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Q9SMZ4

- AASS_ARATH

UniProt

Q9SMZ4 - AASS_ARATH

Protein

Alpha-aminoadipic semialdehyde synthase

Gene

LKR/SDH

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 93 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-oxoglutarate reductase and saccharopine dehydrogenase activity, respectively. Negatively regulates free Lys accumulation in seeds.3 Publications

    Catalytic activityi

    N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH.
    N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH.

    Enzyme regulationi

    The LKR activity is stimulated by NaCl.1 Publication

    Kineticsi

    1. KM=5.180 mM for lysine (isoform Long at pH 7.5 and 30 degrees Celsius)1 Publication
    2. KM=0.272 mM for alpha-ketoglutarate (isoform Long at pH 7.5 and 30 degrees Celsius)1 Publication
    3. KM=0.044 mM for NADPH (isoform Long at pH 7.5 and 30 degrees Celsius)1 Publication
    4. KM=0.063 mM for saccharopine (isoform Long at pH 7 and 30 degrees Celsius)1 Publication
    5. KM=0.035 mM for saccharopine (isoform Long at pH 9 and 30 degrees Celsius)1 Publication
    6. KM=0.130 mM for saccharopine (isoform Short at pH 7 and 30 degrees Celsius)1 Publication
    7. KM=0.050 mM for saccharopine (isoform Short at pH 9 and 30 degrees Celsius)1 Publication
    8. KM=0.374 mM for NAD (isoform Long at pH 7 and 30 degrees Celsius)1 Publication
    9. KM=0.698 mM for NAD (isoform Long at pH 9 and 30 degrees Celsius)1 Publication
    10. KM=0.333 mM for NAD (isoform Short at pH 7 and 30 degrees Celsius)1 Publication
    11. KM=0.759 mM for NAD (isoform Short at pH 9 and 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.5 for LKR activity of isoform Long, and 9 for SDH activity of both isoforms Long and Short.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity Source: UniProtKB-EC
    2. saccharopine dehydrogenase (NADP+, L-lysine-forming) activity Source: UniProtKB-EC

    GO - Biological processi

    1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    BioCyciARA:AT4G33150-MONOMER.
    ARA:GQT-806-MONOMER.
    ARA:GQT-807-MONOMER.
    UniPathwayiUPA00868; UER00835.
    UPA00868; UER00836.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-aminoadipic semialdehyde synthase
    Alternative name(s):
    cAt-LKR/SDH
    Short name:
    LKR/SDH
    Including the following 2 domains:
    Lysine ketoglutarate reductase (EC:1.5.1.8)
    Short name:
    LKR
    Saccharopine dehydrogenase (EC:1.5.1.9)
    Alternative name(s):
    cAt-SDH
    Short name:
    SDH
    Gene namesi
    Name:LKR/SDH
    Synonyms:LKR, SDH
    Ordered Locus Names:At4g33150
    ORF Names:F4I10.80
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G33150.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi238 – 2381T → A or D: No effect on LKR and SDH activity. 1 Publication
    Mutagenesisi407 – 4071S → A: No effect on LKR and SDH activity. 1 Publication
    Mutagenesisi407 – 4071S → D: No LKR activity, but no effect on SDH activity. 1 Publication
    Mutagenesisi458 – 4581S → A: Reduced LKR activity, but no effect on SDH activity. 1 Publication
    Mutagenesisi458 – 4581S → D: No effect on LKR and SDH activity. 1 Publication
    Mutagenesisi551 – 5544NEDY → IEGR: Loss of LKR activity stimulation by NaCl.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10641064Alpha-aminoadipic semialdehyde synthasePRO_0000226070Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei238 – 2381Phosphothreonine1 Publication
    Modified residuei458 – 4581Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation of Ser-458 seems important for the LKR activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9SMZ4.
    PRIDEiQ9SMZ4.

    Expressioni

    Tissue specificityi

    Ubiquitous, with higher levels in flowers. Isoform Long is mostly present in young leaves, cotyledons, root tips and mature root parts. Whereas isoform Short is mostly expressed in cotyledons and at low levels in all root parts.2 Publications

    Developmental stagei

    In flowers, confined to ovules and vascular tissue of anther filament. In developing and mature seeds, expressed in embryo and the outer layers of the endosperm.1 Publication

    Inductioni

    Lysine, Sugar starvation, ABA and MeJA induce isoform Long, but not isoform Short (at protein level). Nitrogen starvation repress isoform Long, but not isoform Short (at protein level). Isoform Long and isoform Short are both slightly induced by NaCl and drought stress, but repressed by sugars.2 Publications

    Gene expression databases

    ArrayExpressiQ9SMZ4.
    GenevestigatoriQ9SMZ4.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SMZ4.
    SMRiQ9SMZ4. Positions 214-239, 589-1062.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 445422Lysine-ketoglutarate reductaseAdd
    BLAST
    Regioni583 – 1064482Saccharopine dehydrogenaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the AlaDH/PNT family.Curated
    In the C-terminal section; belongs to the saccharopine dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1748.
    InParanoidiQ9SMZ4.
    PhylomeDBiQ9SMZ4.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR007886. AlaDH/PNT_N.
    IPR007698. AlaDH/PNT_NAD(H)-bd.
    IPR007545. LOR/SDH_bifunc_enz_cons_dom.
    IPR016040. NAD(P)-bd_dom.
    IPR005097. Saccharopine_DH/HSpermid_syn.
    [Graphical view]
    PfamiPF01262. AlaDh_PNT_C. 1 hit.
    PF05222. AlaDh_PNT_N. 1 hit.
    PF03435. Saccharop_dh. 1 hit.
    PF04455. Saccharop_dh_N. 1 hit.
    [Graphical view]
    SMARTiSM01002. AlaDh_PNT_C. 1 hit.
    SM01003. AlaDh_PNT_N. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Long (identifier: Q9SMZ4-1) [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

    MNSNGHEEEK KLGNGVVGIL AETVNKWERR TPLTPSHCAR LLHGGKDRTG     50
    ISRIVVQPSA KRIHHDALYE DVGCEISDDL SDCGLILGIK QPELEMILPE 100
    RAYAFFSHTH KAQKENMPLL DKILSERVTL CDYELIVGDH GKRLLAFGKY 150
    AGRAGLVDFL HGLGQRKLIL GYSTPFLSLG ASYMYSSLAA AKAAVISVGE 200
    EIASQGLPLG ICPLVFVFTG TGNVSLGAQE IFKLLPHTFV EPSKLPELFV 250
    KDKGISQNGI STKRVYQVYG CIITSQDMVE HKDPSKSFDK ADYYAHPEHY 300
    NPVFHEKISP YTSVLVNCMY WEKRFPCLLS TKQLQDLTKK GLPLVGICDI 350
    TCDIGGSIEF VNRATLIDSP FFRFNPSNNS YYDDMDGDGV LCMAVDILPT 400
    EFAKEASQHF GDILSGFVGS LASMTEISDL PAHLKRACIS YRGELTSLYE 450
    YIPRMRKSNP EEAQDNIIAN GVSSQRTFNI LVSLSGHLFD KFLINEALDM 500
    IEAAGGSFHL AKCELGQSAD AESYSELEVG ADDKRVLDQI IDSLTRLANP 550
    NEDYISPHRE ANKISLKIGK VQQENEIKEK PEMTKKSGVL ILGAGRVCRP 600
    AADFLASVRT ISSQQWYKTY FGADSEEKTD VHVIVASLYL KDAKETVEGI 650
    SDVEAVRLDV SDSESLLKYV SQVDVVLSLL PASCHAVVAK TCIELKKHLV 700
    TASYVDDETS MLHEKAKSAG ITILGEMGLD PGIDHMMAMK MINDAHIKKG 750
    KVKSFTSYCG GLPSPAAANN PLAYKFSWNP AGAIRAGQNP AKYKSNGDII 800
    HVDGKNLYDS AARFRVPNLP AFALECFPNR DSLVYGEHYG IESEATTIFR 850
    GTLRYEGFSM IMATLSKLGF FDSEANQVLS TGKRITFGAL LSNILNKDAD 900
    NESEPLAGEE EISKRIIKLG HSKETAAKAA KTIVFLGFNE EREVPSLCKS 950
    VFDATCYLME EKLAYSGNEQ DMVLLHHEVE VEFLESKRIE KHTATLLEFG 1000
    DIKNGQTTTA MAKTVGIPAA IGALLLIEDK IKTRGVLRPL EAEVYLPALD 1050
    ILQAYGIKLM EKAE 1064

    Note: Contains both LKR and SDH activities.

    Length:1,064
    Mass (Da):117,149
    Last modified:May 1, 2000 - v1
    Checksum:i6CA4EBDB22898C7E
    GO
    Isoform Short (identifier: Q9SMZ4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-582: Missing.

    Note: Contains only SDH activity.

    Show »
    Length:482
    Mass (Da):52,704
    Checksum:iA249E25010D557A3
    GO

    Sequence cautioni

    The sequence AAK97099.1 differs from that shown. Reason: Chimeric cDNA. Its C-terminal part is derived from gene At1G61240 whose function is unknown. Originally thought to be an alternative splicing form of At4g33150.
    The sequence AAK64010.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAM16268.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1693KLI → YLS in AAB53975. (PubMed:9286108)Curated
    Sequence conflicti167 – 1693KLI → YLS in AAB96825. (PubMed:9426595)Curated
    Sequence conflicti167 – 1693KLI → YLS in AAB96826. (PubMed:9426595)Curated
    Sequence conflicti167 – 1693KLI → YLS in AAK97099. (PubMed:12226495)Curated
    Sequence conflicti324 – 3241R → S in AAB53975. (PubMed:9286108)Curated
    Sequence conflicti324 – 3241R → S in AAK97099. (PubMed:12226495)Curated
    Sequence conflicti621 – 6211F → V in AAK64010. (PubMed:14593172)Curated
    Sequence conflicti621 – 6211F → V in AAM16268. (PubMed:14593172)Curated
    Sequence conflicti715 – 7151K → N in AAB53975. (PubMed:9286108)Curated
    Sequence conflicti715 – 7151K → N in AAD00700. (PubMed:9286108)Curated
    Sequence conflicti735 – 7351H → P in AAB53975. (PubMed:9286108)Curated
    Sequence conflicti735 – 7351H → P in AAD00700. (PubMed:9286108)Curated
    Sequence conflicti739 – 7391M → K in AAB53975. (PubMed:9286108)Curated
    Sequence conflicti739 – 7391M → K in AAD00700. (PubMed:9286108)Curated
    Sequence conflicti746 – 7483HIK → PIT in AAB53975. (PubMed:9286108)Curated
    Sequence conflicti746 – 7483HIK → PIT in AAD00700. (PubMed:9286108)Curated
    Sequence conflicti765 – 7651P → R in AAB53975. (PubMed:9286108)Curated
    Sequence conflicti765 – 7651P → R in AAD00700. (PubMed:9286108)Curated
    Sequence conflicti827 – 8271F → L in AAB96825. (PubMed:9426595)Curated
    Sequence conflicti827 – 8271F → L in AAB96826. (PubMed:9426595)Curated
    Sequence conflicti1040 – 10401L → F in AAB96825. (PubMed:9426595)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 582582Missing in isoform Short. 1 PublicationVSP_018641Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90522 mRNA. Translation: AAB53975.1.
    U90523 mRNA. Translation: AAD00700.1.
    U95758 Genomic DNA. Translation: AAB96825.1.
    U95759 mRNA. Translation: AAB96826.1.
    AF295389 mRNA. Translation: AAK97099.1. Sequence problems.
    AL035525 Genomic DNA. Translation: CAB36789.1.
    AL161583 Genomic DNA. Translation: CAB80032.1.
    CP002687 Genomic DNA. Translation: AEE86184.1.
    AY039906 mRNA. Translation: AAK64010.1. Different initiation.
    AY094007 mRNA. Translation: AAM16268.1. Different initiation.
    PIRiT05195.
    RefSeqiNP_001154283.1. NM_001160811.1. [Q9SMZ4-2]
    UniGeneiAt.20921.

    Genome annotation databases

    EnsemblPlantsiAT4G33150.1; AT4G33150.1; AT4G33150.
    AT4G33150.2; AT4G33150.2; AT4G33150.
    GeneIDi829452.
    KEGGiath:AT4G33150.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90522 mRNA. Translation: AAB53975.1 .
    U90523 mRNA. Translation: AAD00700.1 .
    U95758 Genomic DNA. Translation: AAB96825.1 .
    U95759 mRNA. Translation: AAB96826.1 .
    AF295389 mRNA. Translation: AAK97099.1 . Sequence problems.
    AL035525 Genomic DNA. Translation: CAB36789.1 .
    AL161583 Genomic DNA. Translation: CAB80032.1 .
    CP002687 Genomic DNA. Translation: AEE86184.1 .
    AY039906 mRNA. Translation: AAK64010.1 . Different initiation.
    AY094007 mRNA. Translation: AAM16268.1 . Different initiation.
    PIRi T05195.
    RefSeqi NP_001154283.1. NM_001160811.1. [Q9SMZ4-2 ]
    UniGenei At.20921.

    3D structure databases

    ProteinModelPortali Q9SMZ4.
    SMRi Q9SMZ4. Positions 214-239, 589-1062.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q9SMZ4.
    PRIDEi Q9SMZ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G33150.1 ; AT4G33150.1 ; AT4G33150 .
    AT4G33150.2 ; AT4G33150.2 ; AT4G33150 .
    GeneIDi 829452.
    KEGGi ath:AT4G33150.

    Organism-specific databases

    TAIRi AT4G33150.

    Phylogenomic databases

    eggNOGi COG1748.
    InParanoidi Q9SMZ4.
    PhylomeDBi Q9SMZ4.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00835 .
    UPA00868 ; UER00836 .
    BioCyci ARA:AT4G33150-MONOMER.
    ARA:GQT-806-MONOMER.
    ARA:GQT-807-MONOMER.

    Gene expression databases

    ArrayExpressi Q9SMZ4.
    Genevestigatori Q9SMZ4.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR007886. AlaDH/PNT_N.
    IPR007698. AlaDH/PNT_NAD(H)-bd.
    IPR007545. LOR/SDH_bifunc_enz_cons_dom.
    IPR016040. NAD(P)-bd_dom.
    IPR005097. Saccharopine_DH/HSpermid_syn.
    [Graphical view ]
    Pfami PF01262. AlaDh_PNT_C. 1 hit.
    PF05222. AlaDh_PNT_N. 1 hit.
    PF03435. Saccharop_dh. 1 hit.
    PF04455. Saccharop_dh_N. 1 hit.
    [Graphical view ]
    SMARTi SM01002. AlaDh_PNT_C. 1 hit.
    SM01003. AlaDh_PNT_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of lysine catabolism through lysine-ketoglutarate reductase and saccharopine dehydrogenase in Arabidopsis."
      Tang G., Miron D., Zhu-Shimoni J.X., Galili G.
      Plant Cell 9:1305-1316(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: cv. Columbia.
      Tissue: Seedling hypocotyl.
    2. "Lysine-ketoglutarate reductase and saccharopine dehydrogenase from Arabidopsis thaliana: nucleotide sequence and characterization."
      Epelbaum S., McDevitt R., Falco S.C.
      Plant Mol. Biol. 35:735-748(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG), FUNCTION.
      Strain: cv. Columbia and cv. Landsberg erecta.
    3. "The bifunctional LKR/SDH locus of plants also encodes a highly active monofunctional lysine-ketoglutarate reductase using a polyadenylation signal located within an intron."
      Tang G., Zhu X., Gakiere B., Levanony H., Kahana A., Galili G.
      Plant Physiol. 130:147-154(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 529-1064 (ISOFORM LONG).
      Strain: cv. Columbia.
    7. "A novel composite locus of Arabidopsis encoding two polypeptides with metabolically related but distinct functions in lysine catabolism."
      Tang G., Zhu X., Tang X., Galili G.
      Plant J. 23:195-203(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE INITIATION.
    8. "Characterization of the two saccharopine dehydrogenase isozymes of lysine catabolism encoded by the single composite AtLKR/SDH locus of Arabidopsis."
      Zhu X., Tang G., Galili G.
      Plant Physiol. 124:1363-1371(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "A T-DNA insertion knockout of the bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase gene elevates lysine levels in Arabidopsis seeds."
      Zhu X., Tang G., Granier F., Bouchez D., Galili G.
      Plant Physiol. 126:1539-1545(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains."
      Zhu X., Tang G., Galili G.
      J. Biol. Chem. 277:49655-49661(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBUNIT, PHOSPHORYLATION AT THR-238 AND SER-458, MUTAGENESIS OF THR-238; SER-407; SER-458 AND 551-ASN--ARG-554.
    11. "Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is concertedly regulated by metabolic and stress-associated signals."
      Stepansky A., Galili G.
      Plant Physiol. 133:1407-1415(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    12. "Regulation of lysine catabolism in Arabidopsis through concertedly regulated synthesis of the two distinct gene products of the composite AtLKR/SDH locus."
      Stepansky A., Yao Y., Tang G., Galili G.
      J. Exp. Bot. 56:525-536(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.

    Entry informationi

    Entry nameiAASS_ARATH
    AccessioniPrimary (citable) accession number: Q9SMZ4
    Secondary accession number(s): O04155
    , O04156, O04884, Q7DM71, Q947M5, Q94BT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 93 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