Q9LYU8 (AK1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	569 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	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	Plastid › chloroplast 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

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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular amino acid biosynthetic process Traceable author statement Ref.1. Source: TAIR 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 sequence or structural similarity Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 90

90

Chloroplast Potential

Chain

91 – 569

479

Aspartokinase 1, chloroplastic

PRO_0000248157

Regions

Domain

406 – 481

76

ACT 1

Domain

482 – 549

68

ACT 2

Sites

Binding site

91

1

ATP By similarity

Binding site

94

1

ATP; via amide nitrogen By similarity

Binding site

123

1

ATP By similarity

Binding site

207

1

Substrate

Binding site

413

1

Allosteric effector lysine; via carbonyl oxygen

Binding site

415

1

Allosteric effector lysine; via amide nitrogen

Binding site

430

1

Allosteric effector S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen

Binding site

431

1

Allosteric effector lysine; via amide nitrogen

Binding site

432

1

Allosteric effector lysine; via carbonyl oxygen

Binding site

437

1

Allosteric effector lysine; via carbonyl oxygen

Binding site

452

1

Allosteric effector S-adenosyl-L-methionine

Binding site

453

1

Allosteric effector S-adenosyl-L-methionine; via amide nitrogen

Experimental info

Sequence conflict

369

1

N → S in CAA67376. Ref.1

Sequence conflict

569

1

N → D in CAA67376. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

569

Helix Strand Turn

Details...

Beta strand

88 – 92

5

Helix

95 – 97

3

Helix

100 – 112

13

Beta strand

118 – 122

5

Helix

128 – 139

12

Turn

140 – 142

3

Turn

144 – 146

3

Helix

147 – 149

3

Helix

151 – 167

17

Helix

172 – 191

20

Helix

196 – 220

25

Beta strand

225 – 228

4

Helix

230 – 232

3

Helix

250 – 264

15

Beta strand

268 – 278

11

Turn

279 – 281

3

Beta strand

284 – 286

3

Helix

291 – 303

13

Beta strand

308 – 320

13

Turn

322 – 324

3

Beta strand

333 – 335

3

Helix

336 – 346

11

Helix

352 – 361

10

Beta strand

365 – 369

5

Beta strand

378 – 382

5

Beta strand

391 – 406

16

Helix

408 – 410

3

Helix

416 – 426

11

Beta strand

431 – 437

7

Beta strand

440 – 445

6

Helix

448 – 450

3

Beta strand

451 – 453

3

Helix

457 – 467

11

Turn

468 – 470

3

Beta strand

471 – 486

16

Helix

488 – 490

3

Helix

491 – 505

15

Beta strand

510 – 514

5

Beta strand

519 – 526

8

Helix

527 – 542

16

Sequences

	Sequence		Length	Mass (Da)
	Q9LYU8 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F66A35F4E84DC429	FASTA	569	62,298
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.

IPI

IPI00544203.

PIR

T48575.

RefSeq

NP_196832.1. NM_121331.2.

UniGene

At.124.
At.32091.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CDQ	X-ray	2.85	A/B	61-569	[»]

ProteinModelPortal

Q9LYU8.

SMR

Q9LYU8. Positions 84-553.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9LYU8. 4 interactions.

Proteomic databases

PaxDb

Q9LYU8.

PRIDE

Q9LYU8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G13280.1; AT5G13280.1; AT5G13280.

GeneID

831169.

KEGG

ath:AT5G13280.

Organism-specific databases

TAIR

At5g13280.

Phylogenomic databases

eggNOG

COG0527.

HOGENOM

HOG000293094.

InParanoid

Q9LYU8.

KO

K00928.

OMA

IRLICYG.

PhylomeDB

Q9LYU8.

ProtClustDB

PLN02551.

Enzyme and pathway databases

BRENDA

2.7.2.4. 399.

SABIO-RK

Q9LYU8.

UniPathway

UPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.

Gene expression databases

Genevestigator

Q9LYU8.

GermOnline

AT5G13280. 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. 1 hit.
[Graphical view]

SUPFAM

SSF53633. Aa_kinase. 1 hit.

TIGRFAMs

TIGR00657. asp_kinases. 1 hit.

PROSITE

PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9LYU8.

Entry information

Entry name

AK1_ARATH

Accession

Primary (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 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program