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Database: UniProt
Entry: A0A388LAQ5_CHABU
LinkDB: A0A388LAQ5_CHABU
Original site: A0A388LAQ5_CHABU 
ID   A0A388LAQ5_CHABU        Unreviewed;       395 AA.
AC   A0A388LAQ5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=CBR_g29552 {ECO:0000313|EMBL:GBG79405.1};
OS   Chara braunii (Braun's stonewort).
OC   Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC   Chara.
OX   NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG79405.1, ECO:0000313|Proteomes:UP000265515};
RN   [1] {ECO:0000313|EMBL:GBG79405.1, ECO:0000313|Proteomes:UP000265515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S276 {ECO:0000313|EMBL:GBG79405.1,
RC   ECO:0000313|Proteomes:UP000265515};
RX   PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA   Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA   Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA   Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA   Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA   Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA   Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA   Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA   Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA   Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA   Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA   Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA   Rensing S.A.;
RT   "The Chara Genome: Secondary Complexity and Implications for Plant
RT   Terrestrialization.";
RL   Cell 174:448-464(2018).
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         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|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, 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:GBG79405.1}.
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DR   EMBL; BFEA01000318; GBG79405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A388LAQ5; -.
DR   STRING; 69332.A0A388LAQ5; -.
DR   EnsemblPlants; GBG79405; GBG79405; CBR_g29552.
DR   Gramene; GBG79405; GBG79405; CBR_g29552.
DR   OMA; EWVDIFT; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000265515; Unassembled WGS sequence.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
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   Gene3D; 1.20.120.1320; Aspartokinase, catalytic domain; 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; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
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   PIRSF; PIRSF000726; Asp_kin; 2.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS51671; ACT; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   Kinase {ECO:0000256|RuleBase:RU003448};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265515};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          236..313
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          314..384
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   395 AA;  43636 MW;  C1B64B1122C12A1B CRC64;
     MKFLTDLHLK TAEELGVDRS LVTGLLEELQ QLLTGIALMR EMTPRTKDYL VSFGERMSTR
     LFAAYLNKNG VKACQGAKTG AITTLGRGGS DLTATAIGKA LGLKEIQVWK DVDGVLTADP
     HLVSKKALPV PYLTFDEAAE LAYFGAQVLH PQAMRPARDA DIPVRVKNSY NPAASGTLIM
     RERDMSKNFV RLQNQWEEEG VPEPAFEPTD LCLAERPSQA LLTSIVLKPH VTMLDIVSTR
     MLGQFGFLAK VFSIFEDMGI SVDCVATSEV SVSLTLDPAR MWTRELIQQE LDRVVEQLRK
     IAFVKLSQKK SIISLIGNVE RSSLILEKVF SVFRSCGINV QMISQGASKV NISVIVDDDE
     AELCVKALHC VFFEQEHLVE RLIAGYGNGN LEPCC
//
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