Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P08660 (AK3_ECOLI)

Entry version 168 (07 Apr 2021)
Sequence version 2 (01 Oct 1993)
Previous versions | rss
Add a publicationFeedback
Protein

Lysine-sensitive aspartokinase 3

Gene

lysC

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

Miscellaneous

Aspartokinases I and II also catalyze the same reaction(s).

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Synthesis and activity are sensitive to the allosteric inhibitor lysine, one of the end metabolites of the aspartic acid family branched pathway.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 1 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Aspartokinase (lysC), Lysine-sensitive aspartokinase 3 (lysC), Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional aspartokinase/homoserine dehydrogenase (FAZ83_20520), Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
  2. Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd)
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA), 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
  4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB), 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei45Substrate1
Binding sitei119Substrate1
Binding sitei227ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei232ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi8 – 11ATP4
Nucleotide bindingi221 – 222ATP2
Nucleotide bindingi257 – 258ATP2

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAllosteric enzyme, Kinase, Transferase
Biological processAmino-acid biosynthesis, Lysine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P08660

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00034;UER00015

<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%5Fand%5Ftaxonomy%5Fsection">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:
Lysine-sensitive aspartokinase 3 (EC:2.7.2.4)
Alternative name(s):
Aspartate kinase III
Short name:
AKIII
Lysine-sensitive aspartokinase III
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:lysC
Synonyms:apk
Ordered Locus Names:b4024, JW3984
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi8K → R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition. 1 Publication1
Mutagenesisi119E → D: Increases KM for aspartate about 3000-fold. 1 Publication1
Mutagenesisi198R → K: Increases KM for aspartate about 200-fold. 1 Publication1
Mutagenesisi202D → E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition. 1 Publication1

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000666762 – 449Lysine-sensitive aspartokinase 3Add BLAST448

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P08660

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

More...PaxDbi		P08660

PRoteomics IDEntifications database

More...PRIDEi		P08660

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. In the inactive form a homotetramer is formed.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261955, 8 interactors

STRING: functional protein association networks

More...STRINGi		511145.b4024

<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

1449
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

The Protein Circular Dichroism Data Bank

More...PCDDBi		P08660

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

More...SMRi		P08660

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08660

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini313 – 394ACTPROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 245AspartokinaseAdd BLAST244
Regioni198 – 201Substrate binding4
Regioni246 – 449InterfaceAdd BLAST204
Regioni299 – 449Required for homodimerizationAdd BLAST151
Regioni318 – 321Allosteric inhibitor binding 14
Regioni324 – 325Allosteric inhibitor binding 12
Regioni338 – 340Allosteric inhibitor binding 23
Regioni345 – 346Allosteric inhibitor binding 12

<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

Belongs to the aspartokinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0527, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_009116_6_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08660

Database for complete collections of gene phylogenies

More...PhylomeDBi		P08660

Family and domain databases

Conserved Domains Database

More...CDDi		cd04258, AAK_AKiii-LysC-EC, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.120.1320, 1 hit
3.40.1160.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036393, AceGlu_kinase-like_sf
IPR002912, ACT_dom
IPR041745, AKiii-LysC-EC
IPR001048, Asp/Glu/Uridylate_kinase
IPR005260, Asp_kin_monofn
IPR001341, Asp_kinase
IPR042199, AsparK_Bifunc_asparK/hSer_DH
IPR018042, Aspartate_kinase_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00696, AA_kinase, 1 hit
PF01842, ACT, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000726, Asp_kin, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53633, SSF53633, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00656, asp_kin_monofn, 1 hit
TIGR00657, asp_kinases, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51671, ACT, 1 hit
PS00324, ASPARTOKINASE, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P08660-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEIVVSKFG GTSVADFDAM NRSADIVLSD ANVRLVVLSA SAGITNLLVA 
        60         70         80         90        100
LAEGLEPGER FEKLDAIRNI QFAILERLRY PNVIREEIER LLENITVLAE 
       110        120        130        140        150
AAALATSPAL TDELVSHGEL MSTLLFVEIL RERDVQAQWF DVRKVMRTND 
       160        170        180        190        200
RFGRAEPDIA ALAELAALQL LPRLNEGLVI TQGFIGSENK GRTTTLGRGG 
       210        220        230        240        250
SDYTAALLAE ALHASRVDIW TDVPGIYTTD PRVVSAAKRI DEIAFAEAAE 
       260        270        280        290        300
MATFGAKVLH PATLLPAVRS DIPVFVGSSK DPRAGGTLVC NKTENPPLFR 
       310        320        330        340        350
ALALRRNQTL LTLHSLNMLH SRGFLAEVFG ILARHNISVD LITTSEVSVA 
       360        370        380        390        400
LTLDTTGSTS TGDTLLTQSL LMELSALCRV EVEEGLALVA LIGNDLSKAC 
       410        420        430        440 
GVGKEVFGVL EPFNIRMICY GASSHNLCFL VPGEDAEQVV QKLHSNLFE
Length:449
Mass (Da):48,532
Last modified:October 1, 1993 - v2
<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:i5B41CE3A6E4D984B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti14 – 15VA → AS in CAA24910 (PubMed:6312411).Curated2
Sequence conflicti20M → E in CAA24910 (PubMed:6312411).Curated1
Sequence conflicti58G → C in AAA24095 (PubMed:3003049).Curated1
Sequence conflicti401G → A in AAA24095 (PubMed:3003049).Curated1

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
M11812 Genomic DNA Translation: AAA24095.1
U00006 Genomic DNA Translation: AAC43118.1
U00096 Genomic DNA Translation: AAC76994.1
AP009048 Genomic DNA Translation: BAE78026.1
X00008 Genomic DNA Translation: CAA24910.1

Protein sequence database of the Protein Information Resource

More...PIRi		G65209, KIECD3

NCBI Reference Sequences

More...RefSeqi		NP_418448.1, NC_000913.3
WP_001290310.1, NZ_SSZK01000049.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76994; AAC76994; b4024
BAE78026; BAE78026; BAE78026

Database of genes from NCBI RefSeq genomes

More...GeneIDi		57730519
948531

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3984
eco:b4024

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2689

<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
M11812 Genomic DNA Translation: AAA24095.1
U00006 Genomic DNA Translation: AAC43118.1
U00096 Genomic DNA Translation: AAC76994.1
AP009048 Genomic DNA Translation: BAE78026.1
X00008 Genomic DNA Translation: CAA24910.1
PIRiG65209, KIECD3
RefSeqiNP_418448.1, NC_000913.3
WP_001290310.1, NZ_SSZK01000049.1

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
2J0WX-ray2.50A1-449[»]
2J0XX-ray2.80A/B1-449[»]
PCDDBiP08660
SMRiP08660
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261955, 8 interactors
STRINGi511145.b4024

Proteomic databases

jPOSTiP08660
PaxDbiP08660
PRIDEiP08660

Genome annotation databases

EnsemblBacteriaiAAC76994; AAC76994; b4024
BAE78026; BAE78026; BAE78026
GeneIDi57730519
948531
KEGGiecj:JW3984
eco:b4024
PATRICifig|1411691.4.peg.2689

Organism-specific databases

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

More...EchoBASEi		EB0545

Phylogenomic databases

eggNOGiCOG0527, Bacteria
HOGENOMiCLU_009116_6_0_6
InParanoidiP08660
PhylomeDBiP08660

Enzyme and pathway databases

UniPathwayiUPA00034;UER00015
BioCyciEcoCyc:ASPKINIII-MONOMER
MetaCyc:ASPKINIII-MONOMER
SABIO-RKiP08660

Miscellaneous databases

EvolutionaryTraceiP08660

Protein Ontology

More...PROi		PR:P08660

Family and domain databases

CDDicd04258, AAK_AKiii-LysC-EC, 1 hit
Gene3Di1.20.120.1320, 1 hit
3.40.1160.10, 1 hit
InterProiView protein in InterPro
IPR036393, AceGlu_kinase-like_sf
IPR002912, ACT_dom
IPR041745, AKiii-LysC-EC
IPR001048, Asp/Glu/Uridylate_kinase
IPR005260, Asp_kin_monofn
IPR001341, Asp_kinase
IPR042199, AsparK_Bifunc_asparK/hSer_DH
IPR018042, Aspartate_kinase_CS
PfamiView protein in Pfam
PF00696, AA_kinase, 1 hit
PF01842, ACT, 1 hit
PIRSFiPIRSF000726, Asp_kin, 1 hit
SUPFAMiSSF53633, SSF53633, 1 hit
TIGRFAMsiTIGR00656, asp_kin_monofn, 1 hit
TIGR00657, asp_kinases, 1 hit
PROSITEiView protein in PROSITE
PS51671, ACT, 1 hit
PS00324, ASPARTOKINASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 nameiAK3_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: P08660
Secondary accession number(s): Q2M6T0
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 1, 1993
Last modified: April 7, 2021
This is version 168 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again