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Q9LYU8 (AK1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 1, chloroplastic

EC=2.7.2.4
Alternative name(s):
Aspartate kinase 1
Gene names
Name:AK1
Synonyms:AK, AK-LYS1
Ordered Locus Names:At5g13280
ORF Names:T31B5.100
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length569 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

Inhibited by S-adenosyl-L-methionine (SAM) and lysine in a synergistic manner. No inhibition by threonine, leucine or SAM alone, and no activation or inhibition by alanine, cysteine, isoleucine, serine, valine, methionine, glutamine, asparagine, glutamic acid or arginine. Ref.5 Ref.6

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.

Subunit structure

Homodimer. Ref.7

Subcellular location

Plastidchloroplast Potential.

Miscellaneous

Only one ACT domain (ACT1) is implicated in effector binding.

Sequence similarities

Belongs to the aspartokinase family.

Contains 2 ACT domains.

Biophysicochemical properties

Kinetic parameters:

K(cat) is 23.4/sec.

KM=1700 µM for ATP Ref.6

KM=2037 µM for aspartate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 9090Chloroplast Potential
Chain91 – 569479Aspartokinase 1, chloroplastic
PRO_0000248157

Regions

Domain405 – 48379ACT 1
Domain484 – 56077ACT 2

Sites

Binding site911ATP By similarity
Binding site941ATP; via amide nitrogen By similarity
Binding site1231ATP By similarity
Binding site2071Substrate
Binding site4131Allosteric effector lysine; via carbonyl oxygen
Binding site4151Allosteric effector lysine; via amide nitrogen
Binding site4301Allosteric effector S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen
Binding site4311Allosteric effector lysine; via amide nitrogen
Binding site4321Allosteric effector lysine; via carbonyl oxygen
Binding site4371Allosteric effector lysine; via carbonyl oxygen
Binding site4521Allosteric effector S-adenosyl-L-methionine
Binding site4531Allosteric effector S-adenosyl-L-methionine; via amide nitrogen

Experimental info

Sequence conflict3691N → S in CAA67376. Ref.1
Sequence conflict5691N → D in CAA67376. Ref.1

Secondary structure

........................................................................ 569
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9LYU8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F66A35F4E84DC429

FASTA56962,298
        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 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterisation of an Arabidopsis thaliana cDNA coding for a monofunctional aspartate kinase."
Frankard V., Vauterin M., Jacobs M.
Plant Mol. Biol. 34:233-242(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"S-adenosylmethionine -- a novel regulator of aspartate kinase."
Rognes S.E., Lea P.J., Miflin B.J.
Nature 287:357-359(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[6]"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.
[7]"A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase."
Mas-Droux C., Curien G., Robert-Genthon M., Laurencin M., Ferrer J.L., Dumas R.
Plant Cell 18:1681-1692(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 61-569 IN COMPLEX WITH SUBSTRATE ANALOG AND ALLOSTERIC REGULATORS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98873 mRNA. Translation: CAA67376.1.
AL163491 Genomic DNA. Translation: CAB86635.1.
CP002688 Genomic DNA. Translation: AED91874.1.
BT000493 mRNA. Translation: AAN18062.1.
AY057674 mRNA. Translation: AAL15305.1.
PIRT48575.
RefSeqNP_196832.1. NM_121331.2.
UniGeneAt.124.
At.32091.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CDQX-ray2.85A/B61-569[»]
ProteinModelPortalQ9LYU8.
SMRQ9LYU8. Positions 84-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16447. 4 interactions.
IntActQ9LYU8. 4 interactions.

Proteomic databases

PaxDbQ9LYU8.
PRIDEQ9LYU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G13280.1; AT5G13280.1; AT5G13280.
GeneID831169.
KEGGath:AT5G13280.

Organism-specific databases

TAIRAT5G13280.

Phylogenomic databases

eggNOGCOG0527.
HOGENOMHOG000293094.
InParanoidQ9LYU8.
KOK00928.
OMAVMRTDSH.
PhylomeDBQ9LYU8.

Enzyme and pathway databases

BioCycARA:AT5G13280-MONOMER.
BRENDA2.7.2.4. 399.
SABIO-RKQ9LYU8.
UniPathwayUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.

Gene expression databases

GenevestigatorQ9LYU8.

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. 1 hit.
[Graphical view]
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00657. asp_kinases. 1 hit.
PROSITEPS51671. ACT. 1 hit.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9LYU8.

Entry information

Entry nameAK1_ARATH
AccessionPrimary (citable) accession number: Q9LYU8
Secondary accession number(s): O23152
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 96 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names