ID   AK2_ARATH               Reviewed;         544 AA.
AC   O23653; Q9FMU4; Q9FY44;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=Aspartokinase 2, chloroplastic;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase 2;
DE   Flags: Precursor;
GN   Name=AK2; Synonyms=AK-LYS2, CARAB-AK-LYS; OrderedLocusNames=At5g14060;
GN   ORFNames=MUA22.6;
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], AND TISSUE SPECIFICITY.
RX   PubMed=9207844; DOI=10.1023/a:1005849228945;
RA   Tang G., Zhu-Shimoni J.X., Amir R., Zchori I.B.-T., Galili G.;
RT   "Cloning and expression of an Arabidopsis thaliana cDNA encoding a
RT   monofunctional aspartate kinase homologous to the lysine-sensitive enzyme
RT   of Escherichia coli.";
RL   Plant Mol. Biol. 34:287-293(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RA   Frankard V.M.S., Vauterin M., Jacobs M.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [4]
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   [5]
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).
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: Allosterically inhibited by lysine, but not by S-
CC       adenosyl-L-methionine (SAM). K(0.5) for lysine in the presence of
CC       physiological concentrations of substrates is 12.5 uM. No inhibition by
CC       threonine or leucine and no activation or inhibition by alanine,
CC       cysteine, isoleucine, serine, valine, methionine, glutamine,
CC       asparagine, glutamic acid or arginine. {ECO:0000269|PubMed:17140415}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=980 uM for ATP {ECO:0000269|PubMed:17140415};
CC         KM=1940 uM for aspartate {ECO:0000269|PubMed:17140415};
CC         Note=K(cat) is 14.5/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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in stems, leaves, floral organs and young
CC       seedlings. {ECO:0000269|PubMed:9207844}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR   EMBL; U62020; AAB63104.1; -; mRNA.
DR   EMBL; Y16255; CAC06395.1; -; Genomic_DNA.
DR   EMBL; AB007650; BAB08285.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91982.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91983.1; -; Genomic_DNA.
DR   RefSeq; NP_001078581.1; NM_001085112.2.
DR   RefSeq; NP_196910.1; NM_121409.4.
DR   AlphaFoldDB; O23653; -.
DR   SMR; O23653; -.
DR   STRING; 3702.O23653; -.
DR   iPTMnet; O23653; -.
DR   MetOSite; O23653; -.
DR   PaxDb; 3702-AT5G14060-2; -.
DR   ProteomicsDB; 244807; -.
DR   EnsemblPlants; AT5G14060.1; AT5G14060.1; AT5G14060.
DR   EnsemblPlants; AT5G14060.2; AT5G14060.2; AT5G14060.
DR   GeneID; 831255; -.
DR   Gramene; AT5G14060.1; AT5G14060.1; AT5G14060.
DR   Gramene; AT5G14060.2; AT5G14060.2; AT5G14060.
DR   KEGG; ath:AT5G14060; -.
DR   Araport; AT5G14060; -.
DR   TAIR; AT5G14060; CARAB-AK-LYS.
DR   eggNOG; KOG0456; Eukaryota.
DR   HOGENOM; CLU_009116_6_1_1; -.
DR   InParanoid; O23653; -.
DR   OMA; THWEQEN; -.
DR   OrthoDB; 2608453at2759; -.
DR   PhylomeDB; O23653; -.
DR   BioCyc; ARA:AT5G14060-MONOMER; -.
DR   BRENDA; 2.7.2.4; 399.
DR   SABIO-RK; O23653; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   PRO; PR:O23653; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O23653; baseline and differential.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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; 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:SF54; ASPARTOKINASE 2, 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; 2.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
DR   Genevisible; O23653; AT.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; ATP-binding; Chloroplast; Kinase;
KW   Nucleotide-binding; Plastid; Reference proteome; Repeat;
KW   Threonine biosynthesis; Transferase; Transit peptide.
FT   TRANSIT         1..84
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           85..544
FT                   /note="Aspartokinase 2, chloroplastic"
FT                   /id="PRO_0000248158"
FT   DOMAIN          401..479
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   DOMAIN          481..544
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        94
FT                   /note="E -> G (in Ref. 1; AAB63104 and 2; CAC06395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="L -> F (in Ref. 1; AAB63104 and 2; CAC06395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="T -> I (in Ref. 1; AAB63104 and 2; CAC06395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="E -> G (in Ref. 1; AAB63104)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   544 AA;  59605 MW;  7DBCFDC1138645AC CRC64;
     MASLQLYGVK TPGLALSSKR LEFASKGACF SVTLPSSSAV FRDVEHSCRN IGLRVSCEAL
     RVDLLQRKEP ETCDSSGTGK ELTCVMKFGG SSVESAERMK EVANLILSFP DERPVIVLSA
     MGKTTNKLLK AGEKAVTCGV TNVESIEELS FIKELHLRTA HELGVETTVI EKHLEGLHQL
     LKGISMMKEL TLRTRDYLVS FGECMSTRLF SAYLNKIGHK ARQYDAFEIG FITTDDFTNA
     DILEATYPAV SKTLVGDWSK ENAVPVVTGY LGKGWRSCAI TTLGRGGSDL TATTIGKALG
     LREIQVWKDV DGVLTCDPNI YPGAQSVPYL TFDEAAELAY FGAQVLHPLS MRPARDGDIP
     VRVKNSYNPT APGTVITRSR DMSKAVLTSI VLKRNVTMLD IASTRMLGQY GFLAKVFTTF
     EDLGISVDVV ATSEVSISLT LDPAKLWGRE LIQRVNELDN LVEELEKIAV VKLLQRRSII
     SLIGNVQKSS LILEKVFQVF RSNGVNVQMI SQGASKVNIS LIVNDEEAEQ CVRALHSAFF
     ETDP
//