ID A0A2K3MNV7_TRIPR Unreviewed; 398 AA.
AC A0A2K3MNV7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN ORFNames=L195_g015535 {ECO:0000313|EMBL:PNX92399.1};
OS Trifolium pratense (Red clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=57577 {ECO:0000313|EMBL:PNX92399.1, ECO:0000313|Proteomes:UP000236291};
RN [1] {ECO:0000313|EMBL:PNX92399.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNX92399.1};
RX PubMed=24500806; DOI=10.3732/ajb.1300340;
RA Istvanek J., Jaros M., Krenek A., Repkova J.;
RT "Genome assembly and annotation for red clover (Trifolium pratense;
RT Fabaceae).";
RL Am. J. Bot. 101:327-337(2014).
RN [2] {ECO:0000313|EMBL:PNX92399.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNX92399.1};
RX PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT (Trifolium pratense) Breeding.";
RL Front. Plant Sci. 8:367-367(2017).
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:PNX92399.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASHM01010552; PNX92399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3MNV7; -.
DR STRING; 57577.A0A2K3MNV7; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000236291; Unassembled WGS sequence.
DR ExpressionAtlas; A0A2K3MNV7; baseline.
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; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS51671; ACT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:PNX92399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236291};
KW Transferase {ECO:0000256|RuleBase:RU003448}.
FT DOMAIN 237..317
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 398 AA; 43823 MW; 28069726BFA178A2 CRC64;
MYVEIFPEHL VELEQLLNGI AMMKELTKRT QDYLVSFGEC MSTRIFAAYL NKLGVKARQY
DAFEMGFITT DDFTNADILE ATYPAVAKRL HGDWLADPAI AIVTGFLGKA RKSCAVTTLG
RGGSDLTATT IGKALGLPEI QVWKDVDGVL TCDPNIYPKA EPVPFLTFDE AAELAYFGAQ
VLHPQSMRPA RESDIPVRVK NSYNPKAPGT LITKERDMSK AVLTSIVLKR NVTMLDIVST
RMLGQYGFLA KVFSIFEDLG ISVDVVATSE VSVSLTLDPS KLWSRELIQQ ASELDHVVEE
LEKIAVVNLL QNRSIISLIG NVQKSSLILE KAFRVLRTLG VTVQMISQGA SKVNISLVVN
DSEADQCVRA LHEAFFESEY SNLHKEYTSG NGSVAKSS
//
