aspC: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

AspC

Synonyms

aspartate aminotransferase, PLP-dependent[1], B0928[2][1], AspC[2][1] , ECK0919, JW0911, b0928

Product description

AspC[2][3];

Component of aspartate transaminase[2]; aspartate aminotransferase, PLP-dependent[3]

Aspartate aminotransferase, AspAT; kynurenine aminotransferase; glutamine transaminase K[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:0004069

L-aspartate:2-oxoglutarate aminotransferase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.6.1.1

F

Seeded from EcoCyc (v14.0)

complete

GO:0005829

cytosol

PMID:16858726[5]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0004838

L-tyrosine:2-oxoglutarate aminotransferase activity

PMID:15983[6]

IMP: Inferred from Mutant Phenotype

F

Table 4

complete

GO:0030170

pyridoxal phosphate binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004838

F

Seeded from EcoCyc (v14.0)

complete

GO:0004069

L-aspartate:2-oxoglutarate aminotransferase activity

PMID:15983[6]

IMP: Inferred from Mutant Phenotype

F

Table 3

complete

GO:0030170

pyridoxal phosphate binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004839

F

Seeded from EcoCyc (v14.0)

complete

GO:0009094

L-phenylalanine biosynthetic process

PMID:15983[6]

IGI: Inferred from Genetic Interaction

EcoliWiki:ilvE|EcoliWiki:tyrB

P

complete

GO:0030170

pyridoxal phosphate binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015421

F

Seeded from EcoCyc (v14.0)

complete

GO:0030170

pyridoxal phosphate binding

PMID:352693[7]

IDA: Inferred from Direct Assay

F

complete

GO:0033585

L-phenylalanine biosynthetic process from chorismate via phenylpyruvate

PMID:15983[6]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc (v14.0)

complete

GO:0042803

protein homodimerization activity

PMID:352693[7]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:352693[7]

IDA: Inferred from Direct Assay

C

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 aspartate transaminase

could be indirect

Protein

nadE

PMID:16606699[8]

Experiment(s):EBI-1138400

Protein

nuoC

PMID:19402753[9]

LCMS(ID Probability):99.6

Protein

tig

PMID:19402753[9]

LCMS(ID Probability):99.6

Protein

glf

PMID:19402753[9]

LCMS(ID Probability):99.6

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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

Cytoplasm

PMID:3521591[10]

EchoLocation:aspC


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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 

MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE
TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT PGGTGALRVA ADFLAKNTSV
KRVWVSNPSW PNHKSVFNSA GLEVREYAYY DAENHTLDFD ALINSLNEAQ AGDVVLFHGC
CHNPTGIDPT LEQWQTLAQL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV
ASSYSKNFGL YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN
DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF SGLTKEQVLR
LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL
Length

396

Mol. Wt

43.573 kDa

pI

5.6 (calculated)

Extinction coefficient

43,890 - 44,515 (calc based on 11 Y, 5 W, and 5 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

26..392

PF00155 Aminotransferase class I and II

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=aspC 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:16128895

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945553

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0003150

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P00509

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10096

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10096

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945553

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000092

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0094

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 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 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. ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  6. ↑ 6.0 6.1 6.2 6.3 Gelfand, DH & Steinberg, RA (1977) Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. J. Bacteriol. 130 429-40 PubMed
  7. ↑ 7.0 7.1 7.2 Powell, JT & Morrison, JF (1978) The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli. Eur. J. Biochem. 87 391-400 PubMed
  8. ↑ Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  9. ↑ 9.0 9.1 9.2 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  10. ↑ Fotheringham, IG et al. (1986) The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Biochem. J. 234 593-604 PubMed
  11. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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