AK2_ARATH
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 03-AUG-2022, entry version 140.
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.AT5G14060.2; -.
DR iPTMnet; O23653; -.
DR MetOSite; O23653; -.
DR PaxDb; O23653; -.
DR PRIDE; O23653; -.
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; locus:2174708; AT5G14060.
DR eggNOG; KOG0456; Eukaryota.
DR HOGENOM; CLU_009116_6_1_1; -.
DR InParanoid; O23653; -.
DR OMA; IIQSQRC; -.
DR OrthoDB; 113181at2759; -.
DR PhylomeDB; O23653; -.
DR BioCyc; ARA:AT5G14060-MON; -.
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 Genevisible; O23653; AT.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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; 2.
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..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
