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 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

    Pathway: 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 2, chloroplastic (AK2), Aspartokinase 1, chloroplastic (AK1), Aspartokinase 3, chloroplastic (AK3), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), 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.

    Pathway: 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 2, chloroplastic (AK2), Aspartokinase 1, chloroplastic (AK1), Aspartokinase 3, chloroplastic (AK3), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase, Homoserine dehydrogenase (At5g21060), 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei91 – 911ATPBy similarity
    Binding sitei94 – 941ATP; via amide nitrogenBy similarity
    Binding sitei123 – 1231ATPBy similarity
    Binding sitei207 – 2071Substrate
    Binding sitei413 – 4131Allosteric effector lysine; via carbonyl oxygen
    Binding sitei415 – 4151Allosteric effector lysine; via amide nitrogen
    Binding sitei430 – 4301Allosteric effector S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen
    Binding sitei431 – 4311Allosteric effector lysine; via amide nitrogen
    Binding sitei432 – 4321Allosteric effector lysine; via carbonyl oxygen
    Binding sitei437 – 4371Allosteric effector lysine; via carbonyl oxygen
    Binding sitei452 – 4521Allosteric effector S-adenosyl-L-methionine
    Binding sitei453 – 4531Allosteric effector S-adenosyl-L-methionine; via amide nitrogen

    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
    ProteomesiUP000006548 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)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 9090ChloroplastSequence AnalysisAdd
    BLAST
    Chaini91 – 569479Aspartokinase 1, chloroplasticPRO_0000248157Add
    BLAST

    Proteomic databases

    PaxDbiQ9LYU8.
    PRIDEiQ9LYU8.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi16447. 4 interactions.
    IntActiQ9LYU8. 4 interactions.
    STRINGi3702.AT5G13280.1.

    Structurei

    Secondary structure

    1
    569
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi88 – 925Combined sources
    Helixi95 – 973Combined sources
    Helixi100 – 11213Combined sources
    Beta strandi118 – 1225Combined sources
    Helixi128 – 13912Combined sources
    Turni140 – 1423Combined sources
    Turni144 – 1463Combined sources
    Helixi147 – 1493Combined sources
    Helixi151 – 16717Combined sources
    Helixi172 – 19120Combined sources
    Helixi196 – 22025Combined sources
    Beta strandi225 – 2284Combined sources
    Helixi230 – 2323Combined sources
    Helixi250 – 26415Combined sources
    Beta strandi268 – 27811Combined sources
    Turni279 – 2813Combined sources
    Beta strandi284 – 2863Combined sources
    Helixi291 – 30313Combined sources
    Beta strandi308 – 32013Combined sources
    Turni322 – 3243Combined sources
    Beta strandi333 – 3353Combined sources
    Helixi336 – 34611Combined sources
    Helixi352 – 36110Combined sources
    Beta strandi365 – 3695Combined sources
    Beta strandi378 – 3825Combined sources
    Beta strandi391 – 40616Combined sources
    Helixi408 – 4103Combined sources
    Helixi416 – 42611Combined sources
    Beta strandi431 – 4377Combined sources
    Beta strandi440 – 4456Combined sources
    Helixi448 – 4503Combined sources
    Beta strandi451 – 4533Combined sources
    Helixi457 – 46711Combined sources
    Turni468 – 4703Combined sources
    Beta strandi471 – 48616Combined sources
    Helixi488 – 4903Combined sources
    Helixi491 – 50515Combined sources
    Beta strandi510 – 5145Combined sources
    Beta strandi519 – 5268Combined sources
    Helixi527 – 54216Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CDQX-ray2.85A/B61-569[»]
    ProteinModelPortaliQ9LYU8.
    SMRiQ9LYU8. Positions 84-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9LYU8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini405 – 48379ACT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini484 – 56077ACT 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0527.
    HOGENOMiHOG000293094.
    InParanoidiQ9LYU8.
    KOiK00928.
    OMAiATISHGQ.
    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.
    PF01842. ACT. 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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti369 – 3691N → S in CAA67376 (PubMed:9207839).Curated
    Sequence conflicti569 – 5691N → D in CAA67376 (PubMed:9207839).Curated

    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_121331.2.
    UniGeneiAt.124.
    At.32091.

    Genome annotation databases

    EnsemblPlantsiAT5G13280.1; AT5G13280.1; AT5G13280.
    GeneIDi831169.
    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_121331.2.
    UniGeneiAt.124.
    At.32091.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CDQX-ray2.85A/B61-569[»]
    ProteinModelPortaliQ9LYU8.
    SMRiQ9LYU8. Positions 84-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi16447. 4 interactions.
    IntActiQ9LYU8. 4 interactions.
    STRINGi3702.AT5G13280.1.

    Proteomic databases

    PaxDbiQ9LYU8.
    PRIDEiQ9LYU8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TAIRiAT5G13280.

    Phylogenomic databases

    eggNOGiCOG0527.
    HOGENOMiHOG000293094.
    InParanoidiQ9LYU8.
    KOiK00928.
    OMAiATISHGQ.
    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.

    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.
    PF01842. ACT. 1 hit.
    [Graphical view]
    SUPFAMiSSF53633. SSF53633. 1 hit.
    TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS00324. ASPARTOKINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular characterisation of an Arabidopsis thaliana cDNA coding for a monofunctional aspartate kinase."
      Frankard V., Vauterin M., Jacobs M.
      Plant Mol. Biol. 34:233-242(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "S-adenosylmethionine -- a novel regulator of aspartate kinase."
      Rognes S.E., Lea P.J., Miflin B.J.
      Nature 287:357-359(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    6. "Allosteric monofunctional aspartate kinases from Arabidopsis."
      Curien G., Laurencin M., Robert-Genthon M., Dumas R.
      FEBS J. 274:164-176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    7. "A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase."
      Mas-Droux C., Curien G., Robert-Genthon M., Laurencin M., Ferrer J.L., Dumas R.
      Plant Cell 18:1681-1692(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 61-569 IN COMPLEX WITH SUBSTRATE ANALOG AND ALLOSTERIC REGULATORS, SUBUNIT.

    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: June 24, 2015
    This is version 101 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

    External Data

    Dasty 3

    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 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.