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Q9LYU8

- AK1_ARATH

UniProt

Q9LYU8 - AK1_ARATH

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Protein
Aspartokinase 1, chloroplastic
Gene
AK1, AK, AK-LYS1, At5g13280, T31B5.100
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.

Catalytic activityi

ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

Enzyme regulationi

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.2 Publications

Kineticsi

K(cat) is 23.4/sec.

  1. KM=1700 µM for ATP1 Publication
  2. KM=2037 µM for aspartate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911ATP By similarity
Binding sitei94 – 941ATP; via amide nitrogen By similarity
Binding sitei123 – 1231ATP By similarity
Binding sitei207 – 2071Substrate
Binding sitei413 – 4131Allosteric effector lysine; via carbonyl oxygen
Binding sitei415 – 4151Allosteric effector lysine; via amide nitrogen
Binding sitei430 – 4301Allosteric effector S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen
Binding sitei431 – 4311Allosteric effector lysine; via amide nitrogen
Binding sitei432 – 4321Allosteric effector lysine; via carbonyl oxygen
Binding sitei437 – 4371Allosteric effector lysine; via carbonyl oxygen
Binding sitei452 – 4521Allosteric effector S-adenosyl-L-methionine
Binding sitei453 – 4531Allosteric effector S-adenosyl-L-methionine; via amide nitrogen

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. amino acid binding Source: InterPro
  3. aspartate kinase activity Source: TAIR
Complete GO annotation...

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: TAIR
  2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
  3. threonine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Threonine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G13280-MONOMER.
BRENDAi2.7.2.4. 399.
SABIO-RKQ9LYU8.
UniPathwayiUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartokinase 1, chloroplastic (EC:2.7.2.4)
Alternative name(s):
Aspartate kinase 1
Gene namesi
Name:AK1
Synonyms:AK, AK-LYS1
Ordered Locus Names:At5g13280
ORF Names:T31B5.100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G13280.

Subcellular locationi

Plastidchloroplast Reviewed prediction

GO - Cellular componenti

  1. chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 9090Chloroplast Reviewed prediction
Add
BLAST
Chaini91 – 569479Aspartokinase 1, chloroplastic
PRO_0000248157Add
BLAST

Proteomic databases

PaxDbiQ9LYU8.
PRIDEiQ9LYU8.

Expressioni

Gene expression databases

GenevestigatoriQ9LYU8.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi16447. 4 interactions.
IntActiQ9LYU8. 4 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi88 – 925
Helixi95 – 973
Helixi100 – 11213
Beta strandi118 – 1225
Helixi128 – 13912
Turni140 – 1423
Turni144 – 1463
Helixi147 – 1493
Helixi151 – 16717
Helixi172 – 19120
Helixi196 – 22025
Beta strandi225 – 2284
Helixi230 – 2323
Helixi250 – 26415
Beta strandi268 – 27811
Turni279 – 2813
Beta strandi284 – 2863
Helixi291 – 30313
Beta strandi308 – 32013
Turni322 – 3243
Beta strandi333 – 3353
Helixi336 – 34611
Helixi352 – 36110
Beta strandi365 – 3695
Beta strandi378 – 3825
Beta strandi391 – 40616
Helixi408 – 4103
Helixi416 – 42611
Beta strandi431 – 4377
Beta strandi440 – 4456
Helixi448 – 4503
Beta strandi451 – 4533
Helixi457 – 46711
Turni468 – 4703
Beta strandi471 – 48616
Helixi488 – 4903
Helixi491 – 50515
Beta strandi510 – 5145
Beta strandi519 – 5268
Helixi527 – 54216

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CDQX-ray2.85A/B61-569[»]
ProteinModelPortaliQ9LYU8.
SMRiQ9LYU8. Positions 84-553.

Miscellaneous databases

EvolutionaryTraceiQ9LYU8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini405 – 48379ACT 1
Add
BLAST
Domaini484 – 56077ACT 2
Add
BLAST

Sequence similaritiesi

Belongs to the aspartokinase family.
Contains 2 ACT domains.

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0527.
HOGENOMiHOG000293094.
InParanoidiQ9LYU8.
KOiK00928.
OMAiVMRTDSH.
PhylomeDBiQ9LYU8.

Family and domain databases

Gene3Di3.40.1160.10. 2 hits.
InterProiIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01842. ACT. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LYU8-1 [UniParc]FASTAAdd to Basket

« Hide

MAATRVRCCH SNAAFTRLPL TRHRNSPTLP ISLNRVDFPT LKKLSLPIGD    50
GSSIRKVSGS GSRNIVRAVL EEKKTEAITE VDEKGITCVM KFGGSSVASA 100
ERMKEVADLI LTFPEESPVI VLSAMGKTTN NLLLAGEKAV SCGVSNASEI 150
EELSIIKELH IRTVKELNID PSVILTYLEE LEQLLKGIAM MKELTLRTRD 200
YLVSFGECLS TRIFAAYLNT IGVKARQYDA FEIGFITTDD FTNGDILEAT 250
YPAVAKRLYD DWMHDPAVPI VTGFLGKGWK TGAVTTLGRG GSDLTATTIG 300
KALGLKEIQV WKDVDGVLTC DPTIYKRATP VPYLTFDEAA ELAYFGAQVL 350
HPQSMRPARE GEIPVRVKNS YNPKAPGTII TKTRDMTKSI LTSIVLKRNV 400
TMLDIASTRM LGQVGFLAKV FSIFEELGIS VDVVATSEVS ISLTLDPSKL 450
WSRELIQQEL DHVVEELEKI AVVNLLKGRA IISLIGNVQH SSLILERAFH 500
VLYTKGVNVQ MISQGASKVN ISFIVNEAEA EGCVQALHKS FFESGDLSEL 550
LIQPRLGNGS PVRTLQVEN 569
Length:569
Mass (Da):62,298
Last modified:October 1, 2000 - v1
Checksum:iF66A35F4E84DC429
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti369 – 3691N → S in CAA67376. 1 Publication
Sequence conflicti569 – 5691N → D in CAA67376. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT48575.
RefSeqiNP_196832.1. NM_121331.2.
UniGeneiAt.124.
At.32091.

Genome annotation databases

EnsemblPlantsiAT5G13280.1; AT5G13280.1; AT5G13280.
GeneIDi831169.
KEGGiath:AT5G13280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T48575.
RefSeqi NP_196832.1. NM_121331.2.
UniGenei At.124.
At.32091.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CDQ X-ray 2.85 A/B 61-569 [» ]
ProteinModelPortali Q9LYU8.
SMRi Q9LYU8. Positions 84-553.
ModBasei Search...

Protein-protein interaction databases

BioGridi 16447. 4 interactions.
IntActi Q9LYU8. 4 interactions.

Proteomic databases

PaxDbi Q9LYU8.
PRIDEi Q9LYU8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G13280.1 ; AT5G13280.1 ; AT5G13280 .
GeneIDi 831169.
KEGGi ath:AT5G13280.

Organism-specific databases

TAIRi AT5G13280.

Phylogenomic databases

eggNOGi COG0527.
HOGENOMi HOG000293094.
InParanoidi Q9LYU8.
KOi K00928.
OMAi VMRTDSH.
PhylomeDBi Q9LYU8.

Enzyme and pathway databases

UniPathwayi UPA00034 ; UER00015 .
UPA00050 ; UER00461 .
UPA00051 ; UER00462 .
BioCyci ARA:AT5G13280-MONOMER.
BRENDAi 2.7.2.4. 399.
SABIO-RK Q9LYU8.

Miscellaneous databases

EvolutionaryTracei Q9LYU8.

Gene expression databases

Genevestigatori Q9LYU8.

Family and domain databases

Gene3Di 3.40.1160.10. 2 hits.
InterProi IPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
[Graphical view ]
Pfami PF00696. AA_kinase. 1 hit.
PF01842. ACT. 1 hit.
[Graphical view ]
SUPFAMi SSF53633. SSF53633. 1 hit.
TIGRFAMsi TIGR00657. asp_kinases. 1 hit.
PROSITEi PS51671. ACT. 1 hit.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiAK1_ARATH
AccessioniPrimary (citable) accession number: Q9LYU8
Secondary accession number(s): O23152
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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