AK_CORFL
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 03-AUG-2022, entry version 109.
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; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC 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=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: 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}.
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DR EMBL; L16848; AAA23293.1; -; Genomic_DNA.
DR AlphaFoldDB; P41398; -.
DR SMR; P41398; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04261; AAK_AKii-LysC-BS; 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; 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 InterPro; IPR027795; CASTOR_ACT_dom.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF13840; ACT_7; 1.
DR PIRSF; PIRSF000726; Asp_kin; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR TIGRFAMs; TIGR00657; asp_kinases; 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
