ID AK_CORFL Reviewed; 421 AA. AC P41398; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 124. DE RecName: Full=Aspartokinase; DE EC=2.7.2.4; DE AltName: Full=Aspartate kinase; GN Name=lysC; Synonyms=ask; OS Corynebacterium flavescens. OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=28028; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ASP-345, AND ACTIVITY RP REGULATION. RC STRAIN=N13; RX PubMed=8100567; DOI=10.1128/jb.175.13.4096-4103.1993; RA Follettie M.T., Peoples O.P., Agoropoulou C., Sinskey A.J.; RT "Gene structure and expression of the Corynebacterium flavum N13 ask-asd RT operon."; RL J. Bacteriol. 175:4096-4103(1993). CC -!- FUNCTION: Catalyzes the phosphorylation of the beta-carboxyl group of CC aspartic acid with ATP to yield 4-phospho-L-aspartate, which is CC involved in the branched biosynthetic pathway leading to the CC biosynthesis of amino acids lysine, threonine, isoleucine and CC methionine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate + ATP = 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: Low feedback inhibition by lysine and threonine. CC The decreased sensitivity of C.flavum, as compared to C.glutamicum, is CC probably due to the Asp-345-Gly sequence difference. CC {ECO:0000269|PubMed:8100567}. 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: Tetramer consisting of 2 isoforms Alpha (catalytic and CC regulation) and of a homodimer of 2 isoforms Beta (regulation). CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Alpha; Synonyms=Aspartokinase subunit alpha; CC IsoId=P41398-1; Sequence=Displayed; CC Name=Beta; Synonyms=Aspartokinase subunit beta; CC IsoId=P41398-2; Sequence=VSP_018657, VSP_018658; 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; L16848; AAA23293.1; -; Genomic_DNA. DR AlphaFoldDB; P41398; -. DR SMR; P41398; -. DR STRING; 28028.CFLV_01295; -. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00461. DR UniPathway; UPA00051; UER00462. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009090; P:L-homoserine biosynthetic process; IEA:TreeGrafter. DR GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd04261; AAK_AKii-LysC-BS; 1. DR CDD; cd04923; ACT_AK-LysC-DapG-like_2; 1. DR CDD; cd04913; ACT_AKii-LysC-BS-like_1; 1. DR FunFam; 3.40.1160.10:FF:000002; Aspartokinase; 1. DR Gene3D; 3.30.70.260; -; 2. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR045865; ACT-like_dom_sf. DR InterPro; IPR054352; ACT_Aspartokinase. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR041740; AKii-LysC-BS. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kinase. DR InterPro; IPR018042; Aspartate_kinase_CS. DR NCBIfam; TIGR00656; asp_kin_monofn; 1. DR NCBIfam; TIGR00657; asp_kinases; 1. DR NCBIfam; NF005153; PRK06635.1-1; 1. DR NCBIfam; NF005154; PRK06635.1-2; 1. DR NCBIfam; NF005155; PRK06635.1-4; 1. DR PANTHER; PTHR21499; ASPARTATE KINASE; 1. DR PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF22468; ACT_9; 2. DR PIRSF; PIRSF000726; Asp_kin; 1. DR SUPFAM; SSF55021; ACT-like; 2. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. DR PROSITE; PS51671; ACT; 2. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 1: Evidence at protein level; KW Alternative initiation; Amino-acid biosynthesis; ATP-binding; KW Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis; KW Nucleotide-binding; Repeat; Transferase. FT CHAIN 1..421 FT /note="Aspartokinase" FT /id="PRO_0000002377" FT DOMAIN 267..343 FT /note="ACT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007" FT DOMAIN 349..421 FT /note="ACT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007" FT BINDING 7..10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 25..30 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 45..49 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 125..126 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 151..154 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 174..175 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 180..185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 274..279 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 274 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 292..294 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 298 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 360..361 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 374..375 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 381..382 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 7 FT /note="Contribution to the catalysis" FT /evidence="ECO:0000250" FT SITE 74 FT /note="Contribution to the catalysis" FT /evidence="ECO:0000250" FT VAR_SEQ 1..249 FT /note="Missing (in isoform Beta)" FT /evidence="ECO:0000305" FT /id="VSP_018657" FT VAR_SEQ 250 FT /note="V -> M (in isoform Beta)" FT /evidence="ECO:0000305" FT /id="VSP_018658" FT MUTAGEN 345 FT /note="D->G: Decreased sensitivity of AK activity to FT concerted feedback inhibition by lysine and threonine." FT /evidence="ECO:0000269|PubMed:8100567" SQ SEQUENCE 421 AA; 44797 MW; 4B37B0B6597F665E CRC64; MALVVQKYGG SSLESAERIR NVAERIVATK KAGNDVVVVC SAMGDTTDEL LELAAAVNPV PPAREMDMLL TAGERISNAL VAMAIESLGA EAQSFTGSQA GVLTTERHGN ARIVDVTPGR VREALDEGKI CIVAGFQGVN KETRDVTTLG RGGSDTTAVA LAAALNADVC EIYSDVDGVY TADPRIVPNA QKLEKLSFEE MLELAAVGSK ILVLRSVEYA RAFNVPLRVR SSYSNDPGTL IAGSMEDIPV EEAVLTGVAT DKSEAKVTVL GISDKPGEAA KVFRALADAE INIDMVLQNV SSVEDGTTDI TFTCPRADGR RAMEILKKLQ VQGNWTNVLY DDQVDKVSLV GAGMKSHPGV TAEFMEALRD VNVNIELIST SEIRISVLIR EDDLDAAARA LHEQFQLGGE DEAVVYAGTG R //