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Protein

Aspartate kinase

Gene

PP_4473

Organism
Pseudomonas putida (strain KT2440)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate.1 Publication

Catalytic activityi

ATP + L-aspartate = ADP + 4-phospho-L-aspartate.1 Publication

Enzyme regulationi

Allosterically feedback inhibited by L-lysine and L-threonine individually and also subject to a concerted feedback inhibition by these amino acids.1 Publication

Kineticsi

  1. KM=4.35 µM for ATP1 Publication
  2. KM=4.8 µM for L-aspartate1 Publication

    pH dependencei

    Optimum pH is between 7.9 and 8.4.1 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. Aspartate kinase (PP_4473)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA), 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.

    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. Aspartate kinase (PP_4473)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Homoserine dehydrogenase (hom), Homoserine dehydrogenase (PP_0664)
    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. Aspartate kinase (PP_4473)
    2. Aspartate-semialdehyde dehydrogenase (asd)
    3. Homoserine dehydrogenase (hom), Homoserine dehydrogenase (PP_0664)
    4. Homoserine kinase (thrB)
    5. no protein annotated in this organism
    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.

    GO - Molecular functioni

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Lysine biosynthesis, Methionine biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciPPUT160488:GIXO-4560-MONOMER.
    UniPathwayiUPA00034; UER00015.
    UPA00050; UER00461.
    UPA00051; UER00462.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate kinase (EC:2.7.2.4)
    Alternative name(s):
    Aspartokinase
    Gene namesi
    Ordered Locus Names:PP_4473
    OrganismiPseudomonas putida (strain KT2440)
    Taxonomic identifieri160488 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000000556 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 411411Aspartate kinasePRO_0000428880Add
    BLAST

    Expressioni

    Inductioni

    Repressed by L-methionine.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi160488.PP_4473.

    Structurei

    3D structure databases

    ProteinModelPortaliQ88EI9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini265 – 34884ACTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4105CFH. Bacteria.
    COG0527. LUCA.
    HOGENOMiHOG000293093.
    KOiK00928.
    OMAiINIMMIS.
    OrthoDBiEOG6NSGHC.

    Family and domain databases

    Gene3Di3.40.1160.10. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR005260. Asp_kin_monofn.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    IPR027795. GATS-like_ACT_dom.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    PF01842. ACT. 1 hit.
    PF13840. ACT_7. 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.

    Q88EI9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MALIVQKFGG TSVGSIERIE QVAEKVKKHR EAGDDLVVVL SAMSGETNRL
    60 70 80 90 100
    IDLAKQITDQ PVPRELDVIV STGEQVTIAL LTMALIKRGV PAVSYTGNQV
    110 120 130 140 150
    RILTDSSHNK ARILQIDDQK IRADLKEGRV VVVAGFQGVD EHGSITTLGR
    160 170 180 190 200
    GGSDTTGVAL AAALKADECQ IYTDVDGVYT TDPRVVPQAR RLEKITFEEM
    210 220 230 240 250
    LEMASLGSKV LQIRSVEFAG KYNVPLRVLH SFKEGPGTLI TIDEEESMEQ
    260 270 280 290 300
    PIISGIAFNR DEAKLTIRGV PDTPGVAFKI LGPISASNIE VDMIVQNVAH
    310 320 330 340 350
    DNTTDFTFTV HRNEYEKAQS VLENTAREIG AREVIGDTKI AKVSIVGVGM
    360 370 380 390 400
    RSHAGVASCM FEALAKESIN IQMISTSEIK VSVVLEEKYL ELAVRALHTA
    410
    FDLDAPARQG E
    Length:411
    Mass (Da):44,605
    Last modified:June 1, 2003 - v1
    Checksum:iF06EE38BAC0D3F74
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE015451 Genomic DNA. Translation: AAN70048.1.
    RefSeqiNP_746584.1. NC_002947.4.
    WP_003254504.1. NC_002947.4.

    Genome annotation databases

    EnsemblBacteriaiAAN70048; AAN70048; PP_4473.
    GeneIDi1041833.
    KEGGippu:PP_4473.
    PATRICi19947644. VBIPsePut30601_4759.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE015451 Genomic DNA. Translation: AAN70048.1.
    RefSeqiNP_746584.1. NC_002947.4.
    WP_003254504.1. NC_002947.4.

    3D structure databases

    ProteinModelPortaliQ88EI9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi160488.PP_4473.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAN70048; AAN70048; PP_4473.
    GeneIDi1041833.
    KEGGippu:PP_4473.
    PATRICi19947644. VBIPsePut30601_4759.

    Phylogenomic databases

    eggNOGiENOG4105CFH. Bacteria.
    COG0527. LUCA.
    HOGENOMiHOG000293093.
    KOiK00928.
    OMAiINIMMIS.
    OrthoDBiEOG6NSGHC.

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00015.
    UPA00050; UER00461.
    UPA00051; UER00462.
    BioCyciPPUT160488:GIXO-4560-MONOMER.

    Family and domain databases

    Gene3Di3.40.1160.10. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR005260. Asp_kin_monofn.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    IPR027795. GATS-like_ACT_dom.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    PF01842. ACT. 1 hit.
    PF13840. ACT_7. 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...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KT2440.
    2. "The aspartate kinase of Pseudomonas putida. Regulation of synthesis and activity."
      Robert-Gero M., Poiret M., Cohen G.N.
      Biochim. Biophys. Acta 206:17-30(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INDUCTION.

    Entry informationi

    Entry nameiAK_PSEPK
    AccessioniPrimary (citable) accession number: Q88EI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 14, 2014
    Last sequence update: June 1, 2003
    Last modified: May 11, 2016
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. 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.