ID A0A495AD81_9BACI Unreviewed; 412 AA.
AC A0A495AD81;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN Name=dapG {ECO:0000313|EMBL:RKQ37534.1};
GN ORFNames=D8M06_01635 {ECO:0000313|EMBL:RKQ37534.1};
OS Oceanobacillus halophilus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Oceanobacillus.
OX NCBI_TaxID=930130 {ECO:0000313|EMBL:RKQ37534.1, ECO:0000313|Proteomes:UP000269301};
RN [1] {ECO:0000313|EMBL:RKQ37534.1, ECO:0000313|Proteomes:UP000269301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23996 {ECO:0000313|EMBL:RKQ37534.1,
RC ECO:0000313|Proteomes:UP000269301};
RX PubMed=26869142; DOI=.1099/ijsem.0.000952;
RA Amoozegar M.A., Bagheri M., Makhdoumi A., Nikou M.M., Fazeli S.A.S.,
RA Schumann P., Sproer C., Sanchez-Porro C., Ventosa A.;
RT "Oceanobacillus halophilus sp. nov., a novel moderately halophilic
RT bacterium from a hypersaline lake.";
RL Int. J. Syst. Evol. Microbiol. 66:1317-1322(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKQ37534.1}.
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DR EMBL; RBZP01000001; RKQ37534.1; -; Genomic_DNA.
DR RefSeq; WP_121202614.1; NZ_RBZP01000001.1.
DR AlphaFoldDB; A0A495AD81; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000269301; Unassembled WGS sequence.
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 CDD; cd04914; ACT_AKi-DapG-BS_1; 1.
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; IPR002912; ACT_dom.
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; NF005155; PRK06635.1-4; 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; PS51671; ACT; 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:UP000269301};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT DOMAIN 344..412
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 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 412 AA; 44572 MW; CC7985AE6A9B34C3 CRC64;
MQILVQKFGG TSVQSEENRQ HVIKHIKNAL VKNYKLVVVV SALGRKPDPY ATDTLLDLVN
FPANSNTNRE IDLLMSCGEI ISSVVLSNEL QNNHIAATTL TGAQAGFVTT EDFTQAKIKQ
VKPDRVYKEL ESHDVVVVAG FQGQSESGEI TTIGRGGSDT TAAALGAALQ AETIEIFTDV
NGIMTADPRM VENARSLDIV TYTEICNLAY QGAKVVHPRA VEIAMQAKIP MRVRSTYSLE
PGTLVTSSRE REMGVDIPDR LITGIAHMSQ VTQIKVQTKE DSYRLQSDVF KAMAESGISV
DFINISPAGV IYTVPDHLAN KAVHVLETLG FHPEITEKCA KVSAVGAGMT GVPGVAAKIV
QALTDNGVQI LQSADSHTTI WVLVHEKDLK TAVNALHNVF TLNNLNKIDS SR
//
