ID   AK1_ARATH               Reviewed;         569 AA.
AC   Q9LYU8; O23152;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Aspartokinase 1, chloroplastic;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase 1;
DE   Flags: Precursor;
GN   Name=AK1; Synonyms=AK, AK-LYS1; OrderedLocusNames=At5g13280;
GN   ORFNames=T31B5.100;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9207839; DOI=10.1023/a:1005863128558;
RA   Frankard V., Vauterin M., Jacobs M.;
RT   "Molecular characterisation of an Arabidopsis thaliana cDNA coding for a
RT   monofunctional aspartate kinase.";
RL   Plant Mol. Biol. 34:233-242(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   ACTIVITY REGULATION.
RX   PubMed=6252474; DOI=10.1038/287357a0;
RA   Rognes S.E., Lea P.J., Miflin B.J.;
RT   "S-adenosylmethionine -- a novel regulator of aspartate kinase.";
RL   Nature 287:357-359(1980).
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=17140415; DOI=10.1111/j.1742-4658.2006.05573.x;
RA   Curien G., Laurencin M., Robert-Genthon M., Dumas R.;
RT   "Allosteric monofunctional aspartate kinases from Arabidopsis.";
RL   FEBS J. 274:164-176(2007).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 61-569 IN COMPLEX WITH SUBSTRATE
RP   ANALOG AND ALLOSTERIC REGULATORS, AND SUBUNIT.
RX   PubMed=16731588; DOI=10.1105/tpc.105.040451;
RA   Mas-Droux C., Curien G., Robert-Genthon M., Laurencin M., Ferrer J.L.,
RA   Dumas R.;
RT   "A novel organization of ACT domains in allosteric enzymes revealed by the
RT   crystal structure of Arabidopsis aspartate kinase.";
RL   Plant Cell 18:1681-1692(2006).
CC   -!- FUNCTION: Involved in the first step of essential amino acids lysine,
CC       threonine, methionine and isoleucine synthesis via the aspartate-family
CC       pathway.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC         Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC   -!- ACTIVITY REGULATION: Inhibited by S-adenosyl-L-methionine (SAM) and
CC       lysine in a synergistic manner. No inhibition by threonine, leucine or
CC       SAM alone, and no activation or inhibition by alanine, cysteine,
CC       isoleucine, serine, valine, methionine, glutamine, asparagine, glutamic
CC       acid or arginine. {ECO:0000269|PubMed:17140415,
CC       ECO:0000269|PubMed:6252474}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1700 uM for ATP {ECO:0000269|PubMed:17140415};
CC         KM=2037 uM for aspartate {ECO:0000269|PubMed:17140415};
CC         Note=K(cat) is 23.4/sec.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16731588}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- MISCELLANEOUS: Only one ACT domain (ACT1) is implicated in effector
CC       binding.
CC   -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR   EMBL; X98873; CAA67376.1; -; mRNA.
DR   EMBL; AL163491; CAB86635.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91874.1; -; Genomic_DNA.
DR   EMBL; BT000493; AAN18062.1; -; mRNA.
DR   EMBL; AY057674; AAL15305.1; -; mRNA.
DR   PIR; T48575; T48575.
DR   RefSeq; NP_196832.1; NM_121331.3.
DR   PDB; 2CDQ; X-ray; 2.85 A; A/B=61-569.
DR   PDBsum; 2CDQ; -.
DR   AlphaFoldDB; Q9LYU8; -.
DR   SMR; Q9LYU8; -.
DR   BioGRID; 16447; 5.
DR   IntAct; Q9LYU8; 5.
DR   STRING; 3702.Q9LYU8; -.
DR   iPTMnet; Q9LYU8; -.
DR   MetOSite; Q9LYU8; -.
DR   PaxDb; 3702-AT5G13280-1; -.
DR   ProteomicsDB; 244922; -.
DR   EnsemblPlants; AT5G13280.1; AT5G13280.1; AT5G13280.
DR   GeneID; 831169; -.
DR   Gramene; AT5G13280.1; AT5G13280.1; AT5G13280.
DR   KEGG; ath:AT5G13280; -.
DR   Araport; AT5G13280; -.
DR   TAIR; AT5G13280; AK-LYS1.
DR   eggNOG; KOG0456; Eukaryota.
DR   HOGENOM; CLU_009116_6_1_1; -.
DR   InParanoid; Q9LYU8; -.
DR   OMA; DNINIMM; -.
DR   OrthoDB; 2608453at2759; -.
DR   PhylomeDB; Q9LYU8; -.
DR   BioCyc; ARA:AT5G13280-MONOMER; -.
DR   BRENDA; 2.7.2.4; 399.
DR   SABIO-RK; Q9LYU8; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   EvolutionaryTrace; Q9LYU8; -.
DR   PRO; PR:Q9LYU8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LYU8; baseline and differential.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0004072; F:aspartate kinase activity; ISS:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:amino acid biosynthetic process; TAS:TAIR.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04244; AAK_AK-LysC-like; 1.
DR   CDD; cd04933; ACT_AK1-AT_1; 1.
DR   CDD; cd04918; ACT_AK1-AT_2; 1.
DR   Gene3D; 3.30.70.260; -; 2.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   Gene3D; 1.20.120.1320; Aspartokinase, catalytic domain; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041746; AK-LysC-like.
DR   InterPro; IPR047896; AK1_ACT_1.
DR   InterPro; IPR047895; AK1_ACT_2.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   NCBIfam; TIGR00657; asp_kinases; 1.
DR   PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR   PANTHER; PTHR21499:SF58; ASPARTOKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
DR   Genevisible; Q9LYU8; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; ATP-binding; Chloroplast; Kinase;
KW   Nucleotide-binding; Plastid; Reference proteome; Repeat;
KW   Threonine biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..90
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           91..569
FT                   /note="Aspartokinase 1, chloroplastic"
FT                   /id="PRO_0000248157"
FT   DOMAIN          405..483
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   DOMAIN          484..560
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="substrate"
FT   BINDING         413
FT                   /ligand="L-lysine"
FT                   /ligand_id="ChEBI:CHEBI:32551"
FT                   /ligand_note="allosteric effector"
FT   BINDING         415
FT                   /ligand="L-lysine"
FT                   /ligand_id="ChEBI:CHEBI:32551"
FT                   /ligand_note="allosteric effector"
FT   BINDING         430
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_note="allosteric effector"
FT   BINDING         431
FT                   /ligand="L-lysine"
FT                   /ligand_id="ChEBI:CHEBI:32551"
FT                   /ligand_note="allosteric effector"
FT   BINDING         432
FT                   /ligand="L-lysine"
FT                   /ligand_id="ChEBI:CHEBI:32551"
FT                   /ligand_note="allosteric effector"
FT   BINDING         437
FT                   /ligand="L-lysine"
FT                   /ligand_id="ChEBI:CHEBI:32551"
FT                   /ligand_note="allosteric effector"
FT   BINDING         452
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_note="allosteric effector"
FT   BINDING         453
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_note="allosteric effector"
FT   CONFLICT        369
FT                   /note="N -> S (in Ref. 1; CAA67376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="N -> D (in Ref. 1; CAA67376)"
FT                   /evidence="ECO:0000305"
FT   STRAND          88..92
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           100..112
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           128..139
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   TURN            140..142
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           151..167
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           172..191
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           196..220
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           230..232
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           250..264
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          268..278
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   TURN            279..281
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           291..303
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          308..320
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   TURN            322..324
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          333..335
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           336..346
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           352..361
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          365..369
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          378..382
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          391..406
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           408..410
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           416..426
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          431..437
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          440..445
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           448..450
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          451..453
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           457..467
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   TURN            468..470
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          471..486
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           488..490
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           491..505
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          510..514
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   STRAND          519..526
FT                   /evidence="ECO:0007829|PDB:2CDQ"
FT   HELIX           527..542
FT                   /evidence="ECO:0007829|PDB:2CDQ"
SQ   SEQUENCE   569 AA;  62298 MW;  F66A35F4E84DC429 CRC64;
     MAATRVRCCH SNAAFTRLPL TRHRNSPTLP ISLNRVDFPT LKKLSLPIGD GSSIRKVSGS
     GSRNIVRAVL EEKKTEAITE VDEKGITCVM KFGGSSVASA ERMKEVADLI LTFPEESPVI
     VLSAMGKTTN NLLLAGEKAV SCGVSNASEI EELSIIKELH IRTVKELNID PSVILTYLEE
     LEQLLKGIAM MKELTLRTRD YLVSFGECLS TRIFAAYLNT IGVKARQYDA FEIGFITTDD
     FTNGDILEAT YPAVAKRLYD DWMHDPAVPI VTGFLGKGWK TGAVTTLGRG GSDLTATTIG
     KALGLKEIQV WKDVDGVLTC DPTIYKRATP VPYLTFDEAA ELAYFGAQVL HPQSMRPARE
     GEIPVRVKNS YNPKAPGTII TKTRDMTKSI LTSIVLKRNV TMLDIASTRM LGQVGFLAKV
     FSIFEELGIS VDVVATSEVS ISLTLDPSKL WSRELIQQEL DHVVEELEKI AVVNLLKGRA
     IISLIGNVQH SSLILERAFH VLYTKGVNVQ MISQGASKVN ISFIVNEAEA EGCVQALHKS
     FFESGDLSEL LIQPRLGNGS PVRTLQVEN
//