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Entry: A0A0G4J322_PLABS
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ID   A0A0G4J322_PLABS        Unreviewed;       759 AA.
AC   A0A0G4J322;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE            EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN   ORFNames=PBRA_008691 {ECO:0000313|EMBL:CEP01749.1}, PLBR_LOCUS8685
GN   {ECO:0000313|EMBL:SPR01470.1};
OS   Plasmodiophora brassicae (Clubroot disease agent).
OG   Mitochondrion {ECO:0000313|EMBL:SPR01470.1}.
OC   Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC   Plasmodiophoridae; Plasmodiophora.
OX   NCBI_TaxID=37360 {ECO:0000313|EMBL:CEP01749.1, ECO:0000313|Proteomes:UP000039324};
RN   [1] {ECO:0000313|EMBL:CEP01749.1, ECO:0000313|Proteomes:UP000039324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:CEP01749.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SPR01470.1, ECO:0000313|Proteomes:UP000290189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fogelqvist J.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000709};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC       {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}.
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DR   EMBL; CDSF01000117; CEP01749.1; -; Genomic_DNA.
DR   EMBL; OVEO01000017; SPR01470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4J322; -.
DR   STRING; 37360.A0A0G4J322; -.
DR   EnsemblProtists; CEP01749; CEP01749; PBRA_008691.
DR   OrthoDB; 2608453at2759; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000039324; Unassembled WGS sequence.
DR   Proteomes; UP000290189; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; 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; cd04921; ACT_AKi-HSDH-ThrA-like_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; IPR001341; Asp_kinase.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR027795; CASTOR_ACT_dom.
DR   NCBIfam; TIGR00657; asp_kinases; 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   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|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Mitochondrion {ECO:0000313|EMBL:SPR01470.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039324};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          421..498
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   759 AA;  81041 MW;  CE3B44AD57C338E9 CRC64;
     MAWVVHKFGG TSVADAGCYR RAVSLLGDDI GAGHGVVVVV SAQGRARDAH GAMTHDKVTS
     LLIECASRAA RRDSSYADVL RAVVDRHVAA AHDLIDDDTE RDAFLRRLNA DATDLHHILK
     SAWLGRRASS DGSPCPWWTG YGELWSARLF AIHLRESLPD DIAVEFIDAR SLVVVGEGGY
     PDMAETSTRW QAWRIKHGDV RVAVLTGFIC AAHDGTPSTL GRDGSDYSAS IAAAMIPASS
     LTIWSDVDGV FSADPTMVPG AVVRNEMTYN EAMELAYFGA KVLHPKTMSP LLNLDIPIRI
     RNTFRPDIPG SRIVASRPAG SADIVIQGFS TIMDLMLINV EGTGMIGVSG IAHRLFGAIH
     RAGSSVILIT QAGSEHSICL ALPYAQASAA VDAIYAEFRV ELEAGDIQTV DCLGPCACLA
     AVGDGMRHAT GIAGQVLTAL GRANINIRAI AQGASERNIS VVIDQVDASA ALNAVHGQFV
     SNDANRIIAL ATYNCCDRVQ RLVDSIPDLC VSLWNGEVPP PSSIVIDCSG DDTVDYVPAL
     KSNCHVITCN VFAAARASPS SNLWTHGITD ASVPFQATVA AIHDSGDTVE RVVLALPDSV
     SNTAASDNAD ASVGERDCKE RLPSRSAHRG RCLLVVLSNA IGMPITLDDI VSDSETELDA
     ADEECDSARL QRTEGKSEAH AMHVWELDLI TRTARSDLLQ TKHMHADSRR LSVEIYTRRR
     GGSDPIALSG PASVNDDVII GLMQSQLTRV LRQTKCPTN
//
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