AK1_ARATH
ID AK1_ARATH Reviewed; 569 AA.
AC Q9LYU8; O23152;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Aspartokinase 1, chloroplastic;
DE EC=2.7.2.4;
DE AltName: Full=Aspartate kinase 1;
DE Flags: Precursor;
GN Name=AK1; Synonyms=AK, AK-LYS1; OrderedLocusNames=At5g13280;
GN ORFNames=T31B5.100;
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].
RC STRAIN=cv. Columbia;
RX PubMed=9207839; DOI=10.1023/a:1005863128558;
RA Frankard V., Vauterin M., Jacobs M.;
RT "Molecular characterisation of an Arabidopsis thaliana cDNA coding for a
RT monofunctional aspartate kinase.";
RL Plant Mol. Biol. 34:233-242(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=6252474; DOI=10.1038/287357a0;
RA Rognes S.E., Lea P.J., Miflin B.J.;
RT "S-adenosylmethionine -- a novel regulator of aspartate kinase.";
RL Nature 287:357-359(1980).
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 61-569 IN COMPLEX WITH SUBSTRATE
RP ANALOG AND ALLOSTERIC REGULATORS, AND SUBUNIT.
RX PubMed=16731588; DOI=10.1105/tpc.105.040451;
RA Mas-Droux C., Curien G., Robert-Genthon M., Laurencin M., Ferrer J.L.,
RA Dumas R.;
RT "A novel organization of ACT domains in allosteric enzymes revealed by the
RT crystal structure of Arabidopsis aspartate kinase.";
RL Plant Cell 18:1681-1692(2006).
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: Inhibited by S-adenosyl-L-methionine (SAM) and
CC lysine in a synergistic manner. No inhibition by threonine, leucine or
CC SAM alone, and no activation or inhibition by alanine, cysteine,
CC isoleucine, serine, valine, methionine, glutamine, asparagine, glutamic
CC acid or arginine. {ECO:0000269|PubMed:17140415,
CC ECO:0000269|PubMed:6252474}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1700 uM for ATP {ECO:0000269|PubMed:17140415};
CC KM=2037 uM for aspartate {ECO:0000269|PubMed:17140415};
CC Note=K(cat) is 23.4/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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16731588}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- MISCELLANEOUS: Only one ACT domain (ACT1) is implicated in effector
CC binding.
CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR EMBL; X98873; CAA67376.1; -; mRNA.
DR EMBL; AL163491; CAB86635.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91874.1; -; Genomic_DNA.
DR EMBL; BT000493; AAN18062.1; -; mRNA.
DR EMBL; AY057674; AAL15305.1; -; mRNA.
DR PIR; T48575; T48575.
DR RefSeq; NP_196832.1; NM_121331.3.
DR PDB; 2CDQ; X-ray; 2.85 A; A/B=61-569.
DR PDBsum; 2CDQ; -.
DR AlphaFoldDB; Q9LYU8; -.
DR SMR; Q9LYU8; -.
DR BioGRID; 16447; 5.
DR IntAct; Q9LYU8; 4.
DR STRING; 3702.AT5G13280.1; -.
DR iPTMnet; Q9LYU8; -.
DR MetOSite; Q9LYU8; -.
DR PaxDb; Q9LYU8; -.
DR PRIDE; Q9LYU8; -.
DR ProteomicsDB; 244922; -.
DR EnsemblPlants; AT5G13280.1; AT5G13280.1; AT5G13280.
DR GeneID; 831169; -.
DR Gramene; AT5G13280.1; AT5G13280.1; AT5G13280.
DR KEGG; ath:AT5G13280; -.
DR Araport; AT5G13280; -.
DR TAIR; locus:2183896; AT5G13280.
DR eggNOG; KOG0456; Eukaryota.
DR HOGENOM; CLU_009116_6_1_1; -.
DR InParanoid; Q9LYU8; -.
DR OMA; DMIVQTI; -.
DR OrthoDB; 113181at2759; -.
DR PhylomeDB; Q9LYU8; -.
DR BioCyc; ARA:AT5G13280-MON; -.
DR BRENDA; 2.7.2.4; 399.
DR SABIO-RK; Q9LYU8; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR EvolutionaryTrace; Q9LYU8; -.
DR PRO; PR:Q9LYU8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYU8; baseline and differential.
DR Genevisible; Q9LYU8; AT.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0004072; F:aspartate kinase activity; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:TAIR.
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 CDD; cd04244; AAK_AK-LysC-like; 1.
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; IPR041746; AK-LysC-like.
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 3D-structure; Amino-acid biosynthesis; ATP-binding; Chloroplast; Kinase;
KW Nucleotide-binding; Plastid; Reference proteome; Repeat;
KW Threonine biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..90
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 91..569
FT /note="Aspartokinase 1, chloroplastic"
FT /id="PRO_0000248157"
FT DOMAIN 405..483
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 484..560
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="substrate"
FT BINDING 413
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /ligand_note="allosteric effector"
FT BINDING 415
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /ligand_note="allosteric effector"
FT BINDING 430
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_note="allosteric effector"
FT BINDING 431
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /ligand_note="allosteric effector"
FT BINDING 432
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /ligand_note="allosteric effector"
FT BINDING 437
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /ligand_note="allosteric effector"
FT BINDING 452
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_note="allosteric effector"
FT BINDING 453
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_note="allosteric effector"
FT CONFLICT 369
FT /note="N -> S (in Ref. 1; CAA67376)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="N -> D (in Ref. 1; CAA67376)"
FT /evidence="ECO:0000305"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:2CDQ"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2CDQ"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 172..191
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 196..220
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 268..278
FT /evidence="ECO:0007829|PDB:2CDQ"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 308..320
FT /evidence="ECO:0007829|PDB:2CDQ"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 391..406
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 416..426
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:2CDQ"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 471..486
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 491..505
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:2CDQ"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:2CDQ"
FT HELIX 527..542
FT /evidence="ECO:0007829|PDB:2CDQ"
SQ SEQUENCE 569 AA; 62298 MW; F66A35F4E84DC429 CRC64;
MAATRVRCCH SNAAFTRLPL TRHRNSPTLP ISLNRVDFPT LKKLSLPIGD GSSIRKVSGS
GSRNIVRAVL EEKKTEAITE VDEKGITCVM KFGGSSVASA ERMKEVADLI LTFPEESPVI
VLSAMGKTTN NLLLAGEKAV SCGVSNASEI EELSIIKELH IRTVKELNID PSVILTYLEE
LEQLLKGIAM MKELTLRTRD YLVSFGECLS TRIFAAYLNT IGVKARQYDA FEIGFITTDD
FTNGDILEAT YPAVAKRLYD DWMHDPAVPI VTGFLGKGWK TGAVTTLGRG GSDLTATTIG
KALGLKEIQV WKDVDGVLTC DPTIYKRATP VPYLTFDEAA ELAYFGAQVL HPQSMRPARE
GEIPVRVKNS YNPKAPGTII TKTRDMTKSI LTSIVLKRNV TMLDIASTRM LGQVGFLAKV
FSIFEELGIS VDVVATSEVS ISLTLDPSKL WSRELIQQEL DHVVEELEKI AVVNLLKGRA
IISLIGNVQH SSLILERAFH VLYTKGVNVQ MISQGASKVN ISFIVNEAEA EGCVQALHKS
FFESGDLSEL LIQPRLGNGS PVRTLQVEN
