Aspartokinase 2, chloroplastic precursor - Arabidopsis thaliana (Mouse-ear cress)

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O23653 (AK2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aspartokinase 2, chloroplastic
EC=2.7.2.4

Alternative name(s):
Aspartate kinase 2

Gene names

Name:	AK2
Synonyms:	AK-LYS2, CARAB-AK-LYS
Ordered Locus Names:	At5g14060
ORF Names:	MUA22.6

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	544 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.
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. 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	Expressed in stems, leaves, floral organs and young seedlings. Ref.1
Sequence similarities	Belongs to the aspartokinase family. Contains 2 ACT domains.
Biophysicochemical properties	Kinetic parameters: K(cat) is 14.5/sec. K_M=980 µM for ATP Ref.5 K_M=1940 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 Reference proteome
Gene Ontology (GO)
Biological_process	lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: UniProtKB-UniPathway threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast stroma Inferred from direct assay PubMed 20061580. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid binding Inferred from electronic annotation. Source: InterPro aspartate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 84

Chloroplast Potential

Chain

85 – 544

460

Aspartokinase 2, chloroplastic

PRO_0000248158

Regions

Domain

402 – 477

ACT 1

Domain

478 – 539

ACT 2

Sites

Binding site

ATP By similarity

Binding site

ATP; via amide nitrogen By similarity

Binding site

119

ATP By similarity

Binding site

203

Substrate By similarity

Experimental info

Sequence conflict

E → G in AAB63104. Ref.1

Sequence conflict

E → G in CAC06395. Ref.2

Sequence conflict

107

L → F in AAB63104. Ref.1

Sequence conflict

107

L → F in CAC06395. Ref.2

Sequence conflict

125

T → I in AAB63104. Ref.1

Sequence conflict

125

T → I in CAC06395. Ref.2

Sequence conflict

144

E → G in AAB63104. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O23653 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 7DBCFDC1138645AC
Show »

FASTA

544

59,605

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of an Arabidopsis thaliana cDNA encoding a monofunctional aspartate kinase homologous to the lysine-sensitive enzyme of Escherichia coli." Tang G., Zhu-Shimoni J.X., Amir R., Zchori I.B.-T., Galili G. Plant Mol. Biol. 34:287-293(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	Frankard V.M.S., Vauterin M., Jacobs M. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia. Tissue: Leaf.
[3]	"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." Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U62020 mRNA. Translation: AAB63104.1. Y16255 Genomic DNA. Translation: CAC06395.1. AB007650 Genomic DNA. Translation: BAB08285.1. CP002688 Genomic DNA. Translation: AED91982.1. CP002688 Genomic DNA. Translation: AED91983.1.
IPI	IPI00527711.
RefSeq	NP_001078581.1. NM_001085112.1. NP_196910.1. NM_121409.3.
UniGene	At.21761.
3D structure databases
HSSP	HSSP built from PDB template 2CDQ based on UniProtKB Q9LYU8.
ProteinModelPortal	O23653.
SMR	O23653. Positions 80-542.
ModBase	Search...
Proteomic databases
PaxDb	O23653.
PRIDE	O23653.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G14060.1; AT5G14060.1; AT5G14060. AT5G14060.2; AT5G14060.2; AT5G14060.
GeneID	831255.
KEGG	ath:AT5G14060.
Organism-specific databases
TAIR	At5g14060.
Phylogenomic databases
eggNOG	COG0527.
HOGENOM	HOG000293094.
InParanoid	O23653.
KO	K00928.
OMA	MSYIEAM.
PhylomeDB	O23653.
ProtClustDB	PLN02551.
Enzyme and pathway databases
SABIO-RK	O23653.
UniPathway	UPA00034; UER00015. UPA00050; UER00461. UPA00051; UER00462.
Gene expression databases
ArrayExpress	O23653.
Genevestigator	O23653.
GermOnline	AT5G14060. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.1160.10. 2 hits.
InterPro	IPR002912. ACT_dom. IPR001048. Asp/Glu/Uridylate_kinase. IPR001341. Asp_kinase_dom. IPR018042. Aspartate_kinase_CS. [Graphical view]
Pfam	PF00696. AA_kinase. 1 hit. PF01842. ACT. 2 hits. [Graphical view]
SUPFAM	SSF53633. Aa_kinase. 1 hit.
TIGRFAMs	TIGR00657. asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AK2_ARATH

Accession

Primary (citable) accession number: O23653
Secondary accession number(s): Q9FMU4, Q9FY44

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents