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Entry version 140 (26 Feb 2020)
Sequence version 1 (01 May 2000)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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. AK1 (AXX17_At5g12690), Aspartokinase 2, chloroplastic (AK2), Aspartokinase (AXX17_At5g13510), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Aspartokinase (AXX17_At3g01160), Aspartokinase 1, chloroplastic (AK1), Aspartokinase (CARAB-AK-LYS), Aspartokinase 3, chloroplastic (AK3), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic (DHDPS2), 4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic (DHDPS1)
    4. 4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic (DAPB1), 4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic (DAPB2)
    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 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. AK1 (AXX17_At5g12690), Aspartokinase 2, chloroplastic (AK2), Aspartokinase (AXX17_At5g13510), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Aspartokinase (AXX17_At3g01160), Aspartokinase 1, chloroplastic (AK1), Aspartokinase (CARAB-AK-LYS), Aspartokinase 3, chloroplastic (AK3), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. Homoserine dehydrogenase (At5g21060), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Homoserine dehydrogenase (AXX17_At5g21030), Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase (AXX17_At5g21030), Homoserine dehydrogenase, Homoserine dehydrogenase (At5g21060), 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.

    Pathwayi: L-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. AK1 (AXX17_At5g12690), Aspartokinase 2, chloroplastic (AK2), Aspartokinase (AXX17_At5g13510), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Aspartokinase (AXX17_At3g01160), Aspartokinase 1, chloroplastic (AK1), Aspartokinase (CARAB-AK-LYS), Aspartokinase 3, chloroplastic (AK3), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. Homoserine dehydrogenase (At5g21060), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Homoserine dehydrogenase (AXX17_At5g21030), Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase (AXX17_At5g21030), Homoserine dehydrogenase, Homoserine dehydrogenase (At5g21060), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    4. Homoserine kinase (HSK)
    5. Threonine synthase 1, chloroplastic (TS1), Threonine synthase 2, chloroplastic (TS2)
    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)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi559 – 564NADPSequence analysis6

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionKinase, Multifunctional enzyme, Oxidoreductase, Transferase
    Biological processAmino-acid biosynthesis, Methionine biosynthesis
    LigandATP-binding, NADP, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q9SA18

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00034;UER00015
    UPA00050;UER00063
    UPA00050;UER00461
    UPA00051;UER00462
    UPA00051;UER00465

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:AKHSDH1
    Synonyms:AK-HSDH I
    Ordered Locus Names:At1g31230
    ORF Names:F28K20.19, T19E23.1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000007605 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome 1 top arm, Chromosome 1, ARATH_1
    • UP000006548 Componenti: Chromosome 1

    Organism-specific databases

    Arabidopsis Information Portal

    More...
    Araporti
    AT1G31230

    The Arabidopsis Information Resource

    More...
    TAIRi
    locus:2029564 AT1G31230

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chloroplast, Plastid

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 82ChloroplastSequence analysisAdd BLAST82
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000024584483 – 911Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplasticAdd BLAST829

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q9SA18

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9SA18

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9SA18

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9SA18 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9SA18 AT

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homo- or heterodimer.

    Curated

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    25246, 2 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q9SA18, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    3702.AT1G31230.1

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9SA18

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini407 – 482ACT 1PROSITE-ProRule annotationAdd BLAST76
    Domaini488 – 565ACT 2PROSITE-ProRule annotationAdd BLAST78

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni83 – 331AspartokinaseBy similarityAdd BLAST249
    Regioni332 – 557InterfaceBy similarityAdd BLAST226
    Regioni558 – 911Homoserine dehydrogenaseBy similarityAdd BLAST354

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IFE2 Eukaryota
    COG0460 LUCA
    COG0527 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_009116_7_1_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9SA18

    KEGG Orthology (KO)

    More...
    KOi
    K12524

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YTHVDGI

    Database of Orthologous Groups

    More...
    OrthoDBi
    113181at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9SA18

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd04257 AAK_AK-HSDH, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.1160.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036393 AceGlu_kinase-like_sf
    IPR002912 ACT_dom
    IPR041743 AK-HSDH_N
    IPR001048 Asp/Glu/Uridylate_kinase
    IPR005106 Asp/hSer_DH_NAD-bd
    IPR001341 Asp_kinase
    IPR018042 Aspartate_kinase_CS
    IPR027795 CASTOR_ACT_dom
    IPR001342 HDH_cat
    IPR019811 HDH_CS
    IPR036291 NAD(P)-bd_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00696 AA_kinase, 1 hit
    PF01842 ACT, 1 hit
    PF13840 ACT_7, 1 hit
    PF00742 Homoserine_dh, 1 hit
    PF03447 NAD_binding_3, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit
    SSF53633 SSF53633, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00657 asp_kinases, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51671 ACT, 2 hits
    PS00324 ASPARTOKINASE, 1 hit
    PS01042 HOMOSER_DHGENASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i95A663413B68585F
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti517I → M in BAC43372 (PubMed:11910074).Curated1
    Sequence conflicti900I → F in BAC43372 (PubMed:11910074).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E86438
    S46497

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_174408.1, NM_102861.3

    Genome annotation databases

    Ensembl plant genome annotation project

    More...
    EnsemblPlantsi
    AT1G31230.1; AT1G31230.1; AT1G31230

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    840011

    Gramene; a comparative resource for plants

    More...
    Gramenei
    AT1G31230.1; AT1G31230.1; AT1G31230

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ath:AT1G31230

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

    3D structure databases

    SMRiQ9SA18
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi25246, 2 interactors
    IntActiQ9SA18, 1 interactor
    STRINGi3702.AT1G31230.1

    PTM databases

    iPTMnetiQ9SA18

    Proteomic databases

    PaxDbiQ9SA18
    PRIDEiQ9SA18

    Genome annotation databases

    EnsemblPlantsiAT1G31230.1; AT1G31230.1; AT1G31230
    GeneIDi840011
    GrameneiAT1G31230.1; AT1G31230.1; AT1G31230
    KEGGiath:AT1G31230

    Organism-specific databases

    AraportiAT1G31230
    TAIRilocus:2029564 AT1G31230

    Phylogenomic databases

    eggNOGiENOG410IFE2 Eukaryota
    COG0460 LUCA
    COG0527 LUCA
    HOGENOMiCLU_009116_7_1_1
    InParanoidiQ9SA18
    KOiK12524
    OMAiYTHVDGI
    OrthoDBi113181at2759
    PhylomeDBiQ9SA18

    Enzyme and pathway databases

    UniPathwayiUPA00034;UER00015
    UPA00050;UER00063
    UPA00050;UER00461
    UPA00051;UER00462
    UPA00051;UER00465
    SABIO-RKiQ9SA18

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:Q9SA18

    Gene expression databases

    ExpressionAtlasiQ9SA18 baseline and differential
    GenevisibleiQ9SA18 AT

    Family and domain databases

    CDDicd04257 AAK_AK-HSDH, 1 hit
    Gene3Di3.40.1160.10, 1 hit
    InterProiView protein in InterPro
    IPR036393 AceGlu_kinase-like_sf
    IPR002912 ACT_dom
    IPR041743 AK-HSDH_N
    IPR001048 Asp/Glu/Uridylate_kinase
    IPR005106 Asp/hSer_DH_NAD-bd
    IPR001341 Asp_kinase
    IPR018042 Aspartate_kinase_CS
    IPR027795 CASTOR_ACT_dom
    IPR001342 HDH_cat
    IPR019811 HDH_CS
    IPR036291 NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF00696 AA_kinase, 1 hit
    PF01842 ACT, 1 hit
    PF13840 ACT_7, 1 hit
    PF00742 Homoserine_dh, 1 hit
    PF03447 NAD_binding_3, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    SSF53633 SSF53633, 1 hit
    TIGRFAMsiTIGR00657 asp_kinases, 1 hit
    PROSITEiView protein in PROSITE
    PS51671 ACT, 2 hits
    PS00324 ASPARTOKINASE, 1 hit
    PS01042 HOMOSER_DHGENASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAKH1_ARATH
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9SA18
    Secondary accession number(s): Q8GWK9, Q9SHF9, Q9SW59
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: May 1, 2000
    Last modified: February 26, 2020
    This is version 140 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Reference proteome

    Documents

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