ID   AK3_ARATH               Reviewed;         559 AA.
AC   Q9S702;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Aspartokinase 3, chloroplastic;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase 3;
DE   Flags: Precursor;
GN   Name=AK3; Synonyms=AK-LYS3; OrderedLocusNames=At3g02020;
GN   ORFNames=F28J7.35, F1C9.20;
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], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11569502; DOI=10.1266/ggs.76.189;
RA   Yoshioka Y., Kurei S., Machida Y.;
RT   "Identification of a monofunctional aspartate kinase gene of
RT   Arabidopsis thaliana with spatially and temporally regulated
RT   expression.";
RL   Genes Genet. Syst. 76:189-198(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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 7.4 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=560 uM for ATP;
CC         KM=1095 uM for aspartate;
CC         Note=K(cat) is 8.4/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: Highly expressed in xylem of leaves and
CC       hypocotyls, stele of roots and in trichomes after bolting. Weak
CC       expression in veins and mesophyll cells of caulone leaves,
CC       inflorescence stems, sepals, petals and stigmata.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC   -!- SIMILARITY: Contains 2 ACT domains.
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DR   EMBL; AC010797; AAF03452.1; -; Genomic_DNA.
DR   EMBL; AC011664; AAF14833.1; -; Genomic_DNA.
DR   EMBL; AY088366; AAM65905.1; -; mRNA.
DR   EMBL; AK226200; BAE98365.1; -; mRNA.
DR   IPI; IPI00527939; -.
DR   RefSeq; NP_186851.1; -.
DR   UniGene; At.41192; -.
DR   SMR; Q9S702; 81-541.
DR   PRIDE; Q9S702; -.
DR   GeneID; 821287; -.
DR   GenomeReviews; BA000014_GR; AT3G02020.
DR   KEGG; ath:AT3G02020; -.
DR   NMPDR; fig|3702.1.peg.12136; -.
DR   TAIR; At3g02020; -.
DR   OMA; Q9S702; DITSTRM.
DR   BRENDA; 2.7.2.4; 302.
DR   GermOnline; AT3G02020; 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; IGI:TAIR.
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     85       Chloroplast (Potential).
FT   CHAIN        86    559       Aspartokinase 3, chloroplastic.
FT                                /FTId=PRO_0000248159.
FT   DOMAIN      403    478       ACT 1.
FT   DOMAIN      496    538       ACT 2.
FT   BINDING      88     88       ATP (By similarity).
FT   BINDING      91     91       ATP; via amide nitrogen (By similarity).
FT   BINDING     120    120       ATP (By similarity).
FT   BINDING     204    204       Substrate (By similarity).
SQ   SEQUENCE   559 AA;  61216 MW;  FBC8A4A0E814F349 CRC64;
     MAASMQFYGV KTPELALNSK RIEFSSKGLN FSALVSSARV FSRNVDRSCK NIALRVTCEA
     GRVELLERKA SETFKLNKTE KKLTCVMKFG GSSVASAERM IQVAKLILSF PDEKPVVVLS
     AMAKTTNKLL MAGEKAVCCG VTNVDTIEEL SYIKELHIRT AHELGVETAV IAEHLEGLEQ
     LLKGVAMMKE LTLRSRDYLV SFGECMSTRL FAAYLNKIGH KARQYDAFEI GIITTDDFTN
     ADILEATYPA VSKKLLGDWS KENALPVVTG FLGKGWRSCA VTTLGRGGSD LTATTIGKAL
     GLREIQVWKD VDGVLTCDPN IYCGAQPVPH LTFDEAAELA YFGAQVLHPL SMRPAREGNI
     PVRVKNSYNP TAPGTVITRS RDMSKAVLTS IVLKRNVTML DITSTRMLGQ YGFLAKVFST
     FEKLGISVDV VATSEVSISL TLDPSKFCSR ELIQHELDQV VEELEKIAVV NLLRHRSIIS
     LIGNVQRSSF ILEKGFRVLR TNGINVQMIS QGASKVNISL IVNDDEAEHC VKALHSAFFE
     TDTCEAVSEC PTGYIAASS
//