Reviewed, UniProtKB/Swiss-Prot Q9S702 (AK3_ARATH)

Names and origin

Protein names

Recommended name:
    Aspartokinase 3, chloroplastic
    EC=2.7.2.4
Alternative name(s):
    Aspartate kinase 3

Gene names

Name:	AK3
Synonyms:	AK-LYS3
Ordered Locus Names:	At3g02020
ORF Names:	F28J7.35, F1C9.20

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway. Ref.1
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 7.4 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. Ref.5
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
Subcellular location	Plastid › chloroplast Potential.
Tissue specificity	Highly expressed in xylem of leaves and hypocotyls, stele of roots and in trichomes after bolting. Weak expression in veins and mesophyll cells of caulone leaves, inflorescence stems, sepals, petals and stigmata. Ref.1
Sequence similarities	Belongs to the aspartokinase family. Contains 2 ACT domains.
Biophysicochemical properties	Kinetic parameters: K(cat) is 8.4/sec. KM=560 µM for ATP KM=1095 µM for aspartate

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Threonine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Repeat Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid binding Inferred from electronic annotation. Source: InterPro aspartate kinase activity Ref.1 Inferred from genetic interaction. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 85	85	Chloroplast Potential
	Chain	86 – 559	474	Aspartokinase 3, chloroplastic		PRO_0000248159
Regions
	Domain	403 – 478	76	ACT 1
	Domain	496 – 538	43	ACT 2
Sites
	Binding site	88	1	ATP By similarity
	Binding site	91	1	ATP; via amide nitrogen By similarity
	Binding site	120	1	ATP By similarity
	Binding site	204	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9S702-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: FBC8A4A0E814F349	FASTA	559	61,216
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a monofunctional aspartate kinase gene of Arabidopsis thaliana with spatially and temporally regulated expression." Yoshioka Y., Kurei S., Machida Y. Genes Genet. Syst. 76:189-198(2001) [PubMed: 11569502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." 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. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." 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. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Allosteric monofunctional aspartate kinases from Arabidopsis." Curien G., Laurencin M., Robert-Genthon M., Dumas R. FEBS J. 274:164-176(2007) [PubMed: 17140415] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC010797 Genomic DNA. Translation: AAF03452.1. AC011664 Genomic DNA. Translation: AAF14833.1. AY088366 mRNA. Translation: AAM65905.1. AK226200 mRNA. Translation: BAE98365.1.
IPI	IPI00527939.
RefSeq	NP_186851.1.
UniGene	At.41192
3D structure databases
HSSP	HSSP built from PDB template 2CDQ based on UniProtKB Q9LYU8.
SMR	Q9S702. Positions 81-541.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9S702.
Proteomic databases
PRIDE	Q9S702.
Genome annotation databases
GeneID	821287.
GenomeReviews	Gene locus AT3G02020 in contig BA000014_GR.
KEGG	ath:AT3G02020.
NMPDR	fig|3702.1.peg.12136.
Organism-specific databases
TAIR	At3g02020.
Phylogenomic databases
eggNOG	KOG0456.
HOGENOM	HBG724395.
InParanoid	Q9S702.
OMA	DITSTRM.
PhylomeDB	Q9S702.
Enzyme and pathway databases
BRENDA	2.7.2.4. 302.
Gene expression databases
Genevestigator	Q9S702.
GermOnline	AT3G02020. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001048. Asp/Glu/Uridylate_kinase. IPR001341. Asp_kinase_dom. IPR018042. Aspartate_kinase_CS. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF01842. ACT. 1 hit. [Graphical view]
TIGRFAMs	TIGR00657. asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AK3_ARATH

Accession

Primary (citable) accession number: Q9S702

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)