ID A0A0W8DZG3_PHYNI Unreviewed; 596 AA.
AC A0A0W8DZG3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN ORFNames=AM587_10015011 {ECO:0000313|EMBL:KUG01808.1}, AM588_10007770
GN {ECO:0000313|EMBL:KUF95437.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUG01808.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Race 0 {ECO:0000313|EMBL:KUG01808.1}, race 0
RC {ECO:0000313|Proteomes:UP000052943}, race 1
RC {ECO:0000313|Proteomes:UP000054636}, and Race 1
RC {ECO:0000313|EMBL:KUF95437.1};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) 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|RuleBase:RU004249}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|RuleBase:RU004249}.
CC -!- SIMILARITY: Belongs to the aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122}.
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:KUG01808.1}.
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DR EMBL; LNFP01000225; KUF95437.1; -; Genomic_DNA.
DR EMBL; LNFO01000198; KUG01808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8DZG3; -.
DR STRING; 4790.A0A0W8DZG3; -.
DR EnsemblProtists; KUF95437; KUF95437; AM588_10007770.
DR EnsemblProtists; KUG01808; KUG01808; AM587_10015011.
DR OMA; YEIWTDV; -.
DR OrthoDB; 2608453at2759; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR Proteomes; UP000054636; Unassembled WGS sequence.
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 Gene3D; 3.30.70.260; -; 2.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-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; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF59; ASPARTOKINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
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|RuleBase:RU004249};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUG01808.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..339
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT REGION 522..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 64295 MW; 8AE789E6B0A11701 CRC64;
MASSSPWVVL KFGGTSVSTA ARWRCICDQI RSHLESPSSP RVWVTISALS QITNKLTRAL
ALASERGSSH TELATNIALQ HFSLAYEVGL LPALEGVEGS VELHDRWQQL WMDSVMSHGE
DGSSFSTSPI DPLLPKTLHP LLEELKNLIR VLEGIKLTEE ASPGIQARVL AFGELLSTHL
GRCIMVHNGL TDVERVDARD LLVSDPTSAK SEEDRYLQAE VNPRLDREQA ENAANGKRVV
LTQGFIASTS TGATCVLGRG GSDTSGSLFA SLLGAQKYEI WTDVHGMFTT DPRYVPNARL
IKDLDYREAQ ELAAMGAKVL HPRCIIPAQW GKVPLEIRNT NDPNGAKTVI HPATEADKAH
HGSPKILAVV KRQNMTTLSI TAFDMYSTSG FLAKVFAPFE ACGISVDLIA TSQFSVTVTL
DHIPGGVQGA PFQQLLEALN EHSKVRVFED CSVVSIVGRG LRKALAELGC VFSVLENYDV
LLLSESAEDL NLSFVLQQKE ADEVVARMHG FFFPGDDQVS PTAAKAASTD AKPSAALPPL
PPHPSTPTAA NGEASVSPAT PAPGNVVFQQ ATIRRSPSRD LLFGPTWQSL LDSKTS
//
