Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Sitei7Contribution to the catalysisBy similarity1
Binding sitei41ATPBy similarity1
Binding sitei74SubstrateBy similarity1
Sitei74Contribution to the catalysisBy similarity1
Binding sitei154Substrate1
Binding sitei210ATPBy similarity1
Binding sitei274SubstrateBy similarity1
Binding sitei298Substrate1

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

BioCyciCORYNE:G18NG-9806-MONOMER.
MetaCyc: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)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000023791 – 421AspartokinaseAdd BLAST421

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

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi11 – 13Combined sources3
Helixi16 – 31Combined sources16
Beta strandi35 – 40Combined sources6
Helixi46 – 57Combined sources12
Helixi63 – 87Combined sources25
Beta strandi92 – 94Combined sources3
Helixi118 – 126Combined sources9
Beta strandi130 – 134Combined sources5
Beta strandi142 – 150Combined sources9
Helixi154 – 165Combined sources12
Beta strandi168 – 175Combined sources8
Beta strandi180 – 182Combined sources3
Turni184 – 186Combined sources3
Beta strandi194 – 196Combined sources3
Helixi198 – 206Combined sources9
Helixi214 – 222Combined sources9
Beta strandi227 – 234Combined sources8
Beta strandi239 – 241Combined sources3
Helixi245 – 247Combined sources3
Turni250 – 252Combined sources3
Beta strandi254 – 261Combined sources8
Beta strandi263 – 273Combined sources11
Helixi278 – 288Combined sources11
Beta strandi295 – 298Combined sources4
Turni303 – 305Combined sources3
Beta strandi307 – 315Combined sources9
Helixi316 – 318Combined sources3
Helixi319 – 327Combined sources9
Turni328 – 334Combined sources7
Beta strandi336 – 342Combined sources7
Beta strandi344 – 352Combined sources9
Helixi358 – 370Combined sources13
Beta strandi377 – 381Combined sources5
Beta strandi384 – 390Combined sources7
Helixi391 – 393Combined sources3
Helixi394 – 405Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP26512.
SMRiP26512.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26512.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini267 – 343ACT 1PROSITE-ProRule annotationAdd BLAST77
Domaini349 – 421ACT 2PROSITE-ProRule annotationAdd BLAST73

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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)DescriptionActionsGraphical viewLength
Sequence conflicti40C → V in CAA40502 (PubMed:1956296).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0186591 – 249Missing in isoform Beta. CuratedAdd BLAST249
Alternative sequenceiVSP_018660250V → M in isoform Beta. Curated1

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
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[»]
ProteinModelPortaliP26512.
SMRiP26512.
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.
BioCyciCORYNE:G18NG-9806-MONOMER.
MetaCyc: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: November 2, 2016
This is version 135 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.