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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1006/prep.2001.1539; PubMed=11812230 [NCBI, ExPASy, EBI, Israel, Japan]
Paris S.,
Wessel P.M.,
Dumas R.;
"Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana.";
Protein Expr. Purif. 24:105-110(2002).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
DOI=10.1101/gr.1515604; PubMed=14993207 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation.";
Genome Res. 14:406-413(2004).
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[4]
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ENZYME REGULATION, AND MUTAGENESIS OF ILE-441; GLN-443; ILE-522 AND GLN-524.
DOI=10.1074/jbc.M207379200; PubMed=12435751 [NCBI, ExPASy, EBI, Israel, Japan]
Paris S.,
Viemon C.,
Curien G.,
Dumas R.;
"Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine.";
J. Biol. Chem. 278:5361-5366(2003).
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[5]
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ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1074/jbc.M509324200; PubMed=16216875 [NCBI, ExPASy, EBI, Israel, Japan]
Curien G.,
Ravanel S.,
Robert M.,
Dumas R.;
"Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. Physiological context sets the specificity.";
J. Biol. Chem. 280:41178-41183(2005).
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- CATALYTIC ACTIVITY: L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.
- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
- ENZYME REGULATION: 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.
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=11.6 mM for aspartate for the aspartokinase activity (in the presence of 40 mM ATP); | | 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); | | 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); | | KM=26.4 mM for aspartate for the aspartokinase activity (in the presence of 100 mM ATP and 0.5 mM threonine); | | KM=5.5 mM for ATP for the aspartokinase activity (in the presence of 50 mM aspartate); | | 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); | | 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); | | KM=5.2 mM for homoserine for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 1 mM NADP); | | KM=1.4 mM for aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity (in the presence of NADPH); | | 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); | | 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); | | KM=166.1 µM for NADP for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 50 mM homoserine); | | 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); | | Vmax=5.4 µmol/min/mg enzyme toward aspartylhydroxamate for the aspartokinase activity; | | Vmax=165 µmol/min/mg enzyme toward aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity; | | Vmax=18.8 µmol/min/mg enzyme toward NADPH for the reverse reaction of the homoserine dehydrogenase activity; | |
- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 1/4.
- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.
- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
- SUBUNIT: Homo- or heterodimer (Potential).
- SUBCELLULAR LOCATION: Plastid, chloroplast.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
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| Name | 2 |
| Isoform ID | O81852-2 |
| Note: Derived from EST data. No experimental confirmation available. |
| Features which should be applied to build the isoform sequence: VSP_019798. |
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- SIMILARITY: In the N-terminal section; belongs to the aspartokinase family.
- SIMILARITY: In the C-terminal section; belongs to the homoserine dehydrogenase family.
- SIMILARITY: Contains 2 ACT domains.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 916 AA [This is the length of the unprocessed precursor] |
Molecular weight: 100250 Da [This is the MW of the unprocessed precursor] |
CRC64: 7ECD984DAFC97C4F [This is a checksum on the sequence] |
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10 20 30 40 50 60
MATLKPSFTV SPPNSNPIRF GSFPPQCFLR VPKPRRLILP RFRKTTGGGG GLIRCELPDF
70 80 90 100 110 120
HLSATATTVS GVSTVNLVDQ VQIPKGEMWS VHKFGGTCVG NSQRIRNVAE VIINDNSERK
130 140 150 160 170 180
LVVVSAMSKV TDMMYDLIRK AQSRDDSYLS ALEAVLEKHR LTARDLLDGD DLASFLSHLH
190 200 210 220 230 240
NDISNLKAML RAIYIAGHAS ESFSDFVAGH GELWSAQMLS YVVRKTGLEC KWMDTRDVLI
250 260 270 280 290 300
VNPTSSNQVD PDFGESEKRL DKWFSLNPSK IIIATGFIAS TPQNIPTTLK RDGSDFSAAI
310 320 330 340 350 360
MGALLRARQV TIWTDVDGVY SADPRKVNEA VILQTLSYQE AWEMSYFGAN VLHPRTIIPV
370 380 390 400 410 420
MRYNIPIVIR NIFNLSAPGT IICQPPEDDY DLKLTTPVKG FATIDNLALI NVEGTGMAGV
430 440 450 460 470 480
PGTASDIFGC VKDVGANVIM ISQASSEHSV CFAVPEKEVN AVSEALRSRF SEALQAGRLS
490 500 510 520 530 540
QIEVIPNCSI LAAVGQKMAS TPGVSCTLFS ALAKANINVR AISQGCSEYN VTVVIKREDS
550 560 570 580 590 600
VKALRAVHSR FFLSRTTLAM GIVGPGLIGA TLLDQLRDQA AVLKQEFNID LRVLGITGSK
610 620 630 640 650 660
KMLLSDIGID LSRWRELLNE KGTEADLDKF TQQVHGNHFI PNSVVVDCTA DSAIASRYYD
670 680 690 700 710 720
WLRKGIHVIT PNKKANSGPL DQYLKLRDLQ RKSYTHYFYE ATVGAGLPII STLRGLLETG
730 740 750 760 770 780
DKILRIEGIC SGTLSYLFNN FVGDRSFSEV VTEAKNAGFT EPDPRDDLSG TDVARKVIIL
790 800 810 820 830 840
ARESGLKLDL ADLPIRSLVP EPLKGCTSVE EFMEKLPQYD GDLAKERLDA ENSGEVLRYV
850 860 870 880 890 900
GVVDAVNQKG TVELRRYKKE HPFAQLAGSD NIIAFTTTRY KDHPLIVRGP GAGAQVTAGG
910
IFSDILRLAS YLGAPS
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O81852 in FASTA format |
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