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Protein

Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic

Gene

AKHSDH1

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

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

    Pathway:iL-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:iL-methionine biosynthesis via de novo pathway

    This protein is involved in step 1 and 3 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 (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.

    Pathway:iL-threonine biosynthesis

    This protein is involved in step 1 and 3 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. 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 (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.

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    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 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G31230.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • 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.

    Interactioni

    Subunit structurei

    Homo- or heterodimer.Curated

    Protein-protein interaction databases

    BioGridi25246. 1 interaction.
    IntActiQ9SA18. 1 interaction.
    MINTiMINT-8067838.
    STRINGi3702.AT1G31230.1.

    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.
    OMAiRYYSPIP.
    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.
    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]
    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

            10         20         30         40         50
    MPVVSLAKVV TSPAVAGDLA VRVPFIYGKR LVSNRVSFGK LRRRSCIGQC
    60 70 80 90 100
    VRSELQSPRV LGSVTDLALD NSVENGHLPK GDSWAVHKFG GTCVGNSERI
    110 120 130 140 150
    KDVAAVVVKD DSERKLVVVS AMSKVTDMMY DLIHRAESRD DSYLSALSGV
    160 170 180 190 200
    LEKHRATAVD LLDGDELSSF LARLNDDINN LKAMLRAIYI AGHATESFSD
    210 220 230 240 250
    FVVGHGELWS AQMLAAVVRK SGLDCTWMDA RDVLVVIPTS SNQVDPDFVE
    260 270 280 290 300
    SEKRLEKWFT QNSAKIIIAT GFIASTPQNI PTTLKRDGSD FSAAIMSALF
    310 320 330 340 350
    RSHQLTIWTD VDGVYSADPR KVSEAVVLKT LSYQEAWEMS YFGANVLHPR
    360 370 380 390 400
    TIIPVMKYDI PIVIRNIFNL SAPGTMICRQ IDDEDGFKLD APVKGFATID
    410 420 430 440 450
    NLALVNVEGT GMAGVPGTAS AIFSAVKEVG ANVIMISQAS SEHSVCFAVP
    460 470 480 490 500
    EKEVKAVSEA LNSRFRQALA GGRLSQIEII PNCSILAAVG QKMASTPGVS
    510 520 530 540 550
    ATFFNALAKA NINIRAIAQG CSEFNITVVV KREDCIRALR AVHSRFYLSR
    560 570 580 590 600
    TTLAVGIIGP GLIGGTLLDQ IRDQAAVLKE EFKIDLRVIG ITGSSKMLMS
    610 620 630 640 650
    ESGIDLSRWR ELMKEEGEKA DMEKFTQYVK GNHFIPNSVM VDCTADADIA
    660 670 680 690 700
    SCYYDWLLRG IHVVTPNKKA NSGPLDQYLK IRDLQRKSYT HYFYEATVGA
    710 720 730 740 750
    GLPIISTLRG LLETGDKILR IEGIFSGTLS YLFNNFVGTR SFSEVVAEAK
    760 770 780 790 800
    QAGFTEPDPR DDLSGTDVAR KVTILARESG LKLDLEGLPV QNLVPKPLQA
    810 820 830 840 850
    CASAEEFMEK LPQFDEELSK QREEAEAAGE VLRYVGVVDA VEKKGTVELK
    860 870 880 890 900
    RYKKDHPFAQ LSGADNIIAF TTKRYKEQPL IVRGPGAGAQ VTAGGIFSDI
    910
    LRLAFYLGAP S
    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. Curated
    The sequence CAA50500.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi25246. 1 interaction.
    IntActiQ9SA18. 1 interaction.
    MINTiMINT-8067838.
    STRINGi3702.AT1G31230.1.

    Proteomic databases

    PaxDbiQ9SA18.
    PRIDEiQ9SA18.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TAIRiAT1G31230.

    Phylogenomic databases

    eggNOGiCOG0527.
    HOGENOMiHOG000271593.
    InParanoidiQ9SA18.
    KOiK12524.
    OMAiRYYSPIP.
    PhylomeDBiQ9SA18.

    Enzyme and pathway databases

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

    Miscellaneous databases

    PROiQ9SA18.

    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.
    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]
    SUPFAMiSSF53633. SSF53633. 1 hit.
    TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
    PROSITEiPS51671. ACT. 2 hits.
    PS00324. ASPARTOKINASE. 1 hit.
    PS01042. HOMOSER_DHGENASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: July 22, 2015
    This is version 111 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

    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.