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Database: UniProt
Entry: A0A1H3M0A3_9BACI
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ID   A0A1H3M0A3_9BACI        Unreviewed;       405 AA.
AC   A0A1H3M0A3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   18-JUN-2025, entry version 31.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=SAMN05421736_10371 {ECO:0000313|EMBL:SDY70006.1};
OS   Evansella caseinilytica.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Evansella.
OX   NCBI_TaxID=1503961 {ECO:0000313|EMBL:SDY70006.1, ECO:0000313|Proteomes:UP000198935};
RN   [1] {ECO:0000313|Proteomes:UP000198935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP {ECO:0000313|Proteomes:UP000198935};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FNPI01000003; SDY70006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3M0A3; -.
DR   STRING; 1503961.SAMN05421736_10371; -.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000198935; 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   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; 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:UP000198935};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          344..405
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   405 AA;  43418 MW;  DE4B83678EA5D4CB CRC64;
     MKVAVQKFGG TSLKNEELRE HALEHVLDAL RDGYKVVVVV SAMGRTGDPY ATDTLLDLVG
     GHRGNVSKRE LDLLASCGET ISSVVFSNLL NRKGIKALAM TGAQAGFRTN EEYTNAKIID
     MKVEGLRNHL EEYDAIVVTG FQGETPKGTL ATLGRGGSDT SATALGAALK AEVVDIFTDV
     AGVMTADPRI VDGAKPLNVV TYNEICNLAY QGAKVIHPRA VEVAMQAKVP IRIRSTTTKN
     EGTLITSSTT KQVGRDVEDR PVTGIAHVSN VTQVKVFAKE GEYDLQTKVF KAMAKESISV
     DFINIHPMGV AYTVSDDVAD RAVAILEKLD LTPQIVRNCA KVSAVGAGMT GVPGVTSRIV
     EALTSKNIQI LQSADSHTTI WVLVKGEDMV EAVNALHEKF LSERV
//
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