|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
DOI=10.1023/A:1005849228945; PubMed=9207844 [NCBI, ExPASy, EBI, Israel, Japan]
Tang G.,
Zhu-Shimoni J.X.,
Amir R.,
Zchori I.B.-T.,
Galili G.;
"Cloning and expression of an Arabidopsis thaliana cDNA encoding a monofunctional aspartate kinase homologous to the lysine-sensitive enzyme of Escherichia coli.";
Plant Mol. Biol. 34:287-293(1997).
|
[2]
|
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
TISSUE=Leaf;
Frankard V.M.S.,
Vauterin M.,
Jacobs M.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
|
[3]
|
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/4.6.401; PubMed=9501997 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura Y.,
Sato S.,
Kaneko T.,
Kotani H.,
Asamizu E.,
Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
|
[4]
|
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
DOI=10.1111/j.1742-4658.2006.05573.x; PubMed=17140415 [NCBI, ExPASy, EBI, Israel, Japan]
Curien G.,
Laurencin M.,
Robert-Genthon M.,
Dumas R.;
"Allosteric monofunctional aspartate kinases from Arabidopsis.";
FEBS J. 274:164-176(2007).
|
|
|
|
- FUNCTION: Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
- ENZYME REGULATION: Allosterically inhibited by lysine, but not by S-adenosyl-L-methionine (SAM). K(0.5) for lysine in the presence of physiological concentrations of substrates is 12.5 µM. No inhibition by threonine or leucine and no activation or inhibition by alanine, cysteine, isoleucine, serine, valine, methionine, glutamine, asparagine, glutamic acid or arginine.
- BIOPHYSICOCHEMICAL PROPERTIES:
- 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-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
- SUBCELLULAR LOCATION: Plastid, chloroplast (Potential).
- TISSUE SPECIFICITY: Expressed in stems, leaves, floral organs and young seedlings.
- SIMILARITY: Belongs to the aspartokinase family.
- SIMILARITY: Contains 2 ACT domains.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 544 AA [This is the length of the unprocessed precursor] |
Molecular weight: 59605 Da [This is the MW of the unprocessed precursor] |
CRC64: 7DBCFDC1138645AC [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MASLQLYGVK TPGLALSSKR LEFASKGACF SVTLPSSSAV FRDVEHSCRN IGLRVSCEAL
70 80 90 100 110 120
RVDLLQRKEP ETCDSSGTGK ELTCVMKFGG SSVESAERMK EVANLILSFP DERPVIVLSA
130 140 150 160 170 180
MGKTTNKLLK AGEKAVTCGV TNVESIEELS FIKELHLRTA HELGVETTVI EKHLEGLHQL
190 200 210 220 230 240
LKGISMMKEL TLRTRDYLVS FGECMSTRLF SAYLNKIGHK ARQYDAFEIG FITTDDFTNA
250 260 270 280 290 300
DILEATYPAV SKTLVGDWSK ENAVPVVTGY LGKGWRSCAI TTLGRGGSDL TATTIGKALG
310 320 330 340 350 360
LREIQVWKDV DGVLTCDPNI YPGAQSVPYL TFDEAAELAY FGAQVLHPLS MRPARDGDIP
370 380 390 400 410 420
VRVKNSYNPT APGTVITRSR DMSKAVLTSI VLKRNVTMLD IASTRMLGQY GFLAKVFTTF
430 440 450 460 470 480
EDLGISVDVV ATSEVSISLT LDPAKLWGRE LIQRVNELDN LVEELEKIAV VKLLQRRSII
490 500 510 520 530 540
SLIGNVQKSS LILEKVFQVF RSNGVNVQMI SQGASKVNIS LIVNDEEAEQ CVRALHSAFF
ETDP
|
O23653 in FASTA format |
|
ExPASy Home page
SIB Switzerland
