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   16-JUN-2009, entry version 54.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=97351562; 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
RT   enzyme 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   MEDLINE=98162728; 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.
RT   Sequence features of the regions of 1,191,918 bp covered by seventeen
RT   physically assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [4]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME 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
CC       lysine, threonine, methionine and isoleucine synthesis via the
CC       aspartate-family pathway.
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate.
CC   -!- ENZYME REGULATION: Allosterically inhibited by lysine, but not by
CC       S-adenosyl-L-methionine (SAM). K(0.5) for lysine in the presence
CC       of physiological concentrations of substrates is 12.5 uM. No
CC       inhibition by threonine or leucine and no activation or inhibition
CC       by alanine, cysteine, isoleucine, serine, valine, methionine,
CC       glutamine, asparagine, glutamic acid or arginine.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=980 uM for ATP;
CC         KM=1940 uM for aspartate;
CC         Note=K(cat) is 14.5/sec;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in stems, leaves, floral organs and
CC       young seedlings.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC   -!- SIMILARITY: Contains 2 ACT domains.
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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   IPI; IPI00527711; -.
DR   RefSeq; NP_001078581.1; -.
DR   RefSeq; NP_196910.1; -.
DR   UniGene; At.21761; -.
DR   SMR; O23653; 80-542.
DR   PRIDE; O23653; -.
DR   GeneID; 831255; -.
DR   GenomeReviews; BA000015_GR; AT5G14060.
DR   KEGG; ath:AT5G14060; -.
DR   NMPDR; fig|3702.1.peg.23535; -.
DR   TAIR; At5g14060; -.
DR   OMA; O23653; KLSCLFM.
DR   BRENDA; 2.7.2.4; 302.
DR   GermOnline; AT5G14060; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001341; Asp_kin_reg.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 2.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; ATP-binding; Chloroplast; Complete proteome;
KW   Kinase; Nucleotide-binding; Plastid; Repeat; Threonine biosynthesis;
KW   Transferase; Transit peptide.
FT   TRANSIT       1     84       Chloroplast (Potential).
FT   CHAIN        85    544       Aspartokinase 2, chloroplastic.
FT                                /FTId=PRO_0000248158.
FT   DOMAIN      402    477       ACT 1.
FT   DOMAIN      478    539       ACT 2.
FT   BINDING      87     87       ATP (By similarity).
FT   BINDING      90     90       ATP; via amide nitrogen (By similarity).
FT   BINDING     119    119       ATP (By similarity).
FT   BINDING     203    203       Substrate (By similarity).
FT   CONFLICT     94     94       E -> G (in Ref. 1; AAB63104 and 2;
FT                                CAC06395).
FT   CONFLICT    107    107       L -> F (in Ref. 1; AAB63104 and 2;
FT                                CAC06395).
FT   CONFLICT    125    125       T -> I (in Ref. 1; AAB63104 and 2;
FT                                CAC06395).
FT   CONFLICT    144    144       E -> G (in Ref. 1; AAB63104).
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
//