ID A0A3Q9IA26_9BACL Unreviewed; 407 AA.
AC A0A3Q9IA26;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN Name=dapG {ECO:0000313|EMBL:AZS16055.1};
GN ORFNames=EI981_17520 {ECO:0000313|EMBL:AZS16055.1};
OS Paenibacillus lutimineralis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=2707005 {ECO:0000313|EMBL:AZS16055.1, ECO:0000313|Proteomes:UP000270678};
RN [1] {ECO:0000313|Proteomes:UP000270678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBLB1234 {ECO:0000313|Proteomes:UP000270678};
RA Nam Y.-D., Kang J., Chung W.-H., Park Y.S.;
RT "Complete genome sequence of Paenibacillus sp. MBLB1234.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122, ECO:0000256|RuleBase:RU003448}.
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DR EMBL; CP034346; AZS16055.1; -; Genomic_DNA.
DR RefSeq; WP_127000302.1; NZ_CP034346.1.
DR AlphaFoldDB; A0A3Q9IA26; -.
DR KEGG; plut:EI981_17520; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000270678; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0009090; P:homoserine biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR FunFam; 3.40.1160.10:FF:000002; Aspartokinase; 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; 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 NCBIfam; TIGR00656; asp_kin_monofn; 1.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR NCBIfam; NF006068; PRK08210.1; 1.
DR PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF13840; ACT_7; 1.
DR PIRSF; PIRSF000726; Asp_kin; 2.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
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:UP000270678};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT DOMAIN 3..235
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 341..400
FT /note="CASTOR ACT"
FT /evidence="ECO:0000259|Pfam:PF13840"
FT BINDING 7..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 178..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 214..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ SEQUENCE 407 AA; 43909 MW; E65C98A42AA2903C CRC64;
MRILVQKFGG TSLSTPEARD YVISHIRREL ANGFRLVVVV SAMGRKGDPY ATDTLLDLIA
GAGGSLEPRE QDLLLACGEM ISASMLSSLL NRENISSSVL TGAQAGFRTD SHYGNARILE
IVPTRVLEQL EQKDVVIVTG FQGQNQIGDF TTLGRGGSDT SATALGATLH AEMVDIYTDV
NGILTADPRI VEDARQLDYV SYAEICNMAH QGAKVIHPRA VEIAMQSGIP VRVRSTFSES
EGTLVANPEG FKDVQLGILD RYVTGIAYVN NVTQIKVDAS SGNNKEYLQL QVFKTMAENS
ISVDFINVTP SGVVYTVFDH DSDKAVHVLE QLDLRPDVLT GCAKVSVIGG GINGVPGIMA
KIVEALTEQN VQILQSADSN TTIWVLVNQD DMVAALRALH TKFELGR
//
