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Q9LYU8

- AK1_ARATH

UniProt

Q9LYU8 - AK1_ARATH

Protein

Aspartokinase 1, chloroplastic

Gene

AK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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

    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

    1. amino acid binding Source: InterPro
    2. aspartate kinase activity Source: TAIR
    3. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular amino acid biosynthetic process Source: TAIR
    2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
    3. threonine biosynthetic process Source: UniProtKB-UniPathway

    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: Chromosome 5

    Organism-specific databases

    TAIRiAT5G13280.

    Subcellular locationi

    Plastidchloroplast Curated

    GO - Cellular componenti

    1. chloroplast stroma Source: TAIR

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9LYU8.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi16447. 4 interactions.
    IntActiQ9LYU8. 4 interactions.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiVMRTDSH.
    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

    MAATRVRCCH SNAAFTRLPL TRHRNSPTLP ISLNRVDFPT LKKLSLPIGD    50
    GSSIRKVSGS GSRNIVRAVL EEKKTEAITE VDEKGITCVM KFGGSSVASA 100
    ERMKEVADLI LTFPEESPVI VLSAMGKTTN NLLLAGEKAV SCGVSNASEI 150
    EELSIIKELH IRTVKELNID PSVILTYLEE LEQLLKGIAM MKELTLRTRD 200
    YLVSFGECLS TRIFAAYLNT IGVKARQYDA FEIGFITTDD FTNGDILEAT 250
    YPAVAKRLYD DWMHDPAVPI VTGFLGKGWK TGAVTTLGRG GSDLTATTIG 300
    KALGLKEIQV WKDVDGVLTC DPTIYKRATP VPYLTFDEAA ELAYFGAQVL 350
    HPQSMRPARE GEIPVRVKNS YNPKAPGTII TKTRDMTKSI LTSIVLKRNV 400
    TMLDIASTRM LGQVGFLAKV FSIFEELGIS VDVVATSEVS ISLTLDPSKL 450
    WSRELIQQEL DHVVEELEKI AVVNLLKGRA IISLIGNVQH SSLILERAFH 500
    VLYTKGVNVQ MISQGASKVN ISFIVNEAEA EGCVQALHKS FFESGDLSEL 550
    LIQPRLGNGS PVRTLQVEN 569
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T48575.
    RefSeqi NP_196832.1. NM_121331.2.
    UniGenei At.124.
    At.32091.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CDQ X-ray 2.85 A/B 61-569 [» ]
    ProteinModelPortali Q9LYU8.
    SMRi Q9LYU8. Positions 84-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 16447. 4 interactions.
    IntActi Q9LYU8. 4 interactions.

    Proteomic databases

    PaxDbi Q9LYU8.
    PRIDEi Q9LYU8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G13280.1 ; AT5G13280.1 ; AT5G13280 .
    GeneIDi 831169.
    KEGGi ath:AT5G13280.

    Organism-specific databases

    TAIRi AT5G13280.

    Phylogenomic databases

    eggNOGi COG0527.
    HOGENOMi HOG000293094.
    InParanoidi Q9LYU8.
    KOi K00928.
    OMAi VMRTDSH.
    PhylomeDBi Q9LYU8.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00015 .
    UPA00050 ; UER00461 .
    UPA00051 ; UER00462 .
    BioCyci ARA:AT5G13280-MONOMER.
    BRENDAi 2.7.2.4. 399.
    SABIO-RK Q9LYU8.

    Miscellaneous databases

    EvolutionaryTracei Q9LYU8.

    Gene expression databases

    Genevestigatori Q9LYU8.

    Family and domain databases

    Gene3Di 3.40.1160.10. 2 hits.
    InterProi IPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    [Graphical view ]
    Pfami PF00696. AA_kinase. 1 hit.
    PF01842. ACT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53633. SSF53633. 1 hit.
    TIGRFAMsi TIGR00657. asp_kinases. 1 hit.
    PROSITEi PS51671. ACT. 1 hit.
    PS00324. ASPARTOKINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 97 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