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Reviewed, UniProtKB/Swiss-Prot A7ZHF3 (ARAA_ECO24)

Last modified November 3, 2009. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-arabinose isomerase
    EC=5.3.1.4
Gene names
Name: araA
Ordered Locus Names: EcE24377A_0064
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of L-arabinose to L-ribulose By similarity.

Catalytic activity

L-arabinose = L-ribulose. HAMAP MF_00519

Cofactor

Binds 1 manganese ion per subunit By similarity.

Pathway

Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. HAMAP MF_00519

Subunit structure

Homohexamer By similarity.

Sequence similarities

Belongs to the arabinose isomerase family.

Ontologies

Keywords
   Biological processArabinose catabolism
Carbohydrate metabolism
   LigandManganese
Metal-binding
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarabinose catabolic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionL-arabinose isomerase activity

Inferred from electronic annotation. Source: HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500L-arabinose isomerase HAMAP MF_00519
PRO_1000060912

Sites

Metal binding3061Manganese By similarity
Metal binding3331Manganese By similarity
Metal binding3501Manganese By similarity
Metal binding4501Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZHF3-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: E1B1B9F2FACF1FBD

FASTA50056,103
        10         20         30         40         50         60 
MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTTPDEI 

        70         80         90        100        110        120 
TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF 

       130        140        150        160        170        180 
MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR 

       190        200        210        220        230        240 
FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT 

       250        260        270        280        290        300 
PATQIHGEKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG 

       310        320        330        340        350        360 
YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV 

       370        380        390        400        410        420 
EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP 

       430        440        450        460        470        480 
KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT 

       490        500 
RLPAFKDALR WNEVYYGFRR 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000800 Genomic DNA. Translation: ABV17108.1.
RefSeqYP_001461232.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZHF3.

Genome annotation databases

GeneID5586876.
GenomeReviewsGene locus EcE24377A_0064 in contig CP000800_GR.
KEGGecw:EcE24377A_0064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAEVCPTIA.

Family and domain databases

HAMAPMF_00519.
[Tree]
InterProIPR003762. Lara_isomerase.
[Graphical view]
PfamPF02610. Arabinose_Isome. 1 hit.
[Graphical view]
PIRSFPIRSF001478. L-ara_isomerase. 1 hit.
ProDomPD018364. Lara_isomerase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameARAA_ECO24
AccessionPrimary (citable) accession number: A7ZHF3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: November 3, 2009
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents