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Protein

Aspartate aminotransferase

Gene

aspC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei34Aspartate; via amide nitrogen1
Binding sitei130Aspartate1
Binding sitei183Aspartate1
Binding sitei374Aspartate1

GO - Molecular functioni

  • L-aspartate:2-oxoglutarate aminotransferase activity Source: EcoliWiki
  • L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  • L-tyrosine:2-oxoglutarate aminotransferase activity Source: EcoliWiki
  • pyridoxal phosphate binding Source: EcoliWiki

GO - Biological processi

  • L-phenylalanine biosynthetic process Source: EcoliWiki
  • L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:ASPAMINOTRANS-MONOMER.
ECOL316407:JW0911-MONOMER.
MetaCyc:ASPAMINOTRANS-MONOMER.
BRENDAi2.6.1.1. 2026.
SABIO-RKP00509.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase (EC:2.6.1.1)
Short name:
AspAT
Alternative name(s):
Transaminase A
Gene namesi
Name:aspC
Ordered Locus Names:b0928, JW0911
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10096. aspC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65Y → F or S: Slight changes in activity. 1 Publication1
Mutagenesisi133H → A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate. 1 Publication1
Mutagenesisi133H → N: Decreases to 60% in maximum rate of the overall reactions in both directions. 1 Publication1
Mutagenesisi280R → V: Reduces first-order rate constant over 25000-fold. 1 Publication1
Mutagenesisi374R → A: Reduces first-order rate constant about 10000-fold. 2 Publications1
Mutagenesisi374R → F or Y: Second-order rate constants are reduced by >5 orders of magnitude. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001238381 – 396Aspartate aminotransferaseAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei246N6-(pyridoxal phosphate)lysine1 Publication1

Proteomic databases

EPDiP00509.
PaxDbiP00509.
PRIDEiP00509.

2D gel databases

SWISS-2DPAGEP00509.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-907474,EBI-907474

Protein-protein interaction databases

BioGridi4260021. 18 interactors.
DIPiDIP-9181N.
IntActiP00509. 4 interactors.
STRINGi511145.b0928.

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2 – 4Combined sources3
Helixi12 – 22Combined sources11
Beta strandi29 – 32Combined sources4
Beta strandi33 – 35Combined sources3
Turni39 – 41Combined sources3
Helixi47 – 59Combined sources13
Helixi72 – 83Combined sources12
Helixi88 – 91Combined sources4
Beta strandi95 – 101Combined sources7
Helixi102 – 117Combined sources16
Beta strandi122 – 128Combined sources7
Helixi132 – 139Combined sources8
Beta strandi143 – 148Combined sources6
Turni152 – 155Combined sources4
Helixi159 – 166Combined sources8
Beta strandi174 – 178Combined sources5
Beta strandi179 – 181Combined sources3
Turni183 – 185Combined sources3
Helixi191 – 204Combined sources14
Beta strandi207 – 213Combined sources7
Beta strandi217 – 219Combined sources3
Helixi221 – 224Combined sources4
Helixi226 – 234Combined sources9
Beta strandi238 – 243Combined sources6
Turni245 – 249Combined sources5
Helixi251 – 253Combined sources3
Beta strandi256 – 261Combined sources6
Helixi265 – 280Combined sources16
Turni281 – 283Combined sources3
Helixi288 – 298Combined sources11
Helixi301 – 331Combined sources31
Helixi340 – 343Combined sources4
Beta strandi346 – 350Combined sources5
Helixi355 – 365Combined sources11
Beta strandi367 – 369Combined sources3
Turni371 – 373Combined sources3
Beta strandi374 – 376Combined sources3
Helixi377 – 379Combined sources3
Turni382 – 384Combined sources3
Helixi385 – 395Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AAMX-ray2.80A1-396[»]
1AAWX-ray2.40A1-396[»]
1AHEX-ray2.30A/B1-396[»]
1AHFX-ray2.30A/B1-396[»]
1AHGX-ray2.50A/B1-396[»]
1AHXX-ray2.00A/B1-396[»]
1AHYX-ray2.30A/B1-396[»]
1AIAX-ray2.20A/B1-396[»]
1AIBX-ray2.80A/B1-396[»]
1AICX-ray2.40A/B1-396[»]
1AMQX-ray2.20A1-396[»]
1AMRX-ray2.10A1-396[»]
1AMSX-ray2.70A1-396[»]
1ARGX-ray2.20A/B1-396[»]
1ARHX-ray2.30A/B1-396[»]
1ARIX-ray2.30A/B1-396[»]
1ARSX-ray1.80A1-396[»]
1ARTX-ray1.80A1-396[»]
1ASAX-ray2.40A1-396[»]
1ASBX-ray2.60A1-396[»]
1ASCX-ray2.40A1-396[»]
1ASDX-ray2.20A1-396[»]
1ASEX-ray2.50A1-396[»]
1ASFX-ray2.80A1-396[»]
1ASGX-ray2.80A1-396[»]
1ASLX-ray2.60A/B1-396[»]
1ASMX-ray2.35A/B1-396[»]
1ASNX-ray2.50A/B1-396[»]
1B4XX-ray2.45A1-396[»]
1BQAX-ray2.10A/B1-396[»]
1BQDX-ray2.10A/B1-396[»]
1C9CX-ray2.40A1-396[»]
1CQ6X-ray2.70A1-396[»]
1CQ7X-ray2.40A1-396[»]
1CQ8X-ray2.40A1-396[»]
1CZCX-ray2.50A1-396[»]
1CZEX-ray2.40A1-396[»]
1G4VX-ray2.00A1-396[»]
1G4XX-ray2.20A1-396[»]
1G7WX-ray2.20A1-396[»]
1G7XX-ray2.20A1-396[»]
1IX6X-ray2.20A1-396[»]
1IX7X-ray2.20A1-396[»]
1IX8X-ray2.20A1-396[»]
1QIRX-ray2.20A1-396[»]
1QISX-ray1.90A1-396[»]
1QITX-ray1.90A1-396[»]
1SPAX-ray2.00A1-396[»]
1TOEX-ray2.00A1-388[»]
1TOGX-ray2.31A/B1-388[»]
1TOIX-ray1.90A1-388[»]
1TOJX-ray1.90A1-388[»]
1TOKX-ray1.85A/B1-388[»]
1X28X-ray2.40A/B1-396[»]
1X29X-ray2.20A/B1-396[»]
1X2AX-ray2.20A/B1-396[»]
1YOOX-ray2.40A1-396[»]
2AATX-ray2.80A1-396[»]
2D5YX-ray1.98A1-396[»]
2D61X-ray2.01A1-396[»]
2D63X-ray2.05A1-396[»]
2D64X-ray2.05A1-396[»]
2D65X-ray2.30A1-396[»]
2D66X-ray2.18A1-396[»]
2D7YX-ray2.66A1-396[»]
2D7ZX-ray2.65A1-396[»]
2Q7WX-ray1.40A1-396[»]
2QA3X-ray1.75A1-396[»]
2QB2X-ray1.70A1-396[»]
2QB3X-ray1.45A1-396[»]
2QBTX-ray1.75A1-396[»]
3AATX-ray2.80A1-396[»]
3QN6X-ray1.79A1-396[»]
3QPGX-ray1.79A1-396[»]
3ZZJX-ray2.50A1-396[»]
3ZZKX-ray1.78A1-396[»]
4A00X-ray2.34A1-396[»]
4DBCX-ray1.50A1-396[»]
4F5FX-ray2.25A/B2-396[»]
4F5GX-ray1.67A/B2-396[»]
4F5HX-ray1.60A/B2-396[»]
4F5IX-ray2.20A/B2-396[»]
4F5JX-ray1.95A/B2-396[»]
4F5KX-ray2.20A/B2-396[»]
4F5LX-ray1.40A/B2-396[»]
4F5MX-ray1.65A/B2-396[»]
5EAAX-ray2.40A1-396[»]
ProteinModelPortaliP00509.
SMRiP00509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00509.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CGF. Bacteria.
COG1448. LUCA.
HOGENOMiHOG000185899.
InParanoidiP00509.
KOiK00813.
OMAiPNHKGVF.
PhylomeDBiP00509.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00509-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK
60 70 80 90 100
KAEQYLLENE TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT
110 120 130 140 150
PGGTGALRVA ADFLAKNTSV KRVWVSNPSW PNHKSVFNSA GLEVREYAYY
160 170 180 190 200
DAENHTLDFD ALINSLNEAQ AGDVVLFHGC CHNPTGIDPT LEQWQTLAQL
210 220 230 240 250
SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV ASSYSKNFGL
260 270 280 290 300
YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN
310 320 330 340 350
DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF
360 370 380 390
SGLTKEQVLR LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL
Length:396
Mass (Da):43,573
Last modified:July 21, 1986 - v1
Checksum:i9F0437E76DD4FC0F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03629 Genomic DNA. Translation: CAA27279.1.
X05904 Genomic DNA. Translation: CAA29333.1.
U00096 Genomic DNA. Translation: AAC74014.1.
AP009048 Genomic DNA. Translation: BAA35674.1.
PIRiA00598. XNECD.
RefSeqiNP_415448.1. NC_000913.3.
WP_000462687.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74014; AAC74014; b0928.
BAA35674; BAA35674; BAA35674.
GeneIDi945553.
KEGGiecj:JW0911.
eco:b0928.
PATRICi32117069. VBIEscCol129921_0959.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03629 Genomic DNA. Translation: CAA27279.1.
X05904 Genomic DNA. Translation: CAA29333.1.
U00096 Genomic DNA. Translation: AAC74014.1.
AP009048 Genomic DNA. Translation: BAA35674.1.
PIRiA00598. XNECD.
RefSeqiNP_415448.1. NC_000913.3.
WP_000462687.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AAMX-ray2.80A1-396[»]
1AAWX-ray2.40A1-396[»]
1AHEX-ray2.30A/B1-396[»]
1AHFX-ray2.30A/B1-396[»]
1AHGX-ray2.50A/B1-396[»]
1AHXX-ray2.00A/B1-396[»]
1AHYX-ray2.30A/B1-396[»]
1AIAX-ray2.20A/B1-396[»]
1AIBX-ray2.80A/B1-396[»]
1AICX-ray2.40A/B1-396[»]
1AMQX-ray2.20A1-396[»]
1AMRX-ray2.10A1-396[»]
1AMSX-ray2.70A1-396[»]
1ARGX-ray2.20A/B1-396[»]
1ARHX-ray2.30A/B1-396[»]
1ARIX-ray2.30A/B1-396[»]
1ARSX-ray1.80A1-396[»]
1ARTX-ray1.80A1-396[»]
1ASAX-ray2.40A1-396[»]
1ASBX-ray2.60A1-396[»]
1ASCX-ray2.40A1-396[»]
1ASDX-ray2.20A1-396[»]
1ASEX-ray2.50A1-396[»]
1ASFX-ray2.80A1-396[»]
1ASGX-ray2.80A1-396[»]
1ASLX-ray2.60A/B1-396[»]
1ASMX-ray2.35A/B1-396[»]
1ASNX-ray2.50A/B1-396[»]
1B4XX-ray2.45A1-396[»]
1BQAX-ray2.10A/B1-396[»]
1BQDX-ray2.10A/B1-396[»]
1C9CX-ray2.40A1-396[»]
1CQ6X-ray2.70A1-396[»]
1CQ7X-ray2.40A1-396[»]
1CQ8X-ray2.40A1-396[»]
1CZCX-ray2.50A1-396[»]
1CZEX-ray2.40A1-396[»]
1G4VX-ray2.00A1-396[»]
1G4XX-ray2.20A1-396[»]
1G7WX-ray2.20A1-396[»]
1G7XX-ray2.20A1-396[»]
1IX6X-ray2.20A1-396[»]
1IX7X-ray2.20A1-396[»]
1IX8X-ray2.20A1-396[»]
1QIRX-ray2.20A1-396[»]
1QISX-ray1.90A1-396[»]
1QITX-ray1.90A1-396[»]
1SPAX-ray2.00A1-396[»]
1TOEX-ray2.00A1-388[»]
1TOGX-ray2.31A/B1-388[»]
1TOIX-ray1.90A1-388[»]
1TOJX-ray1.90A1-388[»]
1TOKX-ray1.85A/B1-388[»]
1X28X-ray2.40A/B1-396[»]
1X29X-ray2.20A/B1-396[»]
1X2AX-ray2.20A/B1-396[»]
1YOOX-ray2.40A1-396[»]
2AATX-ray2.80A1-396[»]
2D5YX-ray1.98A1-396[»]
2D61X-ray2.01A1-396[»]
2D63X-ray2.05A1-396[»]
2D64X-ray2.05A1-396[»]
2D65X-ray2.30A1-396[»]
2D66X-ray2.18A1-396[»]
2D7YX-ray2.66A1-396[»]
2D7ZX-ray2.65A1-396[»]
2Q7WX-ray1.40A1-396[»]
2QA3X-ray1.75A1-396[»]
2QB2X-ray1.70A1-396[»]
2QB3X-ray1.45A1-396[»]
2QBTX-ray1.75A1-396[»]
3AATX-ray2.80A1-396[»]
3QN6X-ray1.79A1-396[»]
3QPGX-ray1.79A1-396[»]
3ZZJX-ray2.50A1-396[»]
3ZZKX-ray1.78A1-396[»]
4A00X-ray2.34A1-396[»]
4DBCX-ray1.50A1-396[»]
4F5FX-ray2.25A/B2-396[»]
4F5GX-ray1.67A/B2-396[»]
4F5HX-ray1.60A/B2-396[»]
4F5IX-ray2.20A/B2-396[»]
4F5JX-ray1.95A/B2-396[»]
4F5KX-ray2.20A/B2-396[»]
4F5LX-ray1.40A/B2-396[»]
4F5MX-ray1.65A/B2-396[»]
5EAAX-ray2.40A1-396[»]
ProteinModelPortaliP00509.
SMRiP00509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260021. 18 interactors.
DIPiDIP-9181N.
IntActiP00509. 4 interactors.
STRINGi511145.b0928.

2D gel databases

SWISS-2DPAGEP00509.

Proteomic databases

EPDiP00509.
PaxDbiP00509.
PRIDEiP00509.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74014; AAC74014; b0928.
BAA35674; BAA35674; BAA35674.
GeneIDi945553.
KEGGiecj:JW0911.
eco:b0928.
PATRICi32117069. VBIEscCol129921_0959.

Organism-specific databases

EchoBASEiEB0094.
EcoGeneiEG10096. aspC.

Phylogenomic databases

eggNOGiENOG4105CGF. Bacteria.
COG1448. LUCA.
HOGENOMiHOG000185899.
InParanoidiP00509.
KOiK00813.
OMAiPNHKGVF.
PhylomeDBiP00509.

Enzyme and pathway databases

BioCyciEcoCyc:ASPAMINOTRANS-MONOMER.
ECOL316407:JW0911-MONOMER.
MetaCyc:ASPAMINOTRANS-MONOMER.
BRENDAi2.6.1.1. 2026.
SABIO-RKP00509.

Miscellaneous databases

EvolutionaryTraceiP00509.
PROiP00509.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAAT_ECOLI
AccessioniPrimary (citable) accession number: P00509
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.