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Protein

Aspartokinase 1, chloroplastic

Gene

AK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.

Catalytic activityi

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

Enzyme regulationi

Inhibited by S-adenosyl-L-methionine (SAM) and lysine in a synergistic manner. No inhibition by threonine, leucine or SAM alone, and no activation or inhibition by alanine, cysteine, isoleucine, serine, valine, methionine, glutamine, asparagine, glutamic acid or arginine.2 Publications

Kineticsi

K(cat) is 23.4/sec.

  1. KM=1700 µM for ATP1 Publication
  2. KM=2037 µM for aspartate1 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. AK1 (AXX17_At5g12690), Aspartokinase 2, chloroplastic (AK2), Aspartokinase (AXX17_At5g13510), Aspartokinase 1, chloroplastic (AK1), Aspartokinase 3, chloroplastic (AK3), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. 4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic (DHDPS1), 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic (DHDPS2)
    4. 4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic (DAPB2), 4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic (DAPB1)
    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. AK1 (AXX17_At5g12690), Aspartokinase 2, chloroplastic (AK2), Aspartokinase (AXX17_At5g13510), Aspartokinase 1, chloroplastic (AK1), Aspartokinase 3, chloroplastic (AK3), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase, Homoserine dehydrogenase (At5g21060), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    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. AK1 (AXX17_At5g12690), Aspartokinase 2, chloroplastic (AK2), Aspartokinase (AXX17_At5g13510), Aspartokinase 1, chloroplastic (AK1), Aspartokinase 3, chloroplastic (AK3), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase, Homoserine dehydrogenase (At5g21060), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    4. Homoserine kinase (HSK)
    5. Threonine synthase 2, chloroplastic (TS2), Threonine synthase 1, chloroplastic (TS1)
    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
    Binding sitei91ATPBy similarity1
    Binding sitei94ATP; via amide nitrogenBy similarity1
    Binding sitei123ATPBy similarity1
    Binding sitei207Substrate1
    Binding sitei413Allosteric effector lysine; via carbonyl oxygen1
    Binding sitei415Allosteric effector lysine; via amide nitrogen1
    Binding sitei430Allosteric effector S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen1
    Binding sitei431Allosteric effector lysine; via amide nitrogen1
    Binding sitei432Allosteric effector lysine; via carbonyl oxygen1
    Binding sitei437Allosteric effector lysine; via carbonyl oxygen1
    Binding sitei452Allosteric effector S-adenosyl-L-methionine1
    Binding sitei453Allosteric effector S-adenosyl-L-methionine; via amide nitrogen1

    GO - Molecular functioni

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G13280-MONOMER.
    BRENDAi2.7.2.4. 399.
    SABIO-RKQ9LYU8.
    UniPathwayiUPA00034; UER00015.
    UPA00050; UER00461.
    UPA00051; UER00462.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartokinase 1, chloroplastic (EC:2.7.2.4)
    Alternative name(s):
    Aspartate kinase 1
    Gene namesi
    Name:AK1
    Synonyms:AK, AK-LYS1
    Ordered Locus Names:At5g13280
    ORF Names:T31B5.100
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G13280.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast stroma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 90ChloroplastSequence analysisAdd BLAST90
    ChainiPRO_000024815791 – 569Aspartokinase 1, chloroplasticAdd BLAST479

    Proteomic databases

    PaxDbiQ9LYU8.
    PRIDEiQ9LYU8.

    PTM databases

    iPTMnetiQ9LYU8.

    Expressioni

    Gene expression databases

    GenevisibleiQ9LYU8. AT.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi16447. 4 interactors.
    IntActiQ9LYU8. 4 interactors.
    STRINGi3702.AT5G13280.1.

    Structurei

    Secondary structure

    1569
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi88 – 92Combined sources5
    Helixi95 – 97Combined sources3
    Helixi100 – 112Combined sources13
    Beta strandi118 – 122Combined sources5
    Helixi128 – 139Combined sources12
    Turni140 – 142Combined sources3
    Turni144 – 146Combined sources3
    Helixi147 – 149Combined sources3
    Helixi151 – 167Combined sources17
    Helixi172 – 191Combined sources20
    Helixi196 – 220Combined sources25
    Beta strandi225 – 228Combined sources4
    Helixi230 – 232Combined sources3
    Helixi250 – 264Combined sources15
    Beta strandi268 – 278Combined sources11
    Turni279 – 281Combined sources3
    Beta strandi284 – 286Combined sources3
    Helixi291 – 303Combined sources13
    Beta strandi308 – 320Combined sources13
    Turni322 – 324Combined sources3
    Beta strandi333 – 335Combined sources3
    Helixi336 – 346Combined sources11
    Helixi352 – 361Combined sources10
    Beta strandi365 – 369Combined sources5
    Beta strandi378 – 382Combined sources5
    Beta strandi391 – 406Combined sources16
    Helixi408 – 410Combined sources3
    Helixi416 – 426Combined sources11
    Beta strandi431 – 437Combined sources7
    Beta strandi440 – 445Combined sources6
    Helixi448 – 450Combined sources3
    Beta strandi451 – 453Combined sources3
    Helixi457 – 467Combined sources11
    Turni468 – 470Combined sources3
    Beta strandi471 – 486Combined sources16
    Helixi488 – 490Combined sources3
    Helixi491 – 505Combined sources15
    Beta strandi510 – 514Combined sources5
    Beta strandi519 – 526Combined sources8
    Helixi527 – 542Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CDQX-ray2.85A/B61-569[»]
    ProteinModelPortaliQ9LYU8.
    SMRiQ9LYU8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9LYU8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini405 – 483ACT 1PROSITE-ProRule annotationAdd BLAST79
    Domaini484 – 560ACT 2PROSITE-ProRule annotationAdd BLAST77

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiKOG0456. Eukaryota.
    COG0527. LUCA.
    HOGENOMiHOG000293094.
    InParanoidiQ9LYU8.
    KOiK00928.
    OMAiFIKELHF.
    OrthoDBiEOG0936068I.
    PhylomeDBiQ9LYU8.

    Family and domain databases

    Gene3Di3.40.1160.10. 2 hits.
    InterProiIPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53633. SSF53633. 1 hit.
    TIGRFAMsiTIGR00657. 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.

    Q9LYU8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAATRVRCCH SNAAFTRLPL TRHRNSPTLP ISLNRVDFPT LKKLSLPIGD
    60 70 80 90 100
    GSSIRKVSGS GSRNIVRAVL EEKKTEAITE VDEKGITCVM KFGGSSVASA
    110 120 130 140 150
    ERMKEVADLI LTFPEESPVI VLSAMGKTTN NLLLAGEKAV SCGVSNASEI
    160 170 180 190 200
    EELSIIKELH IRTVKELNID PSVILTYLEE LEQLLKGIAM MKELTLRTRD
    210 220 230 240 250
    YLVSFGECLS TRIFAAYLNT IGVKARQYDA FEIGFITTDD FTNGDILEAT
    260 270 280 290 300
    YPAVAKRLYD DWMHDPAVPI VTGFLGKGWK TGAVTTLGRG GSDLTATTIG
    310 320 330 340 350
    KALGLKEIQV WKDVDGVLTC DPTIYKRATP VPYLTFDEAA ELAYFGAQVL
    360 370 380 390 400
    HPQSMRPARE GEIPVRVKNS YNPKAPGTII TKTRDMTKSI LTSIVLKRNV
    410 420 430 440 450
    TMLDIASTRM LGQVGFLAKV FSIFEELGIS VDVVATSEVS ISLTLDPSKL
    460 470 480 490 500
    WSRELIQQEL DHVVEELEKI AVVNLLKGRA IISLIGNVQH SSLILERAFH
    510 520 530 540 550
    VLYTKGVNVQ MISQGASKVN ISFIVNEAEA EGCVQALHKS FFESGDLSEL
    560
    LIQPRLGNGS PVRTLQVEN
    Length:569
    Mass (Da):62,298
    Last modified:October 1, 2000 - v1
    Checksum:iF66A35F4E84DC429
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti369N → S in CAA67376 (PubMed:9207839).Curated1
    Sequence conflicti569N → D in CAA67376 (PubMed:9207839).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X98873 mRNA. Translation: CAA67376.1.
    AL163491 Genomic DNA. Translation: CAB86635.1.
    CP002688 Genomic DNA. Translation: AED91874.1.
    BT000493 mRNA. Translation: AAN18062.1.
    AY057674 mRNA. Translation: AAL15305.1.
    PIRiT48575.
    RefSeqiNP_196832.1. NM_121331.3.
    UniGeneiAt.124.
    At.32091.

    Genome annotation databases

    EnsemblPlantsiAT5G13280.1; AT5G13280.1; AT5G13280.
    GeneIDi831169.
    GrameneiAT5G13280.1; AT5G13280.1; AT5G13280.
    KEGGiath:AT5G13280.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X98873 mRNA. Translation: CAA67376.1.
    AL163491 Genomic DNA. Translation: CAB86635.1.
    CP002688 Genomic DNA. Translation: AED91874.1.
    BT000493 mRNA. Translation: AAN18062.1.
    AY057674 mRNA. Translation: AAL15305.1.
    PIRiT48575.
    RefSeqiNP_196832.1. NM_121331.3.
    UniGeneiAt.124.
    At.32091.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2CDQX-ray2.85A/B61-569[»]
    ProteinModelPortaliQ9LYU8.
    SMRiQ9LYU8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi16447. 4 interactors.
    IntActiQ9LYU8. 4 interactors.
    STRINGi3702.AT5G13280.1.

    PTM databases

    iPTMnetiQ9LYU8.

    Proteomic databases

    PaxDbiQ9LYU8.
    PRIDEiQ9LYU8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G13280.1; AT5G13280.1; AT5G13280.
    GeneIDi831169.
    GrameneiAT5G13280.1; AT5G13280.1; AT5G13280.
    KEGGiath:AT5G13280.

    Organism-specific databases

    TAIRiAT5G13280.

    Phylogenomic databases

    eggNOGiKOG0456. Eukaryota.
    COG0527. LUCA.
    HOGENOMiHOG000293094.
    InParanoidiQ9LYU8.
    KOiK00928.
    OMAiFIKELHF.
    OrthoDBiEOG0936068I.
    PhylomeDBiQ9LYU8.

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00015.
    UPA00050; UER00461.
    UPA00051; UER00462.
    BioCyciARA:AT5G13280-MONOMER.
    BRENDAi2.7.2.4. 399.
    SABIO-RKQ9LYU8.

    Miscellaneous databases

    EvolutionaryTraceiQ9LYU8.
    PROiQ9LYU8.

    Gene expression databases

    GenevisibleiQ9LYU8. AT.

    Family and domain databases

    Gene3Di3.40.1160.10. 2 hits.
    InterProiIPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53633. SSF53633. 1 hit.
    TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS00324. ASPARTOKINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAK1_ARATH
    AccessioniPrimary (citable) accession number: Q9LYU8
    Secondary accession number(s): O23152
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: October 1, 2000
    Last modified: November 30, 2016
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Only one ACT domain (ACT1) is implicated in effector binding.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    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.