AK3_ARATH
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 03-AUG-2022, entry version 140.
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=F1C9.20, F28J7.35;
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], 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 Arabidopsis
RT thaliana with spatially and temporally regulated expression.";
RL Genes Genet. Syst. 76:189-198(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., 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., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., 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 thaliana.";
RL Nature 408:820-822(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].
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 [5]
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., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: Involved in the first step of essential amino acids lysine,
CC threonine, methionine and isoleucine synthesis via the aspartate-family
CC pathway. {ECO:0000269|PubMed:11569502}.
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 7.4 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=560 uM for ATP {ECO:0000269|PubMed:17140415};
CC KM=1095 uM for aspartate {ECO:0000269|PubMed:17140415};
CC Note=K(cat) is 8.4/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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in xylem of leaves and hypocotyls,
CC stele of roots and in trichomes after bolting. Weak expression in veins
CC and mesophyll cells of caulone leaves, inflorescence stems, sepals,
CC petals and stigmata. {ECO:0000269|PubMed:11569502}.
CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC010797; AAF03452.1; -; Genomic_DNA.
DR EMBL; AC011664; AAF14833.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73750.1; -; Genomic_DNA.
DR EMBL; AY088366; AAM65905.1; -; mRNA.
DR EMBL; AK226200; BAE98365.1; -; mRNA.
DR RefSeq; NP_186851.1; NM_111068.4.
DR AlphaFoldDB; Q9S702; -.
DR SMR; Q9S702; -.
DR STRING; 3702.AT3G02020.1; -.
DR PaxDb; Q9S702; -.
DR PRIDE; Q9S702; -.
DR ProteomicsDB; 244723; -.
DR EnsemblPlants; AT3G02020.1; AT3G02020.1; AT3G02020.
DR GeneID; 821287; -.
DR Gramene; AT3G02020.1; AT3G02020.1; AT3G02020.
DR KEGG; ath:AT3G02020; -.
DR Araport; AT3G02020; -.
DR TAIR; locus:2078638; AT3G02020.
DR eggNOG; KOG0456; Eukaryota.
DR HOGENOM; CLU_009116_6_1_1; -.
DR InParanoid; Q9S702; -.
DR OMA; CAFERVE; -.
DR PhylomeDB; Q9S702; -.
DR BioCyc; ARA:AT3G02020-MON; -.
DR BioCyc; MetaCyc:AT3G02020-MON; -.
DR BRENDA; 2.7.2.4; 399.
DR SABIO-RK; Q9S702; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR PRO; PR:Q9S702; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S702; baseline and differential.
DR Genevisible; Q9S702; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004072; F:aspartate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009090; P:homoserine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.120.1320; -; 1.
DR Gene3D; 3.40.1160.10; -; 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 Pfam; PF00696; AA_kinase; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR00657; asp_kinases; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
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..85
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 86..559
FT /note="Aspartokinase 3, chloroplastic"
FT /id="PRO_0000248159"
FT DOMAIN 402..480
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 481..559
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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
