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Reviewed, UniProtKB/Swiss-Prot P08202 (ARAA_ECOLI)

Last modified June 15, 2010. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
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Names and originHide

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

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.
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General annotation (Comments)Hide

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. 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. Ref.6

Sequence similarities

Belongs to the arabinose isomerase family.

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OntologiesHide

Keywords
   Biological processArabinose catabolism
Carbohydrate metabolism
   LigandManganese
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processL-arabinose catabolic process to xylulose 5-phosphate

Inferred from mutant phenotype. Source: UniProtKB

   Molecular functionL-arabinose isomerase activity

Inferred from direct assay. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...
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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500L-arabinose isomerase HAMAP MF_00519
PRO_0000198385

Sites

Metal binding3061Manganese HAMAP MF_00519
Metal binding3331Manganese HAMAP MF_00519
Metal binding3501Manganese HAMAP MF_00519
Metal binding4501Manganese HAMAP MF_00519

Experimental info

Sequence conflict721R → P Ref.1
Sequence conflict721R → P Ref.2
Sequence conflict2481K → E Ref.1
Sequence conflict2481K → E Ref.2
Sequence conflict3601A → V Ref.1
Sequence conflict3601A → V Ref.2

Secondary structure

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

Details...

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SequencesHide

Sequence LengthMass (Da)Tools
P08202-1 [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

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ReferencesHide

« 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.
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Cross-referencesHide

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.
RefSeqAP_000726.1.
NP_414604.1.

3D structure databases

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

Protein-protein interaction databases

DIPDIP-9123N.
STRINGP08202.

2-D gel databases

ECO2DBASEG054.1. 6TH EDITION.

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.

Organism-specific databases

EchoBASEEB0050.
EcoGeneEG10052. araA.
CMRSearch...

Phylogenomic databases

eggNOGCOG2160.
HOGENOMHBG297198.
OMAEVCPTIA.
ProtClustDBPRK02929.

Enzyme and pathway databases

BioCycEcoCyc:ARABISOM-MONOMER.
ECOL168927:B0062-MONOMER.
MetaCyc:ARABISOM-MONOMER.
BRENDA5.3.1.4. 246.

Gene expression databases

GenevestigatorP08202.

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...
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Entry informationHide

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: June 15, 2010
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

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

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