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B3DR33 (XYLA_BIFLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-xylose = D-xylulose. HAMAP MF_00455

Cofactor

Binds 2 magnesium ions per subunit By similarity. HAMAP MF_00455

Subunit structure

Homotetramer By similarity. HAMAP MF_00455

Subcellular location

Cytoplasm By similarity HAMAP 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-KW

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

xylose isomerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Xylose isomerase HAMAP 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: 18505588] [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...

Protein-protein interaction databases

STRINGB3DR33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6364470.
GenomeReviewsGene locus BLD_1871 in contig CP000605_GR.
KEGGblj:BLD_1871.
PATRIC21116792. VBIBifLon134794_1894.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG297199.
OMALLGWDTD.
ProtClustDBPRK05474.

Family and domain databases

HAMAPMF_00455. Xylose_isom_A.
[Tree]
InterProIPR013022. Xyl_isomerase-like_TIM-brl.
IPR012307. Xyl_isomerase_TIM-brl.
IPR013452. Xylose_isom_bac.
IPR001998. Xylose_isomerase.
[Graphical view]
Gene3DG3DSA:3.20.20.150. Xyl_isomerase-like_TIM-brl. 1 hit.
KOK01805.
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSPR00688. XYLOSISMRASE.
SUPFAMSSF51658. Xyl_isomerase-like_TIM-brl. 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: January 25, 2012
This is version 26 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

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