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araA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

AraA

Synonyms

L-arabinose isomerase[1], B0062[2][1], AraA[2][1], L-arabinose ketol-isomerase[2][1]

Product description

L-arabinose isomerase[2][3];

Component of ; L-arabinose isomerase[2][3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0008733

L-arabinose isomerase activity

GO_REF:0000002
GO_REF:0000003
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR003762
EC:5.3.1.4
HAMAP:MF_00519

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0008733

L-arabinose isomerase activity

PMID:8869631[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0019569

L-arabinose catabolic process to xylulose 5-phosphate

PMID:17619876[6]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0005737

cytoplasm

C

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0016052

carbohydrate catabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0019568

arabinose catabolic process

PMID:13829634[7]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0008733

L-arabinose isomerase activity

PMID:13829634[7]

IMP: Inferred from Mutant Phenotype

F

complete

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Interactions

Partner TypePartnerNotesReferences

Protein

Subunits of L-arabinose isomerase

could be indirect


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Notes

Localization

CompartmentDescriptionEvidenceNotes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc 

MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTTPDEI
TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF
MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR
FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT
PATQIHGKKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAA
EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP
KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT
RLPAFKDALR WNEVYYGFRR
Mol. Wt

56.07 kDa (calc) [2]

pI

6.27[2]

Extinction coefficient

76890 - 77765 (calc based on 11 Y, 11 W, and 7 C residues)

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Domains/Motifs/Modification Sites

TypeResiduesDescriptionNotes
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Structure

Structures
  • Representative Escherichia coli structure:
    2AJT|A
    1-500 of 500 residues (E-value: 7.3e-277) (Percent Identity: 99.40)
  • View all other structures.
Models

View models at:

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Notes

Gene Product Resources

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Resource typeSourceNotes/Reference
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Notes

Accessions in Other Databases

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DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:ARABISOM-MONOMER

UniProt (EcoliWiki Page)

UniProt:P08202

PFAM (EcoliWiki Page)

PFAM:PF02610

RefSeq (EcoliWiki Page)

RefSeq:NP_414604

ModBase (EcoliWiki Page)

ModBase:P08202


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Notes

Links

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NameURLComments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 4.0 4.1 4.2 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. ↑ Banerjee S et al. (1995) The evolution of sugar isomerases. Protein Eng 8: 1189-95 PubMed EcoliWiki page
  6. ↑ De Muynck C et al. (2007) Development of a selection system for the detection of L-ribose isomerase expressing mutants of Escherichia coli. Appl Microbiol Biotechnol 76: 1051-7 PubMed EcoliWiki page
  7. ↑ 7.0 7.1 GROSS J & ENGLESBERG E (1959) Determination of the order of mutational sites governing L-arabinose utilization in Escherichia coli B/r bv transduction with phage Plbt. Virology 9: 314-31 PubMed EcoliWiki page


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