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UniProtKB/Swiss-Prot entry Q9S702


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

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Entry information
Entry name AK3_ARATH
Primary accession number Q9S702
Secondary accession numbers None
Integrated into Swiss-Prot on September 5, 2006
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 45)
Name and origin of the protein
Protein name Aspartokinase 3, chloroplastic [Precursor]
Synonyms EC 2.7.2.4
Aspartate kinase 3
Gene name
Name: AK3
Synonyms: AK-LYS3
OrderedLocusNames: At3g02020
ORFNames: F28J7.35, F1C9.20
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], FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1266/ggs.76.189; PubMed=11569502 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshioka Y., Kurei S., Machida Y.;
"Identification of a monofunctional aspartate kinase gene of Arabidopsis thaliana with spatially and temporally regulated expression.";
Genes Genet. Syst. 76:189-198(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[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).
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
AC010797; AAF03452.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC011664; AAF14833.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY088366; AAM65905.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK226200; BAE98365.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_186851.1; -.
UniGene At.41192
3D structure databases
SMR Q9S702; 81-541.
ModBase Q9S702.
Organism-specific databases
TAIR At3g02020; -.
Gene expression databases
GermOnline AT3G02020; Arabidopsis thaliana.
Ontologies
GO
GO:0004072; Molecular function: aspartate kinase activity (inferred from genetic interaction from TAIR).
QuickGo view.
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 Q9S702.
Genome annotation databases
GeneID 821287; -.
GenomeReviews BA000014_GR; AT3G02020.
KEGG ath:AT3G02020; -.
NMPDR fig|3702.1.peg.12136; -.
Other
ProtoNet Q9S702.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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    85  85     Chloroplast (Potential). 
CHAIN   86   559  474     Aspartokinase 3, chloroplastic. PRO_0000248159
DOMAIN   403   478  76     ACT 1. 
DOMAIN   496   538  43     ACT 2. 
BINDING   88    88        ATP (By similarity). 
BINDING   91    91        ATP; via amide nitrogen (By similarity). 
BINDING   120   120        ATP (By similarity). 
BINDING   204   204        Substrate (By similarity). 
Sequence information
Length: 559 AA [This is the length of the unprocessed precursor] Molecular weight: 61216 Da [This is the MW of the unprocessed precursor] CRC64: FBC8A4A0E814F349 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAASMQFYGV KTPELALNSK RIEFSSKGLN FSALVSSARV FSRNVDRSCK NIALRVTCEA 

        70         80         90        100        110        120 
GRVELLERKA SETFKLNKTE KKLTCVMKFG GSSVASAERM IQVAKLILSF PDEKPVVVLS 

       130        140        150        160        170        180 
AMAKTTNKLL MAGEKAVCCG VTNVDTIEEL SYIKELHIRT AHELGVETAV IAEHLEGLEQ 

       190        200        210        220        230        240 
LLKGVAMMKE LTLRSRDYLV SFGECMSTRL FAAYLNKIGH KARQYDAFEI GIITTDDFTN 

       250        260        270        280        290        300 
ADILEATYPA VSKKLLGDWS KENALPVVTG FLGKGWRSCA VTTLGRGGSD LTATTIGKAL 

       310        320        330        340        350        360 
GLREIQVWKD VDGVLTCDPN IYCGAQPVPH LTFDEAAELA YFGAQVLHPL SMRPAREGNI 

       370        380        390        400        410        420 
PVRVKNSYNP TAPGTVITRS RDMSKAVLTS IVLKRNVTML DITSTRMLGQ YGFLAKVFST 

       430        440        450        460        470        480 
FEKLGISVDV VATSEVSISL TLDPSKFCSR ELIQHELDQV VEELEKIAVV NLLRHRSIIS 

       490        500        510        520        530        540 
LIGNVQRSSF ILEKGFRVLR TNGINVQMIS QGASKVNISL IVNDDEAEHC VKALHSAFFE 

       550 
TDTCEAVSEC PTGYIAASS 

Q9S702 in FASTA format

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