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Protein

Lysine-sensitive aspartokinase 3

Gene

lysC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme 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

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. Lysine-sensitive aspartokinase 3 (lysC), Bifunctional aspartokinase/homoserine dehydrogenase 1 (thrA), Bifunctional aspartokinase/homoserine dehydrogenase 2 (metL)
  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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451Substrate
Binding sitei119 – 1191Substrate
Binding sitei227 – 2271ATP; via amide nitrogen and carbonyl oxygen
Binding sitei232 – 2321ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 114ATP
Nucleotide bindingi221 – 2222ATP
Nucleotide bindingi257 – 2582ATP

GO - Molecular functioni

  • amino acid binding Source: InterPro
  • aspartate kinase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • homoserine biosynthetic process Source: EcoCyc
  • lysine biosynthetic process via diaminopimelate Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ASPKINIII-MONOMER.
ECOL316407:JW3984-MONOMER.
MetaCyc:ASPKINIII-MONOMER.
SABIO-RKP08660.
UniPathwayiUPA00034; UER00015.

Names & Taxonomyi

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
Gene namesi
Name:lysC
Synonyms:apk
Ordered Locus Names:b4024, JW3984
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10550. lysC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81K → R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition. 1 Publication
Mutagenesisi119 – 1191E → D: Increases KM for aspartate about 3000-fold. 1 Publication
Mutagenesisi198 – 1981R → K: Increases KM for aspartate about 200-fold. 1 Publication
Mutagenesisi202 – 2021D → E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 449448Lysine-sensitive aspartokinase 3PRO_0000066676Add
BLAST

Proteomic databases

PaxDbiP08660.
PRIDEiP08660.

Interactioni

Subunit structurei

Homodimer. In the inactive form a homotetramer is formed.2 Publications

Protein-protein interaction databases

BioGridi4261955. 8 interactions.
STRINGi511145.b4024.

Structurei

Secondary structure

1
449
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi12 – 143Combined sources
Helixi17 – 2711Combined sources
Beta strandi33 – 386Combined sources
Helixi44 – 518Combined sources
Helixi57 – 7519Combined sources
Beta strandi78 – 803Combined sources
Helixi82 – 10221Combined sources
Helixi108 – 13124Combined sources
Turni132 – 1343Combined sources
Beta strandi137 – 1393Combined sources
Helixi142 – 1443Combined sources
Helixi159 – 16911Combined sources
Helixi171 – 1766Combined sources
Beta strandi177 – 18711Combined sources
Beta strandi193 – 1953Combined sources
Helixi200 – 21112Combined sources
Beta strandi215 – 22915Combined sources
Turni231 – 2333Combined sources
Beta strandi239 – 2446Combined sources
Helixi245 – 2539Combined sources
Turni261 – 2633Combined sources
Helixi264 – 2707Combined sources
Beta strandi274 – 2807Combined sources
Helixi282 – 2843Combined sources
Beta strandi287 – 2915Combined sources
Beta strandi298 – 31316Combined sources
Helixi316 – 3183Combined sources
Helixi321 – 3288Combined sources
Turni329 – 3368Combined sources
Beta strandi340 – 3456Combined sources
Beta strandi348 – 3536Combined sources
Helixi368 – 37710Combined sources
Beta strandi380 – 39516Combined sources
Beta strandi399 – 4013Combined sources
Helixi402 – 4076Combined sources
Helixi408 – 4103Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi426 – 4327Combined sources
Helixi433 – 4353Combined sources
Helixi436 – 44813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0WX-ray2.50A1-449[»]
2J0XX-ray2.80A/B1-449[»]
ProteinModelPortaliP08660.
SMRiP08660. Positions 3-449.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08660.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini313 – 39482ACTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 245244AspartokinaseAdd
BLAST
Regioni198 – 2014Substrate binding
Regioni246 – 449204InterfaceAdd
BLAST
Regioni299 – 449151Required for homodimerizationAdd
BLAST
Regioni318 – 3214Allosteric inhibitor binding 1
Regioni324 – 3252Allosteric inhibitor binding 1
Regioni338 – 3403Allosteric inhibitor binding 2
Regioni345 – 3462Allosteric inhibitor binding 1

Sequence similaritiesi

Belongs to the aspartokinase family.Curated
Contains 1 ACT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CFH. Bacteria.
COG0527. LUCA.
HOGENOMiHOG000293094.
InParanoidiP08660.
KOiK00928.
OMAiMICFGAN.
PhylomeDBiP08660.

Family and domain databases

Gene3Di3.40.1160.10. 2 hits.
InterProiIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005260. Asp_kin_monofn.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01842. ACT. 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. 1 hit.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i5B41CE3A6E4D984B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152VA → AS in CAA24910 (PubMed:6312411).Curated
Sequence conflicti20 – 201M → E in CAA24910 (PubMed:6312411).Curated
Sequence conflicti58 – 581G → C in AAA24095 (PubMed:3003049).Curated
Sequence conflicti401 – 4011G → A in AAA24095 (PubMed:3003049).Curated

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_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76994; AAC76994; b4024.
BAE78026; BAE78026; BAE78026.
GeneIDi948531.
KEGGiecj:JW3984.
eco:b4024.
PATRICi32123577. VBIEscCol129921_4137.

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_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0WX-ray2.50A1-449[»]
2J0XX-ray2.80A/B1-449[»]
ProteinModelPortaliP08660.
SMRiP08660. Positions 3-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261955. 8 interactions.
STRINGi511145.b4024.

Proteomic databases

PaxDbiP08660.
PRIDEiP08660.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76994; AAC76994; b4024.
BAE78026; BAE78026; BAE78026.
GeneIDi948531.
KEGGiecj:JW3984.
eco:b4024.
PATRICi32123577. VBIEscCol129921_4137.

Organism-specific databases

EchoBASEiEB0545.
EcoGeneiEG10550. lysC.

Phylogenomic databases

eggNOGiENOG4105CFH. Bacteria.
COG0527. LUCA.
HOGENOMiHOG000293094.
InParanoidiP08660.
KOiK00928.
OMAiMICFGAN.
PhylomeDBiP08660.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00015.
BioCyciEcoCyc:ASPKINIII-MONOMER.
ECOL316407:JW3984-MONOMER.
MetaCyc:ASPKINIII-MONOMER.
SABIO-RKP08660.

Miscellaneous databases

EvolutionaryTraceiP08660.
PROiP08660.

Family and domain databases

Gene3Di3.40.1160.10. 2 hits.
InterProiIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005260. Asp_kin_monofn.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01842. ACT. 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. 1 hit.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAK3_ECOLI
AccessioniPrimary (citable) accession number: P08660
Secondary accession number(s): Q2M6T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 1, 1993
Last modified: September 7, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.