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UniProtKB/Swiss-Prot entry Q9LYU8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AK1_ARATH
Primary accession number Q9LYU8
Secondary accession number O23152
Integrated into Swiss-Prot on September 5, 2006
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 46)
Name and origin of the protein
Protein name Aspartokinase 1, chloroplastic [Precursor]
Synonyms EC 2.7.2.4
Aspartate kinase 1
Gene name
Name: AK1
Synonyms: AK, AK-LYS1
OrderedLocusNames: At5g13280
ORFNames: T31B5.100
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1023/A:1005863128558; PubMed=9207839 [NCBI, ExPASy, EBI, Israel, Japan]
Frankard V., Vauterin M., Jacobs M.;
"Molecular characterisation of an Arabidopsis thaliana cDNA coding for a monofunctional aspartate kinase.";
Plant Mol. Biol. 34:233-242(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
ENZYME REGULATION.
DOI=10.1038/287357a0; PubMed=6252474 [NCBI, ExPASy, EBI, Israel, Japan]
Rognes S.E., Lea P.J., Miflin B.J.;
"S-adenosylmethionine -- a novel regulator of aspartate kinase.";
Nature 287:357-359(1980).
[5]
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).
[6]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 61-569 IN COMPLEX WITH SUBSTRATE ANALOG AND ALLOSTERIC REGULATORS, AND SUBUNIT.
DOI=10.1105/tpc.105.040451; PubMed=16731588 [NCBI, ExPASy, EBI, Israel, Japan]
Mas-Droux C., Curien G., Robert-Genthon M., Laurencin M., Ferrer J.L., Dumas R.;
"A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase.";
Plant Cell 18:1681-1692(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X98873; CAA67376.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL163491; CAB86635.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000493; AAN18062.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY057674; AAL15305.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T48575; T48575.
RefSeq NP_196832.1; -.
UniGene At.124
3D structure databases
PDB
2CDQ; X-ray; 2.85 A; A/B=61-569.[ExPASy / RCSB / EBI]
PDBsum 2CDQ; -.
ModBase Q9LYU8.
Organism-specific databases
TAIR At5g13280; -.
Gene expression databases
GermOnline AT5G13280; Arabidopsis thaliana.
Family and domain databases
InterPro IPR002912; ACT_bd.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR001341; Asp_kin_reg.
Graphical view of domain structure.
Gene3D G3DSA:3.40.1160.10; Aa_kinase; 1.
Pfam PF00696; AA_kinase; 1.
PF01842; ACT; 2.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00657; asp_kinases; 1.
PROSITE PS00324; ASPARTOKINASE; 1.
BLOCKS Q9LYU8.
Genome annotation databases
GeneID 831169; -.
GenomeReviews BA000015_GR; AT5G13280.
KEGG ath:AT5G13280; -.
NMPDR fig|3702.1.peg.23445; -.
Other
ProtoNet Q9LYU8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; ATP-binding; Chloroplast; Complete proteome; Kinase; Nucleotide-binding; Plastid; Repeat; Threonine biosynthesis; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    90  90     Chloroplast (Potential). 
CHAIN   91   569  479     Aspartokinase 1, chloroplastic. PRO_0000248157
DOMAIN   406   481  76     ACT 1. 
DOMAIN   482   549  68     ACT 2. 
BINDING   91    91        ATP (By similarity). 
BINDING   94    94        ATP; via amide nitrogen (By similarity). 
BINDING   123   123        ATP (By similarity). 
BINDING   207   207        Substrate. 
BINDING   413   413        Allosteric effector lysine; via carbonyl oxygen. 
BINDING   415   415        Allosteric effector lysine; via amide nitrogen. 
BINDING   430   430        Allosteric effector S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen. 
BINDING   431   431        Allosteric effector lysine; via amide nitrogen. 
BINDING   432   432        Allosteric effector lysine; via carbonyl oxygen. 
BINDING   437   437        Allosteric effector lysine; via carbonyl oxygen. 
BINDING   452   452        Allosteric effector S-adenosyl-L-methionine. 
BINDING   453   453        Allosteric effector S-adenosyl-L-methionine; via amide nitrogen. 
CONFLICT   369   369        N -> S (in Ref. 1; CAA67376). 
CONFLICT   569   569        N -> D (in Ref. 1; CAA67376). 
Sequence information
Length: 569 AA [This is the length of the unprocessed precursor] Molecular weight: 62298 Da [This is the MW of the unprocessed precursor] CRC64: F66A35F4E84DC429 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAATRVRCCH SNAAFTRLPL TRHRNSPTLP ISLNRVDFPT LKKLSLPIGD GSSIRKVSGS 

        70         80         90        100        110        120 
GSRNIVRAVL EEKKTEAITE VDEKGITCVM KFGGSSVASA ERMKEVADLI LTFPEESPVI 

       130        140        150        160        170        180 
VLSAMGKTTN NLLLAGEKAV SCGVSNASEI EELSIIKELH IRTVKELNID PSVILTYLEE 

       190        200        210        220        230        240 
LEQLLKGIAM MKELTLRTRD YLVSFGECLS TRIFAAYLNT IGVKARQYDA FEIGFITTDD 

       250        260        270        280        290        300 
FTNGDILEAT YPAVAKRLYD DWMHDPAVPI VTGFLGKGWK TGAVTTLGRG GSDLTATTIG 

       310        320        330        340        350        360 
KALGLKEIQV WKDVDGVLTC DPTIYKRATP VPYLTFDEAA ELAYFGAQVL HPQSMRPARE 

       370        380        390        400        410        420 
GEIPVRVKNS YNPKAPGTII TKTRDMTKSI LTSIVLKRNV TMLDIASTRM LGQVGFLAKV 

       430        440        450        460        470        480 
FSIFEELGIS VDVVATSEVS ISLTLDPSKL WSRELIQQEL DHVVEELEKI AVVNLLKGRA 

       490        500        510        520        530        540 
IISLIGNVQH SSLILERAFH VLYTKGVNVQ MISQGASKVN ISFIVNEAEA EGCVQALHKS 

       550        560 
FFESGDLSEL LIQPRLGNGS PVRTLQVEN 

Q9LYU8 in FASTA format

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