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Protein

Aspartokinase

Gene

lysC

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

Enzyme regulationi

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

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)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
  4. 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.

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.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Aspartokinase (lysC)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Homoserine dehydrogenase (hom)
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.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Aspartokinase (lysC)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Homoserine dehydrogenase (hom)
  4. Homoserine kinase (thrB)
  5. Threonine synthase (thrC)
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei7 – 71Contribution to the catalysisBy similarity
Binding sitei41 – 411ATPBy similarity
Binding sitei74 – 741SubstrateBy similarity
Sitei74 – 741Contribution to the catalysisBy similarity
Binding sitei154 – 1541Substrate
Binding sitei210 – 2101ATPBy similarity
Binding sitei274 – 2741SubstrateBy similarity
Binding sitei298 – 2981Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-6461.
MetaCyc:MONOMER-6462.
BRENDAi2.7.2.4. 960.
UniPathwayiUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartokinase (EC:2.7.2.4)
Alternative name(s):
Aspartate kinase
Gene namesi
Name:lysC
Ordered Locus Names:Cgl0251, cg0306
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi277 – 2771G → A: Change in the inhibitory profile upon addition of threonine. 1 Publication
Mutagenesisi279 – 2791A → V: Absence of inhibition upon addition of threonine and lysine or lysine alone. 1 Publication
Mutagenesisi298 – 2981Q → A: Change in the inhibitory profile and absence of dimerization upon addition of threonine. 1 Publication
Mutagenesisi301 – 3011S → F: Absence of inhibition upon addition of threonine and lysine or lysine alone. 2 Publications
Mutagenesisi301 – 3011S → Y: Feedback-resistant and enhanced expression of the asd gene. 2 Publications
Mutagenesisi360 – 3601V → A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine. 1 Publication
Mutagenesisi361 – 3611T → A: Change in the inhibitory profile and absence of dimerization upon addition of threonine. 1 Publication
Mutagenesisi363 – 3631E → A: Change in the inhibitory profile and absence of dimerization upon addition of threonine. 1 Publication
Mutagenesisi364 – 3641F → A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421AspartokinasePRO_0000002379Add
BLAST

Interactioni

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

STRINGi196627.cg0306.

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi11 – 133Combined sources
Helixi16 – 3116Combined sources
Beta strandi35 – 406Combined sources
Helixi46 – 5712Combined sources
Helixi63 – 8725Combined sources
Beta strandi92 – 943Combined sources
Helixi118 – 1269Combined sources
Beta strandi130 – 1345Combined sources
Beta strandi142 – 1509Combined sources
Helixi154 – 16512Combined sources
Beta strandi168 – 1758Combined sources
Beta strandi180 – 1823Combined sources
Turni184 – 1863Combined sources
Beta strandi194 – 1963Combined sources
Helixi198 – 2069Combined sources
Helixi214 – 2229Combined sources
Beta strandi227 – 2348Combined sources
Beta strandi239 – 2413Combined sources
Helixi245 – 2473Combined sources
Turni250 – 2523Combined sources
Beta strandi254 – 2618Combined sources
Beta strandi263 – 27311Combined sources
Helixi278 – 28811Combined sources
Beta strandi295 – 2984Combined sources
Turni303 – 3053Combined sources
Beta strandi307 – 3159Combined sources
Helixi316 – 3183Combined sources
Helixi319 – 3279Combined sources
Turni328 – 3347Combined sources
Beta strandi336 – 3427Combined sources
Beta strandi344 – 3529Combined sources
Helixi358 – 37013Combined sources
Beta strandi377 – 3815Combined sources
Beta strandi384 – 3907Combined sources
Helixi391 – 3933Combined sources
Helixi394 – 40512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP26512.
SMRiP26512. Positions 253-416.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26512.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 34377ACT 1PROSITE-ProRule annotationAdd
BLAST
Domaini349 – 42173ACT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 104ATP bindingBy similarity
Regioni25 – 306Substrate bindingBy similarity
Regioni45 – 495Substrate binding
Regioni125 – 1262Substrate bindingBy similarity
Regioni151 – 1544Substrate bindingBy similarity
Regioni174 – 1752ATP bindingBy similarity
Regioni180 – 1856ATP bindingBy similarity
Regioni274 – 2796Substrate binding
Regioni292 – 2943Substrate binding
Regioni360 – 3612Substrate binding
Regioni374 – 3752Substrate binding
Regioni381 – 3822Substrate binding

Sequence similaritiesi

Belongs to the aspartokinase family.Curated
Contains 2 ACT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CFH. Bacteria.
COG0527. LUCA.
HOGENOMiHOG000293093.
KOiK00928.
OMAiINIMMIS.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
InterProiIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005260. Asp_kin_monofn.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR027795. GATS-like_ACT_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01842. ACT. 1 hit.
PF13840. ACT_7. 1 hit.
[Graphical view]
PIRSFiPIRSF000726. Asp_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00656. asp_kin_monofn. 1 hit.
TIGR00657. asp_kinases. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 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 'canonical' 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
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401C → V in CAA40502 (PubMed:1956296).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 249249Missing in isoform Beta. CuratedVSP_018659Add
BLAST
Alternative sequencei250 – 2501V → M in isoform Beta. CuratedVSP_018660

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. [P26512-1]
WP_003855724.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB97644; BAB97644; BAB97644.
CAF18822; CAF18822; cg0306.
GeneIDi1021294.
KEGGicgb:cg0306.
cgl:NCgl0247.
PATRICi21492564. VBICorGlu203724_0255.

Keywords - Coding sequence diversityi

Alternative initiation

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. [P26512-1]
WP_003855724.1. NC_006958.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP26512.
SMRiP26512. Positions 253-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg0306.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB97644; BAB97644; BAB97644.
CAF18822; CAF18822; cg0306.
GeneIDi1021294.
KEGGicgb:cg0306.
cgl:NCgl0247.
PATRICi21492564. VBICorGlu203724_0255.

Phylogenomic databases

eggNOGiENOG4105CFH. Bacteria.
COG0527. LUCA.
HOGENOMiHOG000293093.
KOiK00928.
OMAiINIMMIS.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.
BioCyciMetaCyc:MONOMER-6461.
MetaCyc:MONOMER-6462.
BRENDAi2.7.2.4. 960.

Miscellaneous databases

EvolutionaryTraceiP26512.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
InterProiIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005260. Asp_kin_monofn.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR027795. GATS-like_ACT_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01842. ACT. 1 hit.
PF13840. ACT_7. 1 hit.
[Graphical view]
PIRSFiPIRSF000726. Asp_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00656. asp_kin_monofn. 1 hit.
TIGR00657. asp_kinases. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAK_CORGL
AccessioniPrimary (citable) accession number: P26512
Secondary accession number(s): Q59286
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 11, 2002
Last modified: September 7, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.