ID   AK_BACSG                Reviewed;         411 AA.
AC   Q59229;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Aspartokinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase;
GN   Name=lysC;
OS   Bacillus sp. (strain MGA3).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=126782;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1444390; DOI=10.1128/aem.58.9.2806-2814.1992;
RA   Schendel F.J., Flickinger M.C.;
RT   "Cloning and nucleotide sequence of the gene coding for aspartokinase II
RT   from a thermophilic methylotrophic Bacillus sp.";
RL   Appl. Environ. Microbiol. 58:2806-2814(1992).
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 threonine, isoleucine and methionine.
CC       {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: Lysine-sensitive.
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 2 subunit alpha;
CC         IsoId=Q59229-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=Aspartokinase 2 subunit beta;
CC         IsoId=Q59229-2; Sequence=VSP_018653;
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; M93419; AAA22251.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59229; -.
DR   SMR; Q59229; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   GO; GO:0004072; F:aspartate kinase activity; IDA:CACAO.
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; 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; Direct protein sequencing; Kinase;
KW   Lysine biosynthesis; Nucleotide-binding; Repeat; Transferase.
FT   CHAIN           1..411
FT                   /note="Aspartokinase"
FT                   /id="PRO_0000002369"
FT   DOMAIN          264..338
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   DOMAIN          344..411
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         47..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         150..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         179..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         289..291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         355..356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         369..370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         376..377
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..245
FT                   /note="Missing (in isoform Beta)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018653"
SQ   SEQUENCE   411 AA;  44343 MW;  94061572E369CD48 CRC64;
     MGLIVQKFGG TSVGSVERIL NVANRVIEEK KNGNDVVVVV SAMGKTTDEL VDLAKQISAH
     PPKREMDMLL TTGEQVTISL LAMALNEKGY EAISYTGWQA GITTEPVFGN ARILNIETEK
     IQKQLNEGKI VVVAGFQGID EHGEITTLGR GGSDTTAVAL AAALKAEKCD IYTDVTGVFT
     TDPRYVKSAR KLASISYDEM LELANLGAGV LHPRAVEFAK NYGITLEVRS SMEREEGTII
     EEEVTMEQNL VVRGVAFEDE ITRVTVFGLP NSLTSLSTIF TTLAQNRINV DIIIQSATDA
     ETTNLSFSIK SDDLEETMAV LENNKNLLNY QGIESETGLA KVSIVGSGMI SNPGVAAKMF
     EVLALNGIQV KMVSTSEIKV STVVEESQMI KAVEALHQAF ELSGSAVKSE R