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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341Aspartate; via amide nitrogen
Binding sitei130 – 1301Aspartate
Binding sitei183 – 1831Aspartate
Binding sitei374 – 3741Aspartate

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651Y → F or S: Slight changes in activity. 1 Publication
Mutagenesisi133 – 1331H → A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate. 1 Publication
Mutagenesisi133 – 1331H → N: Decreases to 60% in maximum rate of the overall reactions in both directions. 1 Publication
Mutagenesisi280 – 2801R → V: Reduces first-order rate constant over 25000-fold. 1 Publication
Mutagenesisi374 – 3741R → A: Reduces first-order rate constant about 10000-fold. 2 Publications
Mutagenesisi374 – 3741R → F or Y: Second-order rate constants are reduced by >5 orders of magnitude. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Aspartate aminotransferasePRO_0000123838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461N6-(pyridoxal phosphate)lysine1 Publication

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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

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

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 43Combined sources
Helixi12 – 2211Combined sources
Beta strandi29 – 324Combined sources
Beta strandi33 – 353Combined sources
Turni39 – 413Combined sources
Helixi47 – 5913Combined sources
Helixi72 – 8312Combined sources
Helixi88 – 914Combined sources
Beta strandi95 – 1017Combined sources
Helixi102 – 11716Combined sources
Beta strandi122 – 1287Combined sources
Helixi132 – 1398Combined sources
Beta strandi143 – 1486Combined sources
Turni152 – 1554Combined sources
Helixi159 – 1668Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi179 – 1813Combined sources
Turni183 – 1853Combined sources
Helixi191 – 20414Combined sources
Beta strandi207 – 2137Combined sources
Beta strandi217 – 2193Combined sources
Helixi221 – 2244Combined sources
Helixi226 – 2349Combined sources
Beta strandi238 – 2436Combined sources
Turni245 – 2495Combined sources
Helixi251 – 2533Combined sources
Beta strandi256 – 2616Combined sources
Helixi265 – 28016Combined sources
Turni281 – 2833Combined sources
Helixi288 – 29811Combined sources
Helixi301 – 33131Combined sources
Helixi340 – 3434Combined sources
Beta strandi346 – 3505Combined sources
Helixi355 – 36511Combined sources
Beta strandi367 – 3693Combined sources
Turni371 – 3733Combined sources
Beta strandi374 – 3763Combined sources
Helixi377 – 3793Combined sources
Turni382 – 3843Combined sources
Helixi385 – 39511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-396.
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
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. Positions 1-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260021. 18 interactions.
DIPiDIP-9181N.
IntActiP00509. 4 interactions.
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: September 7, 2016
This is version 166 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.