Skip Header

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

P08202 (ARAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-arabinose isomerase
EC=5.3.1.4
Gene names
Name:araA
Ordered Locus Names:b0062, JW0061
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

L-arabinose = L-ribulose. HAMAP MF_00519

Cofactor

Binds 1 manganese ion per subunit.

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. Ref.6

Sequence similarities

Belongs to the arabinose isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500L-arabinose isomerase HAMAP MF_00519
PRO_0000198385

Sites

Metal binding3061Manganese
Metal binding3331Manganese
Metal binding3501Manganese
Metal binding4501Manganese

Experimental info

Sequence conflict721R → P in AAA23463. Ref.1
Sequence conflict2481K → E in AAA23463. Ref.1
Sequence conflict3601A → V in AAA23463. Ref.1

Secondary structure

1 .............................................................................................................. 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08202 [UniParc].

Last modified June 27, 2006. Version 3.
Checksum: E427A145A3455D36

FASTA50056,074
        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 
PATQIHGKKR 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

« Hide 'large scale' references
[1]"The organization of the araBAD operon of Escherichia coli."
Lee N., Gielow W., Martin R., Hamilton E., Fowler A.
Gene 47:231-244(1986) [PubMed: 3549454] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 72; 248 AND 360.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]Bachellier S., Saurin W., Perrin D., Hofnung M., Gilson E.
Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 458-500.
[6]"Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production."
Manjasetty B.A., Chance M.R.
J. Mol. Biol. 360:297-309(2006) [PubMed: 16756997] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
[7]"Crystal structure of Mn2+-bound Escherichia coli L-arabinose isomerase (ECAI) and implications in protein catalytic mechanism and thermo-stability."
Zhu W., Chance M.R., Manjasetty B.A.
Submitted (OCT-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M15263 Genomic DNA. Translation: AAA23463.1.
U00096 Genomic DNA. Translation: AAC73173.1.
AP009048 Genomic DNA. Translation: BAB96631.2.
X74279 Genomic DNA. Translation: CAA52340.1.
PIRISECAB. F64727.
RefSeqNP_414604.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AJTX-ray2.60A/B/C1-500[»]
2HXGX-ray2.80A/B/C1-500[»]
ProteinModelPortalP08202.
SMRP08202. Positions 1-498.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9123N.
IntActP08202. 4 interactions.

2D gel databases

ECO2DBASEG054.1. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000002886; EBESCP00000002886; EBESCG00000002354.
EBESCT00000018166; EBESCP00000017457; EBESCG00000017221.
GeneID947511.
GenomeReviewsGene locus JW0061 in contig AP009048_GR.
Gene locus b0062 in contig U00096_GR.
KEGGecj:JW0061.
eco:b0062.
PATRIC32115225. VBIEscCol129921_0064.

Organism-specific databases

EchoBASEEB0050.
EcoGeneEG10052. araA.

Phylogenomic databases

eggNOGCOG2160.
GeneTreeEBGT00050000011273.
HOGENOMHBG297198.
OMAEVCPTIA.
PhylomeDBP08202.
ProtClustDBPRK02929.

Enzyme and pathway databases

BioCycEcoCyc:ARABISOM-MONOMER.
MetaCyc:ARABISOM-MONOMER.
BRENDA5.3.1.4. 2026.

Gene expression databases

GenevestigatorP08202.

Family and domain databases

HAMAPMF_00519. Arabinose_Isome.
[Tree]
InterProIPR024664. Ara_Isoase_C.
IPR004216. Fuc/Ara_isomerase_C.
IPR009015. Fucose_isomerase_N/cen.
IPR003762. Lara_isomerase.
[Graphical view]
KOK01804.
PfamPF11762. Arabinose_Iso_C. 1 hit.
PF02610. 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]
SUPFAMSSF50443. Fuc_isomerase_C. 1 hit.
SSF53743. Fuc_isomerase_N. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARAA_ECOLI
AccessionPrimary (citable) accession number: P08202
Secondary accession number(s): P78040
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 27, 2006
Last modified: January 25, 2012
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents