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B3DR33 (XYLA_BIFLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Ordered Locus Names:BLD_1871
OrganismBifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]
Taxonomic identifier205913 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00455

Subcellular location

Cytoplasm By similarity 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 termComplete proteome
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 – 449449Xylose isomerase HAMAP-Rule MF_00455
PRO_1000200278

Sites

Active site1011 By similarity
Active site1041 By similarity
Metal binding2321Magnesium 1 By similarity
Metal binding2681Magnesium 1 By similarity
Metal binding2681Magnesium 2 By similarity
Metal binding2711Magnesium 2 By similarity
Metal binding2961Magnesium 1 By similarity
Metal binding3071Magnesium 2 By similarity
Metal binding3091Magnesium 2 By similarity
Metal binding3401Magnesium 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
B3DR33 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 01BA6BD5C6C13937

FASTA44950,918
        10         20         30         40         50         60 
MGLWDVDKIE YVGRAKGPKE DFAFHYYDAD KVVAGKKMKD WLRFGVAWWH TFNQELVDPF 

        70         80         90        100        110        120 
GTGTAHRPYY KYTDPMDQAL AKVDYAFELF QKLGVEYFCF HDRDIAPEGD TLRETNANLD 

       130        140        150        160        170        180 
KVVDKIEENM KSTGVKLLWN TSSLFTNPRF VSGAATSPFA DIYAYAGGQL KKSLEIGKRL 

       190        200        210        220        230        240 
GAENYVFWGG REGYENLWNT EMKRETDHIA KFFHMCADYA KEIGFEAQFL IEPKPKEPTL 

       250        260        270        280        290        300 
HQYDFDAATA IEFLRNHDLT DVFKLNLEGN HANLAGHTYQ HEIRVARESG FLGSLDANQG 

       310        320        330        340        350        360 
DKLIGWDMDE FPTDLYETVA VMWEVLQAGS IGPHGGLNFD AKPRRTSFYE EDLFRSHIAG 

       370        380        390        400        410        420 
MDTYAAGLLV ADKMNQDGFI QDLMAERYSS YDSGIGKDID EGNVTLADLE AYSLDKPQSE 

       430        440 
LIAATKSDHL ESVKATINNY IIDALSEVE 

« Hide

References

[1]"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth."
Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J.
BMC Genomics 9:247-247(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DJO10A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000605 Genomic DNA. Translation: ACD99316.1.
RefSeqYP_001955814.1. NC_010816.1.

3D structure databases

ProteinModelPortalB3DR33.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205913.BLD_1871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD99316; ACD99316; BLD_1871.
GeneID6364470.
KEGGblj:BLD_1871.
PATRIC21116792. VBIBifLon134794_1894.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2115.
HOGENOMHOG000252293.
KOK01805.
OMALFHAHIG.
OrthoDBEOG62NX4R.

Enzyme and pathway databases

BioCycBLON205913:GJB4-1939-MONOMER.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00455. Xylose_isom_A.
InterProIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013452. Xylose_isom_bac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSPR00688. XYLOSISMRASE.
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR02630. xylose_isom_A. 1 hit.
PROSITEPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYLA_BIFLD
AccessionPrimary (citable) accession number: B3DR33
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: May 14, 2014
This is version 40 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