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Reviewed, UniProtKB/Swiss-Prot Q32K31 (ARAA_SHIDS)

Last modified January 19, 2010. Version 29. 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: SDY_0089
OrganismShigella dysenteriae serotype 1 (strain Sd197) [Complete proteome] [HAMAP]
Taxonomic identifier300267 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of L-arabinose to L-ribulose By similarity. HAMAP MF_00519

Catalytic activity

L-arabinose = L-ribulose. HAMAP MF_00519

Cofactor

Binds 1 manganese ion per subunit By similarity. HAMAP MF_00519

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. HAMAP MF_00519

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_0000259344

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q32K31-1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 18077C85A9335FDA

FASTA50056,105
        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 REFSFIGARM 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 MLEVCPSIAA 

       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]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000034 Genomic DNA. Translation: ABB60326.1.
RefSeqYP_401815.1.

3D structure databases

SMRQ32K31. Positions 1-498.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ32K31.

Genome annotation databases

GeneID3799449.
GenomeReviewsGene locus SDY_0089 in contig CP000034_GR.
KEGGsdy:SDY_0089.
NMPDRfig|216598.1.peg.1775.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2160.
HOGENOMHBG297198.
OMAEVCPTIA.
PhylomeDBQ32K31.

Enzyme and pathway databases

BioCycSDYS300267:SDY_0089-MONOMER.

Family and domain databases

HAMAPMF_00519. Arabinose_Isome.
[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_SHIDS
AccessionPrimary (citable) accession number: Q32K31
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 6, 2005
Last modified: January 19, 2010
This is version 29 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