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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)DescriptionActionsGraphical viewLength
Binding sitei45Substrate1
Binding sitei119Substrate1
Binding sitei227ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei232ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi8 – 11ATP4
Nucleotide bindingi221 – 222ATP2
Nucleotide bindingi257 – 258ATP2

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000666762 – 449Lysine-sensitive aspartokinase 3Add BLAST448

Proteomic databases

PaxDbiP08660.
PRIDEiP08660.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi4261955. 8 interactors.
STRINGi511145.b4024.

Structurei

Secondary structure

1449
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi12 – 14Combined sources3
Helixi17 – 27Combined sources11
Beta strandi33 – 38Combined sources6
Helixi44 – 51Combined sources8
Helixi57 – 75Combined sources19
Beta strandi78 – 80Combined sources3
Helixi82 – 102Combined sources21
Helixi108 – 131Combined sources24
Turni132 – 134Combined sources3
Beta strandi137 – 139Combined sources3
Helixi142 – 144Combined sources3
Helixi159 – 169Combined sources11
Helixi171 – 176Combined sources6
Beta strandi177 – 187Combined sources11
Beta strandi193 – 195Combined sources3
Helixi200 – 211Combined sources12
Beta strandi215 – 229Combined sources15
Turni231 – 233Combined sources3
Beta strandi239 – 244Combined sources6
Helixi245 – 253Combined sources9
Turni261 – 263Combined sources3
Helixi264 – 270Combined sources7
Beta strandi274 – 280Combined sources7
Helixi282 – 284Combined sources3
Beta strandi287 – 291Combined sources5
Beta strandi298 – 313Combined sources16
Helixi316 – 318Combined sources3
Helixi321 – 328Combined sources8
Turni329 – 336Combined sources8
Beta strandi340 – 345Combined sources6
Beta strandi348 – 353Combined sources6
Helixi368 – 377Combined sources10
Beta strandi380 – 395Combined sources16
Beta strandi399 – 401Combined sources3
Helixi402 – 407Combined sources6
Helixi408 – 410Combined sources3
Beta strandi417 – 419Combined sources3
Beta strandi426 – 432Combined sources7
Helixi433 – 435Combined sources3
Helixi436 – 448Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP08660.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini313 – 394ACTPROSITE-ProRule annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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)DescriptionActionsGraphical viewLength
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:
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J0WX-ray2.50A1-449[»]
2J0XX-ray2.80A/B1-449[»]
ProteinModelPortaliP08660.
SMRiP08660.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261955. 8 interactors.
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: November 2, 2016
This is version 141 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.