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O81852

- AKH2_ARATH

UniProt

O81852 - AKH2_ARATH

Protein

Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic

Gene

AKHSDH2

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 111 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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

    Threonine interaction with Gln-443 leads to inhibition of aspartate kinase activity and facilitates the binding of a second threonine on Gln-524, leading to a partial inhibition of homoserine dehydrogenase activity (25% of activity remaining at saturation with threonine). Homoserine dehydrogenase activity is also partially inhibited by cysteine (15% of activity remaining at saturation with cysteine). No synergy between threonine and cysteine for the inhibition. 13-fold activation of aspartate kinase activity by cysteine, isoleucine, valine, serine and alanine at 2.5 mM and 4-fold activation by leucine at 2.5 mM, but no activation of homoserine dehydrogenase activity.2 Publications

    Kineticsi

    1. KM=11.6 mM for aspartate for the aspartokinase activity (in the presence of 40 mM ATP)2 Publications
    2. KM=6.15 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 200 µM NADPH and 20 mM ATP)2 Publications
    3. KM=1.5 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 200 µM NADPH, 20 mM ATP and a saturating concentration of alanine)2 Publications
    4. KM=26.4 mM for aspartate for the aspartokinase activity (in the presence of 100 mM ATP and 0.5 mM threonine)2 Publications
    5. KM=5.5 mM for ATP for the aspartokinase activity (in the presence of 50 mM aspartate)2 Publications
    6. KM=2.2 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 200 µM NADPH and 50 mM aspartate)2 Publications
    7. KM=0.42 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 200 µM NADPH, 50 mM aspartate and a saturating concentration of alanine)2 Publications
    8. KM=5.2 mM for homoserine for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 1 mM NADP)2 Publications
    9. KM=1.4 mM for aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity (in the presence of NADPH)2 Publications
    10. KM=311 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)2 Publications
    11. KM=24.5 mM for homoserine for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 1 mM NADP and 60 mM threonine)2 Publications
    12. KM=166.1 µM for NADP for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 50 mM homoserine)2 Publications
    13. KM=676.1 µM for NADP for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 100 mM homoserine and 60 mM threonine)2 Publications

    Vmax=5.4 µmol/min/mg enzyme toward aspartylhydroxamate for the aspartokinase activity2 Publications

    Vmax=165 µmol/min/mg enzyme toward aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity2 Publications

    Vmax=18.8 µmol/min/mg enzyme toward NADPH for the reverse reaction of the homoserine dehydrogenase activity2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi564 – 5696NADPSequence 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

    BioCyciARA:GQT-2291-MONOMER.
    BRENDAi1.1.1.3. 399.
    SABIO-RKO81852.
    UniPathwayiUPA00034; UER00015.
    UPA00050; UER00063.
    UPA00050; UER00461.
    UPA00051; UER00462.
    UPA00051; UER00465.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic
    Short name:
    AK-HD 2
    Short name:
    AK-HSDH 2
    Alternative name(s):
    Beta-aspartyl phosphate homoserine 2
    Including the following 2 domains:
    Aspartokinase (EC:2.7.2.4)
    Homoserine dehydrogenase (EC:1.1.1.3)
    Gene namesi
    Name:AKHSDH2
    Synonyms:AK-HSDH II
    Ordered Locus Names:At4g19710
    ORF Names:T16H5.70
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G19710.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi441 – 4411I → A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine. 1 Publication
    Mutagenesisi443 – 4431Q → A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine. 1 Publication
    Mutagenesisi522 – 5221I → A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine. 1 Publication
    Mutagenesisi524 – 5241Q → A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8787ChloroplastSequence AnalysisAdd
    BLAST
    Chaini88 – 916829Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplasticPRO_0000245845Add
    BLAST

    Proteomic databases

    PaxDbiO81852.
    PRIDEiO81852.

    Expressioni

    Gene expression databases

    ArrayExpressiO81852.
    GenevestigatoriO81852.

    Interactioni

    Subunit structurei

    Homo- or heterodimer.Curated

    Structurei

    3D structure databases

    ProteinModelPortaliO81852.
    SMRiO81852. Positions 90-551, 554-912.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini412 – 48776ACT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini493 – 57078ACT 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni88 – 336249AspartokinaseBy similarityAdd
    BLAST
    Regioni337 – 562226InterfaceBy similarityAdd
    BLAST
    Regioni563 – 916354Homoserine 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.
    InParanoidiO81852.
    KOiK12524.
    OMAiYIFGMLD.
    PhylomeDBiO81852.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O81852-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATLKPSFTV SPPNSNPIRF GSFPPQCFLR VPKPRRLILP RFRKTTGGGG    50
    GLIRCELPDF HLSATATTVS GVSTVNLVDQ VQIPKGEMWS VHKFGGTCVG 100
    NSQRIRNVAE VIINDNSERK LVVVSAMSKV TDMMYDLIRK AQSRDDSYLS 150
    ALEAVLEKHR LTARDLLDGD DLASFLSHLH NDISNLKAML RAIYIAGHAS 200
    ESFSDFVAGH GELWSAQMLS YVVRKTGLEC KWMDTRDVLI VNPTSSNQVD 250
    PDFGESEKRL DKWFSLNPSK IIIATGFIAS TPQNIPTTLK RDGSDFSAAI 300
    MGALLRARQV TIWTDVDGVY SADPRKVNEA VILQTLSYQE AWEMSYFGAN 350
    VLHPRTIIPV MRYNIPIVIR NIFNLSAPGT IICQPPEDDY DLKLTTPVKG 400
    FATIDNLALI NVEGTGMAGV PGTASDIFGC VKDVGANVIM ISQASSEHSV 450
    CFAVPEKEVN AVSEALRSRF SEALQAGRLS QIEVIPNCSI LAAVGQKMAS 500
    TPGVSCTLFS ALAKANINVR AISQGCSEYN VTVVIKREDS VKALRAVHSR 550
    FFLSRTTLAM GIVGPGLIGA TLLDQLRDQA AVLKQEFNID LRVLGITGSK 600
    KMLLSDIGID LSRWRELLNE KGTEADLDKF TQQVHGNHFI PNSVVVDCTA 650
    DSAIASRYYD WLRKGIHVIT PNKKANSGPL DQYLKLRDLQ RKSYTHYFYE 700
    ATVGAGLPII STLRGLLETG DKILRIEGIC SGTLSYLFNN FVGDRSFSEV 750
    VTEAKNAGFT EPDPRDDLSG TDVARKVIIL ARESGLKLDL ADLPIRSLVP 800
    EPLKGCTSVE EFMEKLPQYD GDLAKERLDA ENSGEVLRYV GVVDAVNQKG 850
    TVELRRYKKE HPFAQLAGSD NIIAFTTTRY KDHPLIVRGP GAGAQVTAGG 900
    IFSDILRLAS YLGAPS 916
    Length:916
    Mass (Da):100,250
    Last modified:November 1, 1998 - v1
    Checksum:i7ECD984DAFC97C4F
    GO
    Isoform 2 (identifier: O81852-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         837-916: LRYVGVVDAV...RLASYLGAPS → RLFTTNVFPFDQCDHILTIYICM

    Note: Derived from EST data. No experimental confirmation available.

    Show »
    Length:859
    Mass (Da):94,426
    Checksum:i1785CFCBF23709C7
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei837 – 91680LRYVG…LGAPS → RLFTTNVFPFDQCDHILTIY ICM in isoform 2. CuratedVSP_019798Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL024486 Genomic DNA. Translation: CAA19688.1.
    AL161551 Genomic DNA. Translation: CAB78973.1.
    CP002687 Genomic DNA. Translation: AEE84219.1.
    CP002687 Genomic DNA. Translation: AEE84220.1.
    BX827863 mRNA. No translation available.
    PIRiT04752.
    RefSeqiNP_193706.2. NM_118091.3. [O81852-2]
    NP_974576.1. NM_202847.2. [O81852-1]
    UniGeneiAt.32787.

    Genome annotation databases

    EnsemblPlantsiAT4G19710.2; AT4G19710.2; AT4G19710. [O81852-1]
    GeneIDi827715.
    KEGGiath:AT4G19710.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL024486 Genomic DNA. Translation: CAA19688.1 .
    AL161551 Genomic DNA. Translation: CAB78973.1 .
    CP002687 Genomic DNA. Translation: AEE84219.1 .
    CP002687 Genomic DNA. Translation: AEE84220.1 .
    BX827863 mRNA. No translation available.
    PIRi T04752.
    RefSeqi NP_193706.2. NM_118091.3. [O81852-2 ]
    NP_974576.1. NM_202847.2. [O81852-1 ]
    UniGenei At.32787.

    3D structure databases

    ProteinModelPortali O81852.
    SMRi O81852. Positions 90-551, 554-912.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi O81852.
    PRIDEi O81852.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G19710.2 ; AT4G19710.2 ; AT4G19710 . [O81852-1 ]
    GeneIDi 827715.
    KEGGi ath:AT4G19710.

    Organism-specific databases

    TAIRi AT4G19710.

    Phylogenomic databases

    eggNOGi COG0527.
    HOGENOMi HOG000271593.
    InParanoidi O81852.
    KOi K12524.
    OMAi YIFGMLD.
    PhylomeDBi O81852.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00015 .
    UPA00050 ; UER00063 .
    UPA00050 ; UER00461 .
    UPA00051 ; UER00462 .
    UPA00051 ; UER00465 .
    BioCyci ARA:GQT-2291-MONOMER.
    BRENDAi 1.1.1.3. 399.
    SABIO-RK O81852.

    Gene expression databases

    ArrayExpressi O81852.
    Genevestigatori O81852.

    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 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [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] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES.
    4. "Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
      Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
      Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    5. "Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine."
      Paris S., Viemon C., Curien G., Dumas R.
      J. Biol. Chem. 278:5361-5366(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, MUTAGENESIS OF ILE-441; GLN-443; ILE-522 AND GLN-524.
    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: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiAKH2_ARATH
    AccessioniPrimary (citable) accession number: O81852
    Secondary accession number(s): Q3E9Y8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    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