYDGSKD LAAALDRMRE GVDTAAGYIK DKGYNLRIAL 

       190        200        210        220        230        240 
EPKPNEPRGD IFLPTVGHGL AFIEQLEHGD IVGLNPETGH EQMAGLNFTH GIAQALWAEK 

       250        260        270        280        290        300 
LFHIDLNGQR GIKYDQDLVF GHGDLTSAFF TVDLLENGFP NGGPKYTGPR HFDYKPSRTD 

       310        320        330        340        350        360 
GYDGVWDSAK ANMSMYLLLK ERALAFRADP EVQEAMKTSG VFELGETTLN AGESAADLMN 

       370        380        390 
DSASFAGFDA EAAAERNFAF IRLNQLAIEH LLGSR 

« Hide

References

[1]"D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Gene cloning, sequence and expression."
Loviny-Anderton T., Shaw P.C., Shin M.K., Hartley B.S.
Biochem. J. 277:263-271(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Purification and properties."
Smith C.A., Rangarajan M., Hartley B.S.
Biochem. J. 277:255-261(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, CHARACTERIZATION.
[3]"Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift."
Collyer C.A., Henrick K., Blow D.M.
J. Mol. Biol. 212:211-235(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES HIS-54 AND ASP-57.
[4]"Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5-A and 2.3-A resolution, respectively."
Henrick K., Collyer C.A., Blow D.M.
J. Mol. Biol. 208:129-157(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[5]"Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter."
Henrick K., Blow D.M., Carell H.L., Glusker J.P.
Protein Eng. 1:467-469(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPARISON OF X-RAY STRUCTURES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59466 Genomic DNA. Translation: CAA42073.1.
PIRS16214.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DIDX-ray2.50A/B2-395[»]
1DIEX-ray2.50A/B2-395[»]
1XLAX-ray2.30A/B2-395[»]
1XLBX-ray2.50A/B2-395[»]
1XLCX-ray2.50A/B2-395[»]
1XLDX-ray2.50A/B2-395[»]
1XLEX-ray2.50A/B2-395[»]
1XLFX-ray2.50A/B2-395[»]
1XLGX-ray2.50A/B2-395[»]
1XLHX-ray2.50A/B2-395[»]
1XLIX-ray2.50A/B2-395[»]
1XLJX-ray2.50A/B2-395[»]
1XLKX-ray2.50A/B2-395[»]
1XLLX-ray2.50A/B2-395[»]
1XLMX-ray2.40A/B2-395[»]
4XIAX-ray2.30A/B3-395[»]
5XIAX-ray2.50A/B3-395[»]
ProteinModelPortalP12070.
SMRP12070. Positions 3-395.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP12070.

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

EvolutionaryTraceP12070.

Entry information

Entry nameXYLA_ARTS7
AccessionPrimary (citable) accession number: P12070
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 101 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