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Protein

Alpha-aminoadipic semialdehyde synthase

Gene

LKR/SDH

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

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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciARA:AT4G33150-MONOMER.
ARA:GQT-806-MONOMER.
ARA:GQT-807-MONOMER.
ReactomeiREACT_310104. Lysine catabolism.
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 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G33150.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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. 1 Publication

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

ExpressionAtlasiQ9SMZ4. baseline and differential.
GenevestigatoriQ9SMZ4.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9SMZ4.
SMRiQ9SMZ4. Positions 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.
KOiK14157.
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. AlignAdd to basket

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

        10         20         30         40         50
MNSNGHEEEK KLGNGVVGIL AETVNKWERR TPLTPSHCAR LLHGGKDRTG
60 70 80 90 100
ISRIVVQPSA KRIHHDALYE DVGCEISDDL SDCGLILGIK QPELEMILPE
110 120 130 140 150
RAYAFFSHTH KAQKENMPLL DKILSERVTL CDYELIVGDH GKRLLAFGKY
160 170 180 190 200
AGRAGLVDFL HGLGQRKLIL GYSTPFLSLG ASYMYSSLAA AKAAVISVGE
210 220 230 240 250
EIASQGLPLG ICPLVFVFTG TGNVSLGAQE IFKLLPHTFV EPSKLPELFV
260 270 280 290 300
KDKGISQNGI STKRVYQVYG CIITSQDMVE HKDPSKSFDK ADYYAHPEHY
310 320 330 340 350
NPVFHEKISP YTSVLVNCMY WEKRFPCLLS TKQLQDLTKK GLPLVGICDI
360 370 380 390 400
TCDIGGSIEF VNRATLIDSP FFRFNPSNNS YYDDMDGDGV LCMAVDILPT
410 420 430 440 450
EFAKEASQHF GDILSGFVGS LASMTEISDL PAHLKRACIS YRGELTSLYE
460 470 480 490 500
YIPRMRKSNP EEAQDNIIAN GVSSQRTFNI LVSLSGHLFD KFLINEALDM
510 520 530 540 550
IEAAGGSFHL AKCELGQSAD AESYSELEVG ADDKRVLDQI IDSLTRLANP
560 570 580 590 600
NEDYISPHRE ANKISLKIGK VQQENEIKEK PEMTKKSGVL ILGAGRVCRP
610 620 630 640 650
AADFLASVRT ISSQQWYKTY FGADSEEKTD VHVIVASLYL KDAKETVEGI
660 670 680 690 700
SDVEAVRLDV SDSESLLKYV SQVDVVLSLL PASCHAVVAK TCIELKKHLV
710 720 730 740 750
TASYVDDETS MLHEKAKSAG ITILGEMGLD PGIDHMMAMK MINDAHIKKG
760 770 780 790 800
KVKSFTSYCG GLPSPAAANN PLAYKFSWNP AGAIRAGQNP AKYKSNGDII
810 820 830 840 850
HVDGKNLYDS AARFRVPNLP AFALECFPNR DSLVYGEHYG IESEATTIFR
860 870 880 890 900
GTLRYEGFSM IMATLSKLGF FDSEANQVLS TGKRITFGAL LSNILNKDAD
910 920 930 940 950
NESEPLAGEE EISKRIIKLG HSKETAAKAA KTIVFLGFNE EREVPSLCKS
960 970 980 990 1000
VFDATCYLME EKLAYSGNEQ DMVLLHHEVE VEFLESKRIE KHTATLLEFG
1010 1020 1030 1040 1050
DIKNGQTTTA MAKTVGIPAA IGALLLIEDK IKTRGVLRPL EAEVYLPALD
1060
ILQAYGIKLM EKAE

Note: Contains both LKR and SDH activities.

Length:1,064
Mass (Da):117,149
Last modified:April 30, 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 AAK64010.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAK97099.1 differs from that shown.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.Curated
The sequence AAM16268.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9SMZ4.
SMRiQ9SMZ4. Positions 589-1062.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ9SMZ4.
PRIDEiQ9SMZ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT4G33150.

Phylogenomic databases

eggNOGiCOG1748.
InParanoidiQ9SMZ4.
KOiK14157.
PhylomeDBiQ9SMZ4.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00835.
UPA00868; UER00836.
BioCyciARA:AT4G33150-MONOMER.
ARA:GQT-806-MONOMER.
ARA:GQT-807-MONOMER.
ReactomeiREACT_310104. Lysine catabolism.

Gene expression databases

ExpressionAtlasiQ9SMZ4. baseline and differential.
GenevestigatoriQ9SMZ4.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [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(1996) [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(2001) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2002) [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(1999) [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(1999) [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(2000) [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(2001) [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(2002) [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(2004) [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 6, 2006
Last sequence update: April 30, 2000
Last modified: March 31, 2015
This is version 97 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.