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ECOLI:AAT

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) aspC
Protein Name(s) Aspartate aminotransferase

AspAT Transaminase A

External Links
UniProt P00509
EMBL X03629
X05904
U00096
AP009048
PIR A00598
RefSeq NP_415448.1
YP_489200.1
PDB 1AAM
1AAW
1AHE
1AHF
1AHG
1AHX
1AHY
1AIA
1AIB
1AIC
1AMQ
1AMR
1AMS
1ARG
1ARH
1ARI
1ARS
1ART
1ASA
1ASB
1ASC
1ASD
1ASE
1ASF
1ASG
1ASL
1ASM
1ASN
1B4X
1BQA
1BQD
1C9C
1CQ6
1CQ7
1CQ8
1CZC
1CZE
1G4V
1G4X
1G7W
1G7X
1IX6
1IX7
1IX8
1QIR
1QIS
1QIT
1SPA
1TOE
1TOG
1TOI
1TOJ
1TOK
1X28
1X29
1X2A
1YOO
2AAT
2D5Y
2D61
2D63
2D64
2D65
2D66
2D7Y
2D7Z
2Q7W
2QA3
2QB2
2QB3
2QBT
3AAT
3QN6
3QPG
3ZZJ
3ZZK
4A00
4DBC
4F5F
4F5G
4F5H
4F5I
4F5J
4F5K
4F5L
4F5M
5EAA
PDBsum 1AAM
1AAW
1AHE
1AHF
1AHG
1AHX
1AHY
1AIA
1AIB
1AIC
1AMQ
1AMR
1AMS
1ARG
1ARH
1ARI
1ARS
1ART
1ASA
1ASB
1ASC
1ASD
1ASE
1ASF
1ASG
1ASL
1ASM
1ASN
1B4X
1BQA
1BQD
1C9C
1CQ6
1CQ7
1CQ8
1CZC
1CZE
1G4V
1G4X
1G7W
1G7X
1IX6
1IX7
1IX8
1QIR
1QIS
1QIT
1SPA
1TOE
1TOG
1TOI
1TOJ
1TOK
1X28
1X29
1X2A
1YOO
2AAT
2D5Y
2D61
2D63
2D64
2D65
2D66
2D7Y
2D7Z
2Q7W
2QA3
2QB2
2QB3
2QBT
3AAT
3QN6
3QPG
3ZZJ
3ZZK
4A00
4DBC
4F5F
4F5G
4F5H
4F5I
4F5J
4F5K
4F5L
4F5M
5EAA
ProteinModelPortal P00509
SMR P00509
DIP DIP-9181N
IntAct P00509
STRING 511145.b0928
SWISS-2DPAGE P00509
PaxDb P00509
PRIDE P00509
EnsemblBacteria AAC74014
BAA35674
GeneID 12931027
945553
KEGG ecj:Y75_p0900
eco:b0928
PATRIC 32117069
EchoBASE EB0094
EcoGene EG10096
eggNOG COG1448
HOGENOM HOG000185899
InParanoid P00509
KO K00813
OMA KIWISNP
OrthoDB EOG6C2WBK
PhylomeDB P00509
BioCyc EcoCyc:ASPAMINOTRANS-MONOMER
ECOL316407:JW0911-MONOMER
MetaCyc:ASPAMINOTRANS-MONOMER
BRENDA 2.6.1.1
SABIO-RK P00509
EvolutionaryTrace P00509
PRO PR:P00509
Proteomes UP000000318
UP000000625
Genevestigator P00509
GO GO:0005737
GO:0005829
GO:0042802
GO:0004069
GO:0080130
GO:0004838
GO:0030170
GO:0009094
GO:0033585
Gene3D 3.40.640.10
InterPro IPR004839
IPR000796
IPR004838
IPR015424
IPR015421
PANTHER PTHR11879
Pfam PF00155
PRINTS PR00799
SUPFAM SSF53383
PROSITE PS00105

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0047319

aspartate-phenylpyruvate transaminase activity

PMID:352693[1]

ECO:0000314

F

Figure 1 shows increasing phenylalanine aminotransferase activity with increasing levels of enzyme.

complete
CACAO 4071

GO:0008483

transaminase activity

PMID:9893985[2]

ECO:0000315

F

Fig. 2 shows the difference in transamination rates between wild type AspAT and mutant forms.

complete
CACAO 4664

part_of

GO:0005829

cytosol

PMID:16858726[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10096
PANTHER:PTN000222929

F

Seeded From UniProt

complete

involved_in

GO:0033585

L-phenylalanine biosynthetic process from chorismate via phenylpyruvate

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10096
EcoGene:EG11040
PANTHER:PTN000222931

P

Seeded From UniProt

complete

enables

GO:0030170

pyridoxal phosphate binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10096
EcoGene:EG11040
PANTHER:PTN000222929

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10096
EcoGene:EG11040
PANTHER:PTN000222931

C

Seeded From UniProt

complete

enables

GO:0004838

L-tyrosine:2-oxoglutarate aminotransferase activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10096
EcoGene:EG11040
PANTHER:PTN000222931

F

Seeded From UniProt

complete

enables

GO:0004069

L-aspartate:2-oxoglutarate aminotransferase activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10096
PANTHER:PTN000222932

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P00509

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P00509

F

Seeded From UniProt

complete

enables

GO:0030170

pyridoxal phosphate binding

PMID:352693[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009094

L-phenylalanine biosynthetic process

PMID:15983[6]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:ilvE
EcoliWiki:tyrB

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:352693[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004838

L-tyrosine:2-oxoglutarate aminotransferase activity

PMID:15983[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004069

L-aspartate:2-oxoglutarate aminotransferase activity

PMID:15983[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0033585

L-phenylalanine biosynthetic process from chorismate via phenylpyruvate

PMID:15983[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004838
InterPro:IPR015421
InterPro:IPR015422

F

Seeded From UniProt

complete

involved_in

GO:0006520

cellular amino acid metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000796

P

Seeded From UniProt

complete

enables

GO:0008483

transaminase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000796

F

Seeded From UniProt

complete

involved_in

GO:0009058

biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004838
InterPro:IPR004839

P

Seeded From UniProt

complete

enables

GO:0030170

pyridoxal phosphate binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004838
InterPro:IPR004839

F

Seeded From UniProt

complete

enables

GO:0004069

L-aspartate:2-oxoglutarate aminotransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.6.1.1

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0008483

transaminase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0032

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 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 GONUTS page
  2. Birolo, L et al. (1999) Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase. Biochemistry 38 905-13 PubMed GONUTS page
  3. 3.0 3.1 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 GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 4.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  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 GONUTS page