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B1LJC7 (XYLA_ECOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:EcSMS35_3888
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length440 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 – 440440Xylose isomerase HAMAP MF_00455
PRO_1000200290

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
B1LJC7 [UniParc].

Last modified April 29, 2008. 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]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed: 18708504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SMS-3-5 / SECEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000970 Genomic DNA. Translation: ACB17239.1.
RefSeqYP_001745853.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LJC7.
SMRB1LJC7. Positions 2-439.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1LJC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000063538; EBESCP00000061180; EBESCG00000062585.
GeneID6145005.
GenomeReviewsGene locus EcSMS35_3888 in contig CP000970_GR.
KEGGecm:EcSMS35_3888.
PATRIC18436695. VBIEscCol6161_4030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011705.
HOGENOMHBG297199.
OMALLGWDTD.
ProtClustDBPRK05474.

Enzyme and pathway databases

BioCycECOL439855:ECSMS35_3888-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_ECOSM
AccessionPrimary (citable) accession number: B1LJC7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 31 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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