UniProtKB - P00509 (AAT_ECOLI)
Protein
Aspartate aminotransferase
Gene
aspC
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalytic activityi
- EC:2.6.1.11 Publication
Cofactori
pyridoxal 5'-phosphate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 34 | Aspartate; via amide nitrogenCombined sources | 1 | |
Binding sitei | 130 | AspartateCombined sources | 1 | |
Binding sitei | 183 | AspartateCombined sources | 1 | |
Binding sitei | 374 | AspartateCombined sources | 1 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- L-aspartate:2-oxoglutarate aminotransferase activity Source: EcoliWiki
- L-tyrosine:2-oxoglutarate aminotransferase activity Source: EcoliWiki
- pyridoxal phosphate binding Source: EcoliWiki
- transaminase activity Source: GO_Central
GO - Biological processi
- L-phenylalanine biosynthetic process Source: EcoliWiki
- L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Source: EcoCyc
Keywordsi
Molecular function | Aminotransferase, Transferase |
Ligand | Pyridoxal phosphate |
Enzyme and pathway databases
BioCyci | EcoCyc:ASPAMINOTRANS-MONOMER MetaCyc:ASPAMINOTRANS-MONOMER |
BRENDAi | 2.6.1.1, 2026 |
SABIO-RKi | P00509 |
Names & Taxonomyi
Protein namesi | Recommended name: Aspartate aminotransferase (EC:2.6.1.11 Publication)Short name: AspAT Alternative name(s): Transaminase A |
Gene namesi | Name:aspC Ordered Locus Names:b0928, JW0911 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Biotechnological usei
Has been used to construct a 2,4,6-trinitrotoluene (TNT) biosensor strain.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 65 | Y → F or S: Slight changes in activity. 1 Publication | 1 | |
Mutagenesisi | 133 | H → A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate. 1 Publication | 1 | |
Mutagenesisi | 133 | H → N: Decreases to 60% in maximum rate of the overall reactions in both directions. 1 Publication | 1 | |
Mutagenesisi | 280 | R → V: Reduces first-order rate constant over 25000-fold. 1 Publication | 1 | |
Mutagenesisi | 374 | R → A: Reduces first-order rate constant about 10000-fold. 2 Publications | 1 | |
Mutagenesisi | 374 | R → F or Y: Second-order rate constants are reduced by >5 orders of magnitude. 2 Publications | 1 |
Chemistry databases
DrugBanki | DB02024, 3-phenylpropionic acid DB03553, Glutaric Acid DB02758, Indolepropionic acid DB03750, Isovaleric Acid DB04299, Maleic Acid DB04083, N(6)-(pyridoxal phosphate)-L-lysine DB04467, N-(5'-phosphopyridoxyl)-L-alanine DB01639, N-Methyl-Pyridoxal-5'-Phosphate DB04765, N-PYRIDOXYL-2-METHYL-L-GLUTAMIC ACID-5'-MONOPHOSPHATE DB04762, N-PYRIDOXYL-D-GLUTAMIC ACID-5'-MONOPHOSPHATE DB08845, Oxogluric acid DB03629, Pyridoxal-5'-Phosphate-N-Oxide DB02981, Vitamin B6 Complexed with 2-Amino-Hexanoic Acid DB03662, Vitamin B6 Complexed with 2-Amino-Pentanoic Acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000123838 | 1 – 396 | Aspartate aminotransferaseAdd BLAST | 396 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 246 | N6-(pyridoxal phosphate)lysineCombined sources4 Publications | 1 |
Proteomic databases
jPOSTi | P00509 |
PaxDbi | P00509 |
PRIDEi | P00509 |
2D gel databases
SWISS-2DPAGEi | P00509 |
Expressioni
Inductioni
Transcription is increased specifically in response to 2,4,6-trinitrotoluene (TNT) and its indicator compounds 1,3-DNB, 2,4-DNT, and 2,6-DNT.1 Publication
Interactioni
Subunit structurei
Homodimer.
1 PublicationBinary interactionsi
P00509
With | #Exp. | IntAct |
---|---|---|
itself | 4 | EBI-907474,EBI-907474 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4260021, 28 interactors 849927, 1 interactor |
DIPi | DIP-9181N |
IntActi | P00509, 4 interactors |
STRINGi | 511145.b0928 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P00509 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P00509 |
Family & Domainsi
Sequence similaritiesi
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.Curated
Phylogenomic databases
eggNOGi | COG1448, Bacteria |
HOGENOMi | CLU_032440_1_2_6 |
InParanoidi | P00509 |
PhylomeDBi | P00509 |
Family and domain databases
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
InterProi | View protein in InterPro IPR004839, Aminotransferase_I/II IPR000796, Asp_trans IPR004838, NHTrfase_class1_PyrdxlP-BS IPR015424, PyrdxlP-dep_Trfase IPR015422, PyrdxlP-dep_Trfase_dom1 IPR015421, PyrdxlP-dep_Trfase_major |
PANTHERi | PTHR11879, PTHR11879, 1 hit |
Pfami | View protein in Pfam PF00155, Aminotran_1_2, 1 hit |
PRINTSi | PR00799, TRANSAMINASE |
SUPFAMi | SSF53383, SSF53383, 1 hit |
PROSITEi | View protein in PROSITE PS00105, AA_TRANSFER_CLASS_1, 1 hit |
i Sequence
Sequence statusi: Complete.
P00509-1 [UniParc]FASTAAdd to basket
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
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 |
PIRi | A00598, XNECD |
RefSeqi | NP_415448.1, NC_000913.3 WP_000462687.1, NZ_STEB01000006.1 |
Genome annotation databases
EnsemblBacteriai | AAC74014; AAC74014; b0928 BAA35674; BAA35674; BAA35674 |
GeneIDi | 57728339 945553 |
KEGGi | ecj:JW0911 eco:b0928 |
PATRICi | fig|1411691.4.peg.1348 |
Similar proteinsi
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 |
PIRi | A00598, XNECD |
RefSeqi | NP_415448.1, NC_000913.3 WP_000462687.1, NZ_STEB01000006.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AAM | X-ray | 2.80 | A | 1-396 | [»] | |
1AAW | X-ray | 2.40 | A | 1-396 | [»] | |
1AHE | X-ray | 2.30 | A/B | 1-396 | [»] | |
1AHF | X-ray | 2.30 | A/B | 1-396 | [»] | |
1AHG | X-ray | 2.50 | A/B | 1-396 | [»] | |
1AHX | X-ray | 2.00 | A/B | 1-396 | [»] | |
1AHY | X-ray | 2.30 | A/B | 1-396 | [»] | |
1AIA | X-ray | 2.20 | A/B | 1-396 | [»] | |
1AIB | X-ray | 2.80 | A/B | 1-396 | [»] | |
1AIC | X-ray | 2.40 | A/B | 1-396 | [»] | |
1AMQ | X-ray | 2.20 | A | 1-396 | [»] | |
1AMR | X-ray | 2.10 | A | 1-396 | [»] | |
1AMS | X-ray | 2.70 | A | 1-396 | [»] | |
1ARG | X-ray | 2.20 | A/B | 1-396 | [»] | |
1ARH | X-ray | 2.30 | A/B | 1-396 | [»] | |
1ARI | X-ray | 2.30 | A/B | 1-396 | [»] | |
1ARS | X-ray | 1.80 | A | 1-396 | [»] | |
1ART | X-ray | 1.80 | A | 1-396 | [»] | |
1ASA | X-ray | 2.40 | A | 1-396 | [»] | |
1ASB | X-ray | 2.60 | A | 1-396 | [»] | |
1ASC | X-ray | 2.40 | A | 1-396 | [»] | |
1ASD | X-ray | 2.20 | A | 1-396 | [»] | |
1ASE | X-ray | 2.50 | A | 1-396 | [»] | |
1ASF | X-ray | 2.80 | A | 1-396 | [»] | |
1ASG | X-ray | 2.80 | A | 1-396 | [»] | |
1ASL | X-ray | 2.60 | A/B | 1-396 | [»] | |
1ASM | X-ray | 2.35 | A/B | 1-396 | [»] | |
1ASN | X-ray | 2.50 | A/B | 1-396 | [»] | |
1B4X | X-ray | 2.45 | A | 1-396 | [»] | |
1BQA | X-ray | 2.10 | A/B | 1-396 | [»] | |
1BQD | X-ray | 2.10 | A/B | 1-396 | [»] | |
1C9C | X-ray | 2.40 | A | 1-396 | [»] | |
1CQ6 | X-ray | 2.70 | A | 1-396 | [»] | |
1CQ7 | X-ray | 2.40 | A | 1-396 | [»] | |
1CQ8 | X-ray | 2.40 | A | 1-396 | [»] | |
1CZC | X-ray | 2.50 | A | 1-396 | [»] | |
1CZE | X-ray | 2.40 | A | 1-396 | [»] | |
1G4V | X-ray | 2.00 | A | 1-396 | [»] | |
1G4X | X-ray | 2.20 | A | 1-396 | [»] | |
1G7W | X-ray | 2.20 | A | 1-396 | [»] | |
1G7X | X-ray | 2.20 | A | 1-396 | [»] | |
1IX6 | X-ray | 2.20 | A | 1-396 | [»] | |
1IX7 | X-ray | 2.20 | A | 1-396 | [»] | |
1IX8 | X-ray | 2.20 | A | 1-396 | [»] | |
1QIR | X-ray | 2.20 | A | 1-396 | [»] | |
1QIS | X-ray | 1.90 | A | 1-396 | [»] | |
1QIT | X-ray | 1.90 | A | 1-396 | [»] | |
1SPA | X-ray | 2.00 | A | 1-396 | [»] | |
1TOE | X-ray | 2.00 | A | 1-396 | [»] | |
1TOG | X-ray | 2.31 | A/B | 1-396 | [»] | |
1TOI | X-ray | 1.90 | A | 1-396 | [»] | |
1TOJ | X-ray | 1.90 | A | 1-396 | [»] | |
1TOK | X-ray | 1.85 | A/B | 1-396 | [»] | |
1X28 | X-ray | 2.40 | A/B | 1-396 | [»] | |
1X29 | X-ray | 2.20 | A/B | 1-396 | [»] | |
1X2A | X-ray | 2.20 | A/B | 1-396 | [»] | |
1YOO | X-ray | 2.40 | A | 1-396 | [»] | |
2AAT | X-ray | 2.80 | A | 1-396 | [»] | |
2D5Y | X-ray | 1.98 | A | 1-396 | [»] | |
2D61 | X-ray | 2.01 | A | 1-396 | [»] | |
2D63 | X-ray | 2.05 | A | 1-396 | [»] | |
2D64 | X-ray | 2.05 | A | 1-396 | [»] | |
2D65 | X-ray | 2.30 | A | 1-396 | [»] | |
2D66 | X-ray | 2.18 | A | 1-396 | [»] | |
2D7Y | X-ray | 2.66 | A | 1-396 | [»] | |
2D7Z | X-ray | 2.65 | A | 1-396 | [»] | |
2Q7W | X-ray | 1.40 | A | 1-396 | [»] | |
2QA3 | X-ray | 1.75 | A | 1-396 | [»] | |
2QB2 | X-ray | 1.70 | A | 1-396 | [»] | |
2QB3 | X-ray | 1.45 | A | 1-396 | [»] | |
2QBT | X-ray | 1.75 | A | 1-396 | [»] | |
3AAT | X-ray | 2.80 | A | 1-396 | [»] | |
3QN6 | X-ray | 1.79 | A | 1-396 | [»] | |
3QPG | X-ray | 1.79 | A | 1-396 | [»] | |
3ZZJ | X-ray | 2.50 | A | 1-396 | [»] | |
3ZZK | X-ray | 1.78 | A | 1-396 | [»] | |
4A00 | X-ray | 2.34 | A | 1-396 | [»] | |
4DBC | X-ray | 1.50 | A | 1-396 | [»] | |
4F5F | X-ray | 2.25 | A/B | 2-396 | [»] | |
4F5G | X-ray | 1.67 | A/B | 2-396 | [»] | |
4F5H | X-ray | 1.60 | A/B | 2-396 | [»] | |
4F5I | X-ray | 2.20 | A/B | 2-396 | [»] | |
4F5J | X-ray | 1.95 | A/B | 2-396 | [»] | |
4F5K | X-ray | 2.20 | A/B | 2-396 | [»] | |
4F5L | X-ray | 1.40 | A/B | 2-396 | [»] | |
4F5M | X-ray | 1.65 | A/B | 2-396 | [»] | |
5EAA | X-ray | 2.40 | A | 1-396 | [»] | |
5T4L | X-ray | 1.53 | A | 1-396 | [»] | |
5VWQ | X-ray | 1.80 | A/D/G/J | 1-396 | [»] | |
5VWR | X-ray | 1.72 | A | 1-396 | [»] | |
SMRi | P00509 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260021, 28 interactors 849927, 1 interactor |
DIPi | DIP-9181N |
IntActi | P00509, 4 interactors |
STRINGi | 511145.b0928 |
Chemistry databases
DrugBanki | DB02024, 3-phenylpropionic acid DB03553, Glutaric Acid DB02758, Indolepropionic acid DB03750, Isovaleric Acid DB04299, Maleic Acid DB04083, N(6)-(pyridoxal phosphate)-L-lysine DB04467, N-(5'-phosphopyridoxyl)-L-alanine DB01639, N-Methyl-Pyridoxal-5'-Phosphate DB04765, N-PYRIDOXYL-2-METHYL-L-GLUTAMIC ACID-5'-MONOPHOSPHATE DB04762, N-PYRIDOXYL-D-GLUTAMIC ACID-5'-MONOPHOSPHATE DB08845, Oxogluric acid DB03629, Pyridoxal-5'-Phosphate-N-Oxide DB02981, Vitamin B6 Complexed with 2-Amino-Hexanoic Acid DB03662, Vitamin B6 Complexed with 2-Amino-Pentanoic Acid |
2D gel databases
SWISS-2DPAGEi | P00509 |
Proteomic databases
jPOSTi | P00509 |
PaxDbi | P00509 |
PRIDEi | P00509 |
Genome annotation databases
EnsemblBacteriai | AAC74014; AAC74014; b0928 BAA35674; BAA35674; BAA35674 |
GeneIDi | 57728339 945553 |
KEGGi | ecj:JW0911 eco:b0928 |
PATRICi | fig|1411691.4.peg.1348 |
Organism-specific databases
EchoBASEi | EB0094 |
Phylogenomic databases
eggNOGi | COG1448, Bacteria |
HOGENOMi | CLU_032440_1_2_6 |
InParanoidi | P00509 |
PhylomeDBi | P00509 |
Enzyme and pathway databases
BioCyci | EcoCyc:ASPAMINOTRANS-MONOMER MetaCyc:ASPAMINOTRANS-MONOMER |
BRENDAi | 2.6.1.1, 2026 |
SABIO-RKi | P00509 |
Miscellaneous databases
EvolutionaryTracei | P00509 |
PROi | PR:P00509 |
Family and domain databases
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
InterProi | View protein in InterPro IPR004839, Aminotransferase_I/II IPR000796, Asp_trans IPR004838, NHTrfase_class1_PyrdxlP-BS IPR015424, PyrdxlP-dep_Trfase IPR015422, PyrdxlP-dep_Trfase_dom1 IPR015421, PyrdxlP-dep_Trfase_major |
PANTHERi | PTHR11879, PTHR11879, 1 hit |
Pfami | View protein in Pfam PF00155, Aminotran_1_2, 1 hit |
PRINTSi | PR00799, TRANSAMINASE |
SUPFAMi | SSF53383, SSF53383, 1 hit |
PROSITEi | View protein in PROSITE PS00105, AA_TRANSFER_CLASS_1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | AAT_ECOLI | |
Accessioni | P00509Primary (citable) accession number: P00509 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | July 21, 1986 | |
Last modified: | April 7, 2021 | |
This is version 200 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families