Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O23653 (AK2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Plastidchloroplast 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.

KM=980 µM for ATP Ref.5

KM=1940 µM for aspartate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8484Chloroplast Potential
Chain85 – 544460Aspartokinase 2, chloroplastic
PRO_0000248158

Regions

Domain401 – 47979ACT 1
Domain481 – 54464ACT 2

Sites

Binding site871ATP By similarity
Binding site901ATP; via amide nitrogen By similarity
Binding site1191ATP By similarity
Binding site2031Substrate By similarity

Experimental info

Sequence conflict941E → G in AAB63104. Ref.1
Sequence conflict941E → G in CAC06395. Ref.2
Sequence conflict1071L → F in AAB63104. Ref.1
Sequence conflict1071L → F in CAC06395. Ref.2
Sequence conflict1251T → I in AAB63104. Ref.1
Sequence conflict1251T → I in CAC06395. Ref.2
Sequence conflict1441E → G in AAB63104. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O23653 [UniParc].

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

FASTA54459,605
        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' 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.

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.
RefSeqNP_001078581.1. NM_001085112.1.
NP_196910.1. NM_121409.3.
UniGeneAt.21761.

3D structure databases

ProteinModelPortalO23653.
SMRO23653. Positions 80-542.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbO23653.
PRIDEO23653.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G14060.1; AT5G14060.1; AT5G14060.
AT5G14060.2; AT5G14060.2; AT5G14060.
GeneID831255.
KEGGath:AT5G14060.

Organism-specific databases

TAIRAT5G14060.

Phylogenomic databases

eggNOGCOG0527.
HOGENOMHOG000293094.
InParanoidO23653.
KOK00928.
OMAHHINIAM.
PhylomeDBO23653.
ProtClustDBPLN02551.

Enzyme and pathway databases

BioCycARA:AT5G14060-MONOMER.
ARA:GQT-2418-MONOMER.
SABIO-RKO23653.
UniPathwayUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.

Gene expression databases

ArrayExpressO23653.
GenevestigatorO23653.

Family and domain databases

Gene3D3.40.1160.10. 2 hits.
InterProIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
[Graphical view]
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00657. asp_kinases. 1 hit.
PROSITEPS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAK2_ARATH
AccessionPrimary (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: February 19, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names