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Q0TBN7 (XYLA_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. 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:ECP_3668
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-xylose = 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: HAMAP

pentose-phosphate shunt

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: HAMAP

xylose isomerase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Xylose isomerase HAMAP-Rule MF_00455
PRO_1000026439

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 binding3391Magnesium 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0TBN7 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 6E21039B6EC0561F

FASTA44049,719
        10         20         30         40         50         60 
MQAYFDQLDR VRYEGSKSSN PLAFRHYNPD ELVLGKRMEE HLRFAACYWH TFCWNGADMF 

        70         80         90        100        110        120 
GVGAFNRPWQ QPGEALALAK RKADVAFEFF HKLHVPFYCF HDVDVSPEGA SLKEYINNFA 

       130        140        150        160        170        180 
QMVDVLAGKQ EESGVKLLWG TANCFTNPRY GAGAATNPDP EVFSWAATQV VTAMEATHKL 

       190        200        210        220        230        240 
GGENYVLWGG REGYETLLNT DLRQEREQLG RFMQMVVEHK HKIGFQGTLL IEPKPQEPTK 

       250        260        270        280        290        300 
HQYDYDAATV YGFLKQFGLE KEIKLNIEAN HATLAGHSFH HEIATAIALG LFGSVDANRG 

       310        320        330        340        350        360 
DAQLGWDTDQ FPNSVEENAL VMYEILKAGG FTTGGLNFDA KVRRQSTDKY DLFYGHIGAM 

       370        380        390        400        410        420 
DTMALALKIA ARMIEDGELD KRIAQRYSGW NSELGQQILK GQMSLADLAK YAQEHNLSPV 

       430        440 
HQSGRQEQLE NLVNHYLFDK 

« Hide

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000247 Genomic DNA. Translation: ABG71642.1.
RefSeqYP_671543.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0TBN7.
SMRQ0TBN7. Positions 2-439.
ModBaseSearch...

Protein-protein interaction databases

STRING362663.ECP_3668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG71642; ABG71642; ECP_3668.
GeneID4188059.
KEGGecp:ECP_3668.
PATRIC18198215. VBIEscCol77757_3717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2115.
HOGENOMHOG000252293.
KOK01805.
OMAHTFQHEL.
PhylomeDBQ0TBN7.
ProtClustDBPRK05474.

Enzyme and pathway databases

BioCycECOL362663:GIY5-3697-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. 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_ECOL5
AccessionPrimary (citable) accession number: Q0TBN7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: May 1, 2013
This is version 49 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