ilvA: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

IlvA

Synonyms

threonine deaminase[1], B3772[2][1], Ile[2][1], IlvA[2][1] , ECK3764, JW3745, b3772

Product description

IlvA[2][3];

Component of threonine dehydratase (biosynthetic)[2][3]

Threonine deaminase; also known as threonine dehydratase, biosynthetic[4]

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

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0004794

L-threonine ammonia-lyase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001721

F

Seeded from EcoCyc (v14.0)

complete

GO:0004794

L-threonine ammonia-lyase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005787

F

Seeded from EcoCyc (v14.0)

complete

GO:0004794

L-threonine ammonia-lyase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:4.3.1.19

F

Seeded from EcoCyc (v14.0)

complete

GO:0009097

isoleucine biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001721

P

Seeded from EcoCyc (v14.0)

complete

GO:0009097

isoleucine biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005787

P

Seeded from EcoCyc (v14.0)

complete

GO:0009097

isoleucine biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0412

P

Seeded from EcoCyc (v14.0)

complete

GO:0016597

amino acid binding

PMID:2005118[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0030170

pyridoxal phosphate binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000634

F

Seeded from EcoCyc (v14.0)

complete

GO:0030170

pyridoxal phosphate binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001926

F

Seeded from EcoCyc (v14.0)

complete

GO:0009097

isoleucine biosynthetic process

PMID:4604254[6]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0004794

L-threonine ammonia-lyase activity

PMID:4604254[6]

IDA: Inferred from Direct Assay

F

complete

GO:0009082

branched chain family amino acid biosynthetic process

PMID:348689[7]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0009097

isoleucine biosynthetic process

PMID:8407838[8]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0004794

L-threonine ammonia-lyase activity

PMID:8407838[8]

IDA: Inferred from Direct Assay

F

complete

GO:0005737

cytoplasm

PMID:2005118[5]

IC: Inferred by Curator

C

Missing: with/from

GO:0004794

L-threonine ammonia-lyase activity

PMID:2005118[5]

IDA: Inferred from Direct Assay

F

complete

GO:0016597

amino acid binding

PMID:2005118[5]

IDA: Inferred from Direct Assay

F

L-Valine activates IlvA activity. CHEBI:16414

complete

GO:0016597

amino acid binding

PMID:2005118[5]

IDA: Inferred from Direct Assay

F

L-isoleucine binding negatively regulates IlvA activity. CHEBI:17191

complete

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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 threonine dehydratase (biosynthetic)

could be indirect

Protein

ppc

PMID:16606699[9]

Experiment(s):EBI-1146658

Protein

rpoC

PMID:16606699[9]

Experiment(s):EBI-1146658

Protein

rpsC

PMID:16606699[9]

Experiment(s):EBI-1146658

Protein

rne

PMID:16606699[9]

Experiment(s):EBI-1146658

Protein

yfaS

PMID:16606699[9]

Experiment(s):EBI-1146658

Protein

katG

PMID:19402753[10]

LCMS(ID Probability):99.6 MALDI(Z-score):27.215567

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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

at EcoCyc 

MADSQPLSGA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV KREDRQPVHS
FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR LGVKALIVMP TATADIKVDA
VRGFGGEVLL HGANFDEAKA KAIELSQQQG FTWVPPFDHP MVIAGQGTLA LELLQQDAHL
DRVFVPVGGG GLAAGVAVLI KQLMPQIKVI AVEAEDSACL KAALDAGHPV DLPRVGLFAE
GVAVKRIGDE TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI
ALHNIRGERL AHILSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG SFLKFCQLLG
GRSVTEFNYR FADAKNACIF VGVRLSRGLE ERKEILQMLN DGGYSVVDLS DDEMAKLHVR
YMVGGRPSHP LQERLYSFEF PESPGALLRF LNTLGTYWNI SLFHYRSHGT DYGRVLAAFE
LGDHEPDFET RLNELGYDCH DETNNPAFRF FLAG
Length

514

Mol. Wt

56.195 kDa

pI

5.8 (calculated)

Extinction coefficient

31,860 - 32,735 (calc based on 14 Y, 2 W, and 7 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

Domain

25..316

PF00291 Pyridoxal-phosphate dependent enzyme

PMID:19920124[11]

Domain

329..419

PF00585 C-terminal regulatory domain of Threonine dehydratase

PMID:19920124[11]

Domain

424..512

PF00585 C-terminal regulatory domain of Threonine dehydratase

PMID:19920124[11]

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

Structures

<beststructure> gene=ilvA 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:16131630

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:948287

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0012321

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P04968

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10493

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10493

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:948287

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000486

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0488

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 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 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 5.2 5.3 5.4 Eisenstein, E (1991) Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli. J. Biol. Chem. 266 5801-7 PubMed
  6. ↑ 6.0 6.1 Favre, R et al. (1974) Complementation between different mutations in the ilvA gene of Escherichia coli K-12. J. Bacteriol. 119 1069-71 PubMed
  7. ↑ Williams, AL et al. (1978) Synthesis and activities of branched-chain aminoacyl-tRNA synthetases in threonine deaminase mutants of Escherichia coli. J. Bacteriol. 134 92-9 PubMed
  8. ↑ 8.0 8.1 Fisher, KE & Eisenstein, E (1993) An efficient approach to identify ilvA mutations reveals an amino-terminal catalytic domain in biosynthetic threonine deaminase from Escherichia coli. J. Bacteriol. 175 6605-13 PubMed
  9. ↑ 9.0 9.1 9.2 9.3 9.4 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  10. ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  11. ↑ 11.0 11.1 11.2 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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