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Database: UniProt
Entry: A0A3B6N168_WHEAT
LinkDB: A0A3B6N168_WHEAT
Original site: A0A3B6N168_WHEAT 
ID   A0A3B6N168_WHEAT        Unreviewed;       561 AA.
AC   A0A3B6N168;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE            EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN   ORFNames=CFC21_080460 {ECO:0000313|EMBL:KAF7075703.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5D02G487000.1};
RN   [1] {ECO:0000313|EMBL:KAF7075703.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7075703.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS5D02G487000.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS5D02G487000.1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS5D02G487000.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7075703.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7075703.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) 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}.
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DR   EMBL; CM022225; KAF7075703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6N168; -.
DR   EnsemblPlants; TraesCS5D02G487000.1; TraesCS5D02G487000.1; TraesCS5D02G487000.
DR   Gramene; TraesCS5D02G487000.1; TraesCS5D02G487000.1; TraesCS5D02G487000.
DR   Gramene; TraesCS5D03G1070000.1; TraesCS5D03G1070000.1.CDS; TraesCS5D03G1070000.
DR   Gramene; TraesKAR5D01G0381560.1; cds.TraesKAR5D01G0381560.1; TraesKAR5D01G0381560.
DR   Gramene; TraesWEE_scaffold_085005_01G000100.1; TraesWEE_scaffold_085005_01G000100.1; TraesWEE_scaffold_085005_01G000100.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000019116; Chromosome 5D.
DR   Proteomes; UP000815260; Chromosome 5D.
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; cd04244; AAK_AK-LysC-like; 1.
DR   CDD; cd04933; ACT_AK1-AT_1; 1.
DR   CDD; cd04918; ACT_AK1-AT_2; 1.
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; IPR041746; AK-LysC-like.
DR   InterPro; IPR047896; AK1_ACT_1.
DR   InterPro; IPR047895; AK1_ACT_2.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   NCBIfam; TIGR00657; asp_kinases; 1.
DR   PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR   PANTHER; PTHR21499:SF66; ASPARTATE KINASE; 1.
DR   Pfam; PF00696; AA_kinase; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          393..471
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   561 AA;  60090 MW;  AA798A363F30A98D CRC64;
     MATALRLAAV ARDSPAAVSK LGRERASLCA IARPGGQCFA RRGLVLRCQS GAAAAAATIS
     KGGAADGAGA AAGFTVVMKF GGSSLASAAR MREVADLILS FPEETPVVVL SAMGKTTNNL
     LLAGEKAVSC GAPKASEINE LAVIKKLHLR TIDELGLDSS IVSGFLDELE QLLKGVAMMK
     ELTLRTRDYL VSFGECMSTR IFSAYLNKLG KKARQYDAFD LGFITTDDFT NADILEATYP
     AVAKRLHGDW IDDPAIPIVT GFLGKGWKSC AVTTLGRGGS DLTATTIGKA LGLREIQVWK
     DVDGVLTCDP NIYANAVPVP YLTFDEAAEL AYFGAQVLHP QSMRPAREGG IPVRVKNSYN
     RHAPGTVITK TRDMRKSILT SIVLKSNITM LDIVSTRMLG QYGFLAKVFS IFEDLGISVD
     SVATSEVSIS LTLDPSKLWS RELIQQELDH VVEELEKIAV VHLLQHRSII SLIGNVQRSS
     LILEKAFNVL RRNGVNVQMI SQGASKVNIS LVVNDSEAKQ CVQALHSAFF ENGFLSEVEE
     ADLAQNMAPV LVSSNGAING N
//
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