iaaA: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

IaaA

Synonyms

L-asparaginase[1], B0828[2][1], Spt[2][1], YbiK[2][1] , ECK0818, JW0812, spt, ybiK, b0828

Product description

IaaA[2][3];

Component of asparaginase III α-β complex[3]; asparaginase III[3]

isoAsp aminopeptidase, cleaves isoAsp-X dipeptides, Ntn hydrolase, weak L-asparaginase activity in vitro (EcAIII), precursor is cleaved into an alpha and beta subunit[4]

heterotetrameric, glutathione utilization[5]

EC number (for enzymes)
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Notes

Function

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

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

PMID:PMID

NAS: Non-traceable Author Statement

C

Seeded from Riley et al 2006 [1].

complete

Deprecated

GO:0009063

cellular amino acid catabolic process

PMID:15265041[4]

IDA: Inferred from Direct Assay

P

See notes for the annotation of IaaA toGO:0006530.

complete

GO:0016787

hydrolase activity

PMID:15265041[4]

IDA: Inferred from Direct Assay

F

complete

GO:0004067

asparaginase activity

PMID:15265041[4]

IDA: Inferred from Direct Assay

F

See notes for the annotation of IaaA toGO:0006530.

complete

Deprecated

GO:0006530

asparagine catabolic process

PMID:15265041[4]

IDA: Inferred from Direct Assay

P

IaaA can hydrolyze asparagine to aspartate + NH3 in vitro, but the affinity for asparagine is lower than that of known bacterial asparaginases, so this activity may not be physiologically relevant.[6]

complete

GO:0008798

beta-aspartyl-peptidase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:3.4.19.5

F

Seeded from EcoCyc (v14.0)

complete

GO:0008798

beta-aspartyl-peptidase activity

PMID:15265041[4]

IDA: Inferred from Direct Assay

F

Table 2

complete

GO:0005737

cytoplasm

PMID:15946951[6]

IC: Inferred by Curator

C

Missing: with/from

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Interactions


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

Partner Type Partner Notes References Evidence

Protein

Subunits of asparaginase III α-β complex

could be indirect

Protein

caiB

PMID:16606699[7]

Experiment(s):EBI-1138145

Protein

moeA

PMID:16606699[7]

Experiment(s):EBI-1138145

Protein

yfiR

PMID:16606699[7]

Experiment(s):EBI-1138145

Protein

Subunits of asparaginase III

could be indirect


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Notes

Localization

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

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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

Name
Sequence 
MRITIILVAP ARAENIGAAA RAMKTMGFSD LRIVDSQAHL EPATRWVAHG SGDIIDNIKV
FPTLAESLHD VDFTVATTAR SRAKYHYYAT PVELVPLLEE KSSWMSHAAL VFGREDSGLT
NEELALADVL TGVPMVADYP SLNLGQAVMV YCYQLATLIQ QPAKSDATAD QHQLQALRER
AMTLLTTLAV ADDIKLVDWL QQRLGLLEQR DTAMLHRLLH DIEKNITK
Length

228

Mol. Wt

25.259 kDa

pI

5.9 (calculated)

Extinction coefficient

25,440 - 25,565 (calc based on 6 Y, 3 W, and 1 C residues)

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Domains/Motifs/Modification Sites

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

Type Residues Description Notes References

Initiator Methionine

1

Removed

UniProt:P37595

Domain

2..317

PF01112 Asparaginase

PMID:19920124[8]

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

Structures

<beststructure> gene=iaaA taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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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 type Source Notes/Reference
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Notes

Accessions in Other Databases

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

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128796

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945456

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0002828

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P37595

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG12407

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG12407

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945456

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120002269

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB2307

Escherichia coli str. K-12 substr. MG1655

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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 1.5 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 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 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 4.3 4.4 4.5 Borek, D et al. (2004) Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog. Eur. J. Biochem. 271 3215-26 PubMed
  5. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  6. ↑ 6.0 6.1 Michalska, K et al. (2005) Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate. J. Biol. Chem. 280 28484-91 PubMed
  7. ↑ 7.0 7.1 7.2 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  8. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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