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Q9SA18

- AKH1_ARATH

UniProt

Q9SA18 - AKH1_ARATH

Protein

Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic

Gene

AKHSDH1

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 106 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.
    ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

    Enzyme regulationi

    Inhibition of aspartate kinase activity by threonine and leucine and 3-fold activation by cysteine, isoleucine, valine, serine and alanine at 2.5 mM. Partial inhibition of homoserine dehydrogenase activity by threonine and cysteine (14% of activity remaining at saturation with either amino acid). No synergy between the effectors for both activation or inhibition.1 Publication

    Kineticsi

    1. KM=2.6 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH and 20 mM ATP)1 Publication
    2. KM=2.3 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH, 20 mM ATP and a saturating concentration of alanine)1 Publication
    3. KM=6.5 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH and 50 mM aspartate)1 Publication
    4. KM=0.48 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 150 mM KCl, 20 mM MgCl2, 200 µM NADPH, 50 mM aspartate and a saturating concentration of alanine)1 Publication
    5. KM=290 µM for aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity (at pH 8.0, in the presence of 150 mM KCl and 200 µM NADPH)1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi559 – 5646NADPSequence Analysis

    GO - Molecular functioni

    1. amino acid binding Source: InterPro
    2. aspartate kinase activity Source: TAIR
    3. ATP binding Source: UniProtKB-KW
    4. homoserine dehydrogenase activity Source: TAIR
    5. NADP binding Source: InterPro

    GO - Biological processi

    1. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
    2. methionine biosynthetic process Source: UniProtKB-KW
    3. threonine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Oxidoreductase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    ATP-binding, NADP, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ9SA18.
    UniPathwayiUPA00034; UER00015.
    UPA00050; UER00063.
    UPA00050; UER00461.
    UPA00051; UER00462.
    UPA00051; UER00465.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic
    Short name:
    AK-HD 1
    Short name:
    AK-HSDH 1
    Alternative name(s):
    Beta-aspartyl phosphate homoserine 1
    Including the following 2 domains:
    Aspartokinase (EC:2.7.2.4)
    Homoserine dehydrogenase (EC:1.1.1.3)
    Gene namesi
    Name:AKHSDH1
    Synonyms:AK-HSDH I
    Ordered Locus Names:At1g31230
    ORF Names:F28K20.19, T19E23.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G31230.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast stroma Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8282ChloroplastSequence AnalysisAdd
    BLAST
    Chaini83 – 911829Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplasticPRO_0000245844Add
    BLAST

    Proteomic databases

    PaxDbiQ9SA18.
    PRIDEiQ9SA18.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9SA18.

    Interactioni

    Subunit structurei

    Homo- or heterodimer.Curated

    Protein-protein interaction databases

    BioGridi25246. 1 interaction.
    IntActiQ9SA18. 1 interaction.
    MINTiMINT-8067838.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SA18.
    SMRiQ9SA18. Positions 86-546, 549-904.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini407 – 48276ACT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini488 – 56578ACT 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni83 – 331249AspartokinaseBy similarityAdd
    BLAST
    Regioni332 – 557226InterfaceBy similarityAdd
    BLAST
    Regioni558 – 911354Homoserine dehydrogenaseBy similarityAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the aspartokinase family.Curated
    In the C-terminal section; belongs to the homoserine dehydrogenase family.Curated
    Contains 2 ACT domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0527.
    HOGENOMiHOG000271593.
    InParanoidiQ9SA18.
    KOiK12524.
    OMAiASACEIW.
    PhylomeDBiQ9SA18.

    Family and domain databases

    Gene3Di3.40.1160.10. 2 hits.
    3.40.50.720. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR005106. Asp/hSer_DH_NAD-bd.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    IPR011147. Bifunc_aspartokin/hSer_DH.
    IPR001342. HDH_cat.
    IPR019811. HDH_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    PF01842. ACT. 2 hits.
    PF00742. Homoserine_dh. 1 hit.
    PF03447. NAD_binding_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000727. ThrA. 1 hit.
    SUPFAMiSSF53633. SSF53633. 1 hit.
    TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
    PROSITEiPS51671. ACT. 2 hits.
    PS00324. ASPARTOKINASE. 1 hit.
    PS01042. HOMOSER_DHGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9SA18-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVVSLAKVV TSPAVAGDLA VRVPFIYGKR LVSNRVSFGK LRRRSCIGQC    50
    VRSELQSPRV LGSVTDLALD NSVENGHLPK GDSWAVHKFG GTCVGNSERI 100
    KDVAAVVVKD DSERKLVVVS AMSKVTDMMY DLIHRAESRD DSYLSALSGV 150
    LEKHRATAVD LLDGDELSSF LARLNDDINN LKAMLRAIYI AGHATESFSD 200
    FVVGHGELWS AQMLAAVVRK SGLDCTWMDA RDVLVVIPTS SNQVDPDFVE 250
    SEKRLEKWFT QNSAKIIIAT GFIASTPQNI PTTLKRDGSD FSAAIMSALF 300
    RSHQLTIWTD VDGVYSADPR KVSEAVVLKT LSYQEAWEMS YFGANVLHPR 350
    TIIPVMKYDI PIVIRNIFNL SAPGTMICRQ IDDEDGFKLD APVKGFATID 400
    NLALVNVEGT GMAGVPGTAS AIFSAVKEVG ANVIMISQAS SEHSVCFAVP 450
    EKEVKAVSEA LNSRFRQALA GGRLSQIEII PNCSILAAVG QKMASTPGVS 500
    ATFFNALAKA NINIRAIAQG CSEFNITVVV KREDCIRALR AVHSRFYLSR 550
    TTLAVGIIGP GLIGGTLLDQ IRDQAAVLKE EFKIDLRVIG ITGSSKMLMS 600
    ESGIDLSRWR ELMKEEGEKA DMEKFTQYVK GNHFIPNSVM VDCTADADIA 650
    SCYYDWLLRG IHVVTPNKKA NSGPLDQYLK IRDLQRKSYT HYFYEATVGA 700
    GLPIISTLRG LLETGDKILR IEGIFSGTLS YLFNNFVGTR SFSEVVAEAK 750
    QAGFTEPDPR DDLSGTDVAR KVTILARESG LKLDLEGLPV QNLVPKPLQA 800
    CASAEEFMEK LPQFDEELSK QREEAEAAGE VLRYVGVVDA VEKKGTVELK 850
    RYKKDHPFAQ LSGADNIIAF TTKRYKEQPL IVRGPGAGAQ VTAGGIFSDI 900
    LRLAFYLGAP S 911
    Length:911
    Mass (Da):99,404
    Last modified:May 1, 2000 - v1
    Checksum:i95A663413B68585F
    GO

    Sequence cautioni

    The sequence AAF24602.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA50500.2 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti517 – 5171I → M in BAC43372. (PubMed:11910074)Curated
    Sequence conflicti900 – 9001I → F in BAC43372. (PubMed:11910074)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC004793 Genomic DNA. Translation: AAD21689.1.
    AC007654 Genomic DNA. Translation: AAF24602.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE31330.1.
    AK118779 mRNA. Translation: BAC43372.1.
    X71364 Genomic DNA. Translation: CAA50500.2. Sequence problems.
    PIRiE86438.
    S46497.
    RefSeqiNP_174408.1. NM_102861.3.
    UniGeneiAt.48251.
    At.71214.

    Genome annotation databases

    EnsemblPlantsiAT1G31230.1; AT1G31230.1; AT1G31230.
    GeneIDi840011.
    KEGGiath:AT1G31230.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC004793 Genomic DNA. Translation: AAD21689.1 .
    AC007654 Genomic DNA. Translation: AAF24602.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE31330.1 .
    AK118779 mRNA. Translation: BAC43372.1 .
    X71364 Genomic DNA. Translation: CAA50500.2 . Sequence problems.
    PIRi E86438.
    S46497.
    RefSeqi NP_174408.1. NM_102861.3.
    UniGenei At.48251.
    At.71214.

    3D structure databases

    ProteinModelPortali Q9SA18.
    SMRi Q9SA18. Positions 86-546, 549-904.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 25246. 1 interaction.
    IntActi Q9SA18. 1 interaction.
    MINTi MINT-8067838.

    Proteomic databases

    PaxDbi Q9SA18.
    PRIDEi Q9SA18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G31230.1 ; AT1G31230.1 ; AT1G31230 .
    GeneIDi 840011.
    KEGGi ath:AT1G31230.

    Organism-specific databases

    TAIRi AT1G31230.

    Phylogenomic databases

    eggNOGi COG0527.
    HOGENOMi HOG000271593.
    InParanoidi Q9SA18.
    KOi K12524.
    OMAi ASACEIW.
    PhylomeDBi Q9SA18.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00015 .
    UPA00050 ; UER00063 .
    UPA00050 ; UER00461 .
    UPA00051 ; UER00462 .
    UPA00051 ; UER00465 .
    SABIO-RK Q9SA18.

    Gene expression databases

    Genevestigatori Q9SA18.

    Family and domain databases

    Gene3Di 3.40.1160.10. 2 hits.
    3.40.50.720. 1 hit.
    InterProi IPR002912. ACT_dom.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR005106. Asp/hSer_DH_NAD-bd.
    IPR001341. Asp_kinase_dom.
    IPR018042. Aspartate_kinase_CS.
    IPR011147. Bifunc_aspartokin/hSer_DH.
    IPR001342. HDH_cat.
    IPR019811. HDH_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00696. AA_kinase. 1 hit.
    PF01842. ACT. 2 hits.
    PF00742. Homoserine_dh. 1 hit.
    PF03447. NAD_binding_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000727. ThrA. 1 hit.
    SUPFAMi SSF53633. SSF53633. 1 hit.
    TIGRFAMsi TIGR00657. asp_kinases. 1 hit.
    PROSITEi PS51671. ACT. 2 hits.
    PS00324. ASPARTOKINASE. 1 hit.
    PS01042. HOMOSER_DHGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana."
      Paris S., Wessel P.M., Dumas R.
      Protein Expr. Purif. 24:105-110(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Molecular analysis of the aspartate kinase-homoserine dehydrogenase gene from Arabidopsis thaliana."
      Ghislain M., Frankard V., Vandenbossche D., Matthews B., Jacobs M.
      Plant Mol. Biol. 24:835-851(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-573.
      Strain: cv. Columbia.
    6. "Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. Physiological context sets the specificity."
      Curien G., Ravanel S., Robert M., Dumas R.
      J. Biol. Chem. 280:41178-41183(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiAKH1_ARATH
    AccessioniPrimary (citable) accession number: Q9SA18
    Secondary accession number(s): Q8GWK9, Q9SHF9, Q9SW59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3