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Entry version 160 (02 Jun 2021)
Sequence version 2 (11 Jul 2002)
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Protein

Aspartokinase

Gene

lysC

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
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

Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine.

2 Publications

<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

Feedback inhibition by lysine and threonine, but he enzyme is moderately inhibited by lysine alone, and threonine alone has no effect.2 Publications

<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. 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.

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-homoserine from L-aspartate. This subpathway is part of the pathway L-methionine biosynthesis via de novo 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 L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Pathwayi: L-threonine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-threonine from L-aspartate. This subpathway is part of the pathway L-threonine biosynthesis, 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 L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei7Contribution to the catalysisBy similarity1
<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 sitei41ATPBy similarity1
Binding sitei74SubstrateBy similarity1
Sitei74Contribution to the catalysisBy similarity1
Binding sitei154Substrate1
Binding sitei210ATPBy similarity1
Binding sitei274SubstrateBy similarity1
Binding sitei298Substrate1

<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

GO - Biological processi

<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 functionKinase, Transferase
Biological processAmino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
CORYNE:G18NG-9806-MONOMER
MetaCyc:MONOMER-6461
MetaCyc:MONOMER-6462

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.2.4, 960

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

More...
UniPathwayi
UPA00034;UER00015
UPA00050;UER00461
UPA00051;UER00462

<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:
Aspartokinase (EC:2.7.2.4)
Alternative name(s):
Aspartate kinase
<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
Ordered Locus Names:Cgl0251, cg0306
<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>OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
<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 identifieri196627 [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 lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
<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
  • UP000000582 <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

<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>Mutagenesisi277G → A: Change in the inhibitory profile upon addition of threonine. 1 Publication1
Mutagenesisi279A → V: Absence of inhibition upon addition of threonine and lysine or lysine alone. 1 Publication1
Mutagenesisi298Q → A: Change in the inhibitory profile and absence of dimerization upon addition of threonine. 1 Publication1
Mutagenesisi301S → F: Absence of inhibition upon addition of threonine and lysine or lysine alone. 2 Publications1
Mutagenesisi301S → Y: Feedback-resistant and enhanced expression of the asd gene. 2 Publications1
Mutagenesisi360V → A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine. 1 Publication1
Mutagenesisi361T → A: Change in the inhibitory profile and absence of dimerization upon addition of threonine. 1 Publication1
Mutagenesisi363E → A: Change in the inhibitory profile and absence of dimerization upon addition of threonine. 1 Publication1
Mutagenesisi364F → A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine. 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 '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_00000023791 – 421AspartokinaseAdd BLAST421

<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

Tetramer consisting of 2 isoforms Alpha (catalytic and regulation) and of a homodimer of 2 isoforms Beta (regulation). The dimerization of the beta isoforms is stabilized by the bonding of threonine.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
196627.cg0306

<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

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P26512

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
P26512

<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>Domaini267 – 343ACT 1PROSITE-ProRule annotationAdd BLAST77
Domaini349 – 421ACT 2PROSITE-ProRule annotationAdd BLAST73

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>Regioni7 – 10ATP bindingBy similarity4
Regioni25 – 30Substrate bindingBy similarity6
Regioni45 – 49Substrate binding5
Regioni125 – 126Substrate bindingBy similarity2
Regioni151 – 154Substrate bindingBy similarity4
Regioni174 – 175ATP bindingBy similarity2
Regioni180 – 185ATP bindingBy similarity6
Regioni274 – 279Substrate binding6
Regioni292 – 294Substrate binding3
Regioni360 – 361Substrate binding2
Regioni374 – 375Substrate binding2
Regioni381 – 382Substrate binding2

<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

Keywords - Domaini

Repeat

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_3_2_11

Identification of Orthologs from Complete Genome Data

More...
OMAi
DMIVQTI

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04261, AAK_AKii-LysC-BS, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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
IPR041740, AKii-LysC-BS
IPR001048, Asp/Glu/Uridylate_kinase
IPR005260, Asp_kin_monofn
IPR001341, Asp_kinase
IPR018042, Aspartate_kinase_CS
IPR027795, CASTOR_ACT_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00696, AA_kinase, 1 hit
PF01842, ACT, 1 hit
PF13840, ACT_7, 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, 2 hits
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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform Alpha (identifier: P26512-1) [UniParc]FASTAAdd to basket
Also known as: Aspartokinase subunit alpha

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MALVVQKYGG SSLESAERIR NVAERIVATK KAGNDVVVVC SAMGDTTDEL
60 70 80 90 100
LELAAAVNPV PPAREMDMLL TAGERISNAL VAMAIESLGA EAQSFTGSQA
110 120 130 140 150
GVLTTERHGN ARIVDVTPGR VREALDEGKI CIVAGFQGVN KETRDVTTLG
160 170 180 190 200
RGGSDTTAVA LAAALNADVC EIYSDVDGVY TADPRIVPNA QKLEKLSFEE
210 220 230 240 250
MLELAAVGSK ILVLRSVEYA RAFNVPLRVR SSYSNDPGTL IAGSMEDIPV
260 270 280 290 300
EEAVLTGVAT DKSEAKVTVL GISDKPGEAA KVFRALADAE INIDMVLQNV
310 320 330 340 350
SSVEDGTTDI TFTCPRSDGR RAMEILKKLQ VQGNWTNVLY DDQVGKVSLV
360 370 380 390 400
GAGMKSHPGV TAEFMEALRD VNVNIELIST SEIRISVLIR EDDLDAAARA
410 420
LHEQFQLGGE DEAVVYAGTG R
Length:421
Mass (Da):44,755
Last modified:July 11, 2002 - 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:iE36B4D0081DE0827
GO
Isoform Beta (identifier: P26512-2) [UniParc]FASTAAdd to basket
Also known as: Aspartokinase subunit beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-249: Missing.
     250-250: V → M

Show »
Length:172
Mass (Da):18,537
Checksum:i140CBE126C299ED6
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 conflicti40C → V in CAA40502 (PubMed:1956296).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0186591 – 249Missing in isoform Beta. CuratedAdd BLAST249
Alternative sequenceiVSP_018660250V → M in isoform Beta. 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
X57226 Genomic DNA Translation: CAA40502.1
X57226 Genomic DNA Translation: CAA40503.1
BA000036 Genomic DNA Translation: BAB97644.1
BX927148 Genomic DNA Translation: CAF18822.1
X70959 Genomic DNA Translation: CAA50296.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I40723
S15276

NCBI Reference Sequences

More...
RefSeqi
NP_599504.1, NC_003450.3
WP_003855724.1, NC_006958.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAB97644; BAB97644; BAB97644

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
58310306

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cgb:cg0306
cgl:NCgl0247

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|196627.13.peg.255

Keywords - Coding sequence diversityi

Alternative initiation

<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
X57226 Genomic DNA Translation: CAA40502.1
X57226 Genomic DNA Translation: CAA40503.1
BA000036 Genomic DNA Translation: BAB97644.1
BX927148 Genomic DNA Translation: CAF18822.1
X70959 Genomic DNA Translation: CAA50296.1
PIRiI40723
S15276
RefSeqiNP_599504.1, NC_003450.3
WP_003855724.1, NC_006958.1

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
2DTJX-ray1.58A/B250-421[»]
3AAWX-ray2.50A/C1-421[»]
3AB2X-ray2.59A/C/E/G/I/K/M/O1-421[»]
B/D/F/H/J/L/N/P251-421[»]
3AB4X-ray2.47A/C/E/G/I/K/M/O1-421[»]
B/D/F/H/J/L/N/P251-421[»]
SMRiP26512
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi196627.cg0306

Genome annotation databases

EnsemblBacteriaiBAB97644; BAB97644; BAB97644
GeneIDi58310306
KEGGicgb:cg0306
cgl:NCgl0247
PATRICifig|196627.13.peg.255

Phylogenomic databases

eggNOGiCOG0527, Bacteria
HOGENOMiCLU_009116_3_2_11
OMAiDMIVQTI

Enzyme and pathway databases

UniPathwayiUPA00034;UER00015
UPA00050;UER00461
UPA00051;UER00462
BioCyciCORYNE:G18NG-9806-MONOMER
MetaCyc:MONOMER-6461
MetaCyc:MONOMER-6462
BRENDAi2.7.2.4, 960

Miscellaneous databases

EvolutionaryTraceiP26512

Family and domain databases

CDDicd04261, AAK_AKii-LysC-BS, 1 hit
Gene3Di3.40.1160.10, 1 hit
InterProiView protein in InterPro
IPR036393, AceGlu_kinase-like_sf
IPR002912, ACT_dom
IPR041740, AKii-LysC-BS
IPR001048, Asp/Glu/Uridylate_kinase
IPR005260, Asp_kin_monofn
IPR001341, Asp_kinase
IPR018042, Aspartate_kinase_CS
IPR027795, CASTOR_ACT_dom
PfamiView protein in Pfam
PF00696, AA_kinase, 1 hit
PF01842, ACT, 1 hit
PF13840, ACT_7, 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, 2 hits
PS00324, ASPARTOKINASE, 1 hit

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 nameiAK_CORGL
<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: P26512
Secondary accession number(s): Q59286
<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: August 1, 1992
Last sequence update: July 11, 2002
Last modified: June 2, 2021
This is version 160 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, 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
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