ID   A7GNP1_BACCN            Unreviewed;       410 AA.
AC   A7GNP1;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   04-NOV-2026, entry version 125.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   OrderedLocusNames=Bcer98_1430 {ECO:0000313|EMBL:ABS21749.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21749.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS21749.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., Sanchis V.,
RA   Nguen-The C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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:0000256|ARBA:ARBA00003121}.
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         Evidence={ECO:0000256|ARBA:ARBA00047872,
CC         ECO:0000256|RuleBase:RU003448};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004766, ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004986, ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139,
CC       ECO:0000256|RuleBase:RU004249}.
CC   -!- SUBUNIT: Tetramer consisting of 2 isoforms Alpha (catalytic and
CC       regulation) and of a homodimer of 2 isoforms Beta (regulation).
CC       {ECO:0000256|ARBA:ARBA00063835}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|ARBA:ARBA00010122, ECO:0000256|RuleBase:RU003448}.
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DR   EMBL; CP000764; ABS21749.1; -; Genomic_DNA.
DR   RefSeq; WP_012093923.1; NC_009674.1.
DR   AlphaFoldDB; A7GNP1; -.
DR   STRING; 315749.Bcer98_1430; -.
DR   PaxDb; 315749-Bcer98_1430; -.
DR   GeneID; 33896770; -.
DR   KEGG; bcy:Bcer98_1430; -.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_009116_3_2_9; -.
DR   OMA; AADNIHD; -.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000002300; Chromosome.
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:0009085; P:L-lysine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04261; AAK_AKii-LysC-BS; 1.
DR   CDD; cd04913; ACT_AKii-LysC-BS-like_1; 1.
DR   CDD; cd04936; ACT_AKii-LysC-BS-like_2; 1.
DR   FunFam; 3.40.1160.10:FF:000002; Aspartokinase; 1.
DR   FunFam; 3.30.2130.10:FF:000001; Bifunctional aspartokinase/homoserine dehydrogenase; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   Gene3D; 3.30.2130.10; VC0802-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; NF005154; PRK06635.1-2; 1.
DR   NCBIfam; NF005155; PRK06635.1-4; 1.
DR   NCBIfam; NF005156; PRK06635.1-5; 1.
DR   PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR   PANTHER; PTHR21499:SF68; ASPARTOKINASE 2; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF22468; ACT_9; 1.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000726-
KW   1}; Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002300};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          262..336
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          342..410
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   BINDING         7..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         173..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ   SEQUENCE   410 AA;  44896 MW;  5461CB86FF987D70 CRC64;
     METIVQKFGG TSVGNIQRIQ HVANLMIEEY EKGHNVVTVV SAMGKSTDKL VALATSITEN
     PSKRELDMLL TTGEQVTISL LTMALQTKGY QAISLTGWQA GITTEPVHGN ARITDIHTER
     IQSYLQEGTI VIVAGFQGLS EEKEITTLGR GGSDTTAVAL AAALKAKKCD IYTDVTGVYT
     TDPRVVNNAY KLDEISYDEM LELANLGAGV LHPRAVEFAK NHNVVLEVRS SMEQENGTIV
     RGECNMEQQS IVKGIAFEDN ITRVTIKGLE HDSLSTIFST LAEAHINVDI IIQSITNEGT
     VHLSFSIHSN DLRETLEALK QNQETLHYES VEYENHLAKV SIVGSGMVSN PGVAAHMFST
     LKEENIHVKM VSTSEIKISV VIDRLHLVDG VEALHQAFMT KVEPLVQMNK
//