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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

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

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]

L-Arabinose isomerase; first step in arabinose catabolism; converts L-arabinose to L-ribulose[4]

EC number (for enzymes)

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 [5]

complete

GO:0008733

L-arabinose isomerase activity

PMID:8869631[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0019569

L-arabinose catabolic process to xylulose 5-phosphate

PMID:17619876[7]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc [8]

complete

GO:0005737

cytoplasm

C

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0005975

carbohydrate metabolic process

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0119

P

Seeded from EcoCyc [8]

complete

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003762

P

Seeded from EcoCyc [8]

complete

GO:0016853

isomerase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0413

F

Seeded from EcoCyc [8]

complete

GO:0030145

manganese ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0464

F

Seeded from EcoCyc [8]

complete

GO:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc [8]

complete

GO:0016052

carbohydrate catabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0019568

arabinose catabolic process

PMID:13829634[9]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0008733

L-arabinose isomerase activity

PMID:13829634[9]

IMP: Inferred from Mutant Phenotype

F

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner TypePartnerNotesReferencesEvidence

Protein

Subunits of L-arabinose isomerase

could be indirect

Protein

napC

PMID:16606699[10]

Experiment(s):EBI-1135472

Protein

aceE

PMID:16606699[10]

Experiment(s):EBI-1135472

Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

CompartmentDescriptionEvidenceSourceNotes

Notes

Structure and Physical Properties

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Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

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
Length

500

Mol. Wt

56.073 kDa

pI

6.6 (calculated)

Extinction coefficient

76,890 - 77,765 (calc based on 11 Y, 11 W, and 7 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

TypeResiduesDescriptionNotesReferences


Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures
Models

View models at:

Structure figures

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource typeSourceNotes/Reference

Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:ARABISOM-MONOMER

UniProt (EcoliWiki Page)

UniProt:P08202

PFAM (EcoliWiki Page)

PFAM:PF02610

RefSeq (EcoliWiki Page)

RefSeq:NP_414604


Notes

Links

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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 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. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  6. Banerjee S et al. (1995) The evolution of sugar isomerases. Protein Eng 8: 1189-95 PubMed EcoliWiki page
  7. 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
  8. 8.0 8.1 8.2 8.3 8.4 8.5 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  9. 9.0 9.1 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
  10. 10.0 10.1 Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page

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