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Protein

Aspartate aminotransferase

Gene

aspC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei34Aspartate; via amide nitrogenCombined sources1
Binding sitei130AspartateCombined sources1
Binding sitei183AspartateCombined sources1
Binding sitei374AspartateCombined sources1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>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

GO - Biological processi

  • L-phenylalanine biosynthetic process Source: EcoliWiki
  • L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Source: EcoCyc

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminotransferase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:ASPAMINOTRANS-MONOMER
MetaCyc:ASPAMINOTRANS-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.6.1.1 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00509

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Aspartate aminotransferase (EC:2.6.1.11 Publication)
Short name:
AspAT
Alternative name(s):
Transaminase A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:aspC
Ordered Locus Names:b0928, JW0911
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10096 aspC

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02024 3-phenylpropionic acid
DB03553 Glutaric Acid
DB02758 Indolylpropionic Acid
DB03750 Isovaleric Acid
DB04299 Maleic Acid
DB04083 N'-Pyridoxyl-Lysine-5'-Monophosphate
DB01639 N-Methyl-Pyridoxal-5'-Phosphate
DB04765 N-PYRIDOXYL-2-METHYL-L-GLUTAMIC ACID-5'-MONOPHOSPHATE
DB04762 N-PYRIDOXYL-D-GLUTAMIC ACID-5'-MONOPHOSPHATE
DB03629 Pyridoxal-5'-Phosphate-N-Oxide
DB04467 Pyridoxyl-Alanine-5-Phosphate
DB02981 Vitamin B6 Complexed with 2-Amino-Hexanoic Acid
DB03662 Vitamin B6 Complexed with 2-Amino-Pentanoic Acid

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001238381 – 396Aspartate aminotransferaseAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei246N6-(pyridoxal phosphate)lysineCombined sources4 Publications1

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P00509

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P00509

PRoteomics IDEntifications database

More...
PRIDEi
P00509

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P00509

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260021, 28 interactors

Database of interacting proteins

More...
DIPi
DIP-9181N

Protein interaction database and analysis system

More...
IntActi
P00509, 4 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0998

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00509

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P00509

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00509

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CGF Bacteria
COG1448 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000185899

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00509

KEGG Orthology (KO)

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KOi
K00813

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00509

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.640.10, 1 hit
3.90.1150.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

The PANTHER Classification System

More...
PANTHERi
PTHR11879 PTHR11879, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00155 Aminotran_1_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00799 TRANSAMINASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53383 SSF53383, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00105 AA_TRANSFER_CLASS_1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9F0437E76DD4FC0F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
A00598 XNECD

NCBI Reference Sequences

More...
RefSeqi
NP_415448.1, NC_000913.3
WP_000462687.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74014; AAC74014; b0928
BAA35674; BAA35674; BAA35674

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945553

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0911
eco:b0928

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1348

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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-ray2.00A1-396[»]
1TOGX-ray2.31A/B1-396[»]
1TOIX-ray1.90A1-396[»]
1TOJX-ray1.90A1-396[»]
1TOKX-ray1.85A/B1-396[»]
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[»]
5T4LX-ray1.53A1-396[»]
5VWQX-ray1.80A/D/G/J1-396[»]
5VWRX-ray1.72A1-396[»]
ProteinModelPortaliP00509
SMRiP00509
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260021, 28 interactors
DIPiDIP-9181N
IntActiP00509, 4 interactors
STRINGi316385.ECDH10B_0998

Chemistry databases

DrugBankiDB02024 3-phenylpropionic acid
DB03553 Glutaric Acid
DB02758 Indolylpropionic Acid
DB03750 Isovaleric Acid
DB04299 Maleic Acid
DB04083 N'-Pyridoxyl-Lysine-5'-Monophosphate
DB01639 N-Methyl-Pyridoxal-5'-Phosphate
DB04765 N-PYRIDOXYL-2-METHYL-L-GLUTAMIC ACID-5'-MONOPHOSPHATE
DB04762 N-PYRIDOXYL-D-GLUTAMIC ACID-5'-MONOPHOSPHATE
DB03629 Pyridoxal-5'-Phosphate-N-Oxide
DB04467 Pyridoxyl-Alanine-5-Phosphate
DB02981 Vitamin B6 Complexed with 2-Amino-Hexanoic Acid
DB03662 Vitamin B6 Complexed with 2-Amino-Pentanoic Acid

2D gel databases

SWISS-2DPAGEiP00509

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
PATRICifig|1411691.4.peg.1348

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB0094
EcoGeneiEG10096 aspC

Phylogenomic databases

eggNOGiENOG4105CGF Bacteria
COG1448 LUCA
HOGENOMiHOG000185899
InParanoidiP00509
KOiK00813
PhylomeDBiP00509

Enzyme and pathway databases

BioCyciEcoCyc:ASPAMINOTRANS-MONOMER
MetaCyc:ASPAMINOTRANS-MONOMER
BRENDAi2.6.1.1 2026
SABIO-RKiP00509

Miscellaneous databases

EvolutionaryTraceiP00509

Protein Ontology

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PROi
PR:P00509

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
InterProiView 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
PANTHERiPTHR11879 PTHR11879, 1 hit
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
PRINTSiPR00799 TRANSAMINASE
SUPFAMiSSF53383 SSF53383, 1 hit
PROSITEiView protein in PROSITE
PS00105 AA_TRANSFER_CLASS_1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAAT_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00509
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: December 5, 2018
This is version 184 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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