Reviewed, UniProtKB/Swiss-Prot Q9LYU8 (AK1_ARATH)

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) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › 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.4 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.
Subunit structure	Homodimer. Ref.6
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 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
Gene Ontology (GO)
Biological process	threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 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

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569

Helix Strand Turn

Details...

Beta strand

88 – 92

5

Helix

100 – 112

13

Beta strand

118 – 122

5

Helix

128 – 134

7

Helix

139 – 141

3

Helix

147 – 149

3

Helix

151 – 167

17

Helix

172 – 185

14

Turn

189 – 192

4

Helix

196 – 205

10

Helix

208 – 220

13

Beta strand

225 – 228

4

Helix

230 – 232

3

Helix

250 – 264

15

Beta strand

268 – 271

4

Helix

293 – 298

6

Beta strand

308 – 313

6

Beta strand

318 – 320

3

Turn

322 – 324

3

Beta strand

333 – 335

3

Helix

336 – 342

7

Helix

352 – 359

8

Beta strand

365 – 369

5

Beta strand

379 – 382

4

Beta strand

393 – 397

5

Beta strand

402 – 406

5

Helix

408 – 410

3

Helix

417 – 426

10

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 – 476

6

Beta strand

480 – 485

6

Helix

488 – 490

3

Helix

491 – 504

14

Beta strand

510 – 514

5

Beta strand

521 – 525

5

Helix

527 – 530

4

Helix

534 – 542

9

Sequences

	Sequence		Length	Mass (Da)
	Q9LYU8-1 [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: 9207839] [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: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"S-adenosylmethionine -- a novel regulator of aspartate kinase." Rognes S.E., Lea P.J., Miflin B.J. Nature 287:357-359(1980) [PubMed: 6252474] [Abstract] Cited for: ENZYME REGULATION.
[5]	"Allosteric monofunctional aspartate kinases from Arabidopsis." Curien G., Laurencin M., Robert-Genthon M., Dumas R. FEBS J. 274:164-176(2007) [PubMed: 17140415] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[6]	"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: 16731588] [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

EMBLGenBankDDBJ

X98873 mRNA. Translation: CAA67376.1.
AL163491 Genomic DNA. Translation: CAB86635.1.
BT000493 mRNA. Translation: AAN18062.1.
AY057674 mRNA. Translation: AAL15305.1.

IPI

IPI00544203.

PIR

T48575.

RefSeq

NP_196832.1.

UniGene

At.124

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

STRING

Q9LYU8.

Proteomic databases

PRIDE

Q9LYU8.

Genome annotation databases

GeneID

831169.

GenomeReviews

Gene locus AT5G13280 in contig BA000015_GR.

KEGG

ath:AT5G13280.

NMPDR

fig|3702.1.peg.23445.

Organism-specific databases

TAIR

At5g13280.

Phylogenomic databases

OMA

TENVALI.

Enzyme and pathway databases

BRENDA

2.7.2.4. 302.

Gene expression databases

Genevestigator

Q9LYU8.

GermOnline

AT5G13280. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR002912. ACT_bd.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001341. Asp_kin_reg.
IPR018042. Aspartate_kinase_CS.
[Graphical view]

Gene3D

G3DSA:3.40.1160.10. Aa_kinase. 1 hit.

Pfam

PF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
[Graphical view]

TIGRFAMs

TIGR00657. asp_kinases. 1 hit.

PROSITE

PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	November 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)