Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8G3Q1 (XYLA_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:BL1704
OrganismBifidobacterium longum (strain NCC 2705)
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

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
Reference 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_0000195769

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
Q8G3Q1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 77FB7E971D716CC3

FASTA44950,868
        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 
MDAYAAGLLV ADKMNQDGFI QNLQAERYSS YDSGIGKDID EGNVTLADLE AYSLDKPQSE 

       430        440 
LIAATKSDHL ESVKATINNY IIDALAEVE 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN25490.1.
RefSeqNP_696854.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G3Q1.
SMRQ8G3Q1. Positions 5-449.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1021951.
GenomeReviewsGene locus BL1704 in contig AE014295_GR.
KEGGblo:BL1704.
NMPDRfig|206672.1.peg.1621.
PATRIC21120674. VBIBifLon107831_1757.

Phylogenomic databases

HOGENOMHBG297199.
OMALLGWDTD.
PhylomeDBQ8G3Q1.
ProtClustDBPRK05474.

Enzyme and pathway databases

BioCycBLON206672:BL1704-MONOMER.

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_BIFLO
AccessionPrimary (citable) accession number: Q8G3Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 52 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