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Entry: A0A2K8VFE2_9FLAO
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Original site: A0A2K8VFE2_9FLAO 
ID   A0A2K8VFE2_9FLAO        Unreviewed;       418 AA.
AC   A0A2K8VFE2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=BTO06_14770 {ECO:0000313|EMBL:AUC16334.1};
OS   Tenacibaculum sp. SZ-18.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=754423 {ECO:0000313|EMBL:AUC16334.1, ECO:0000313|Proteomes:UP000232695};
RN   [1] {ECO:0000313|EMBL:AUC16334.1, ECO:0000313|Proteomes:UP000232695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZ-18 {ECO:0000313|EMBL:AUC16334.1,
RC   ECO:0000313|Proteomes:UP000232695};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-2016) 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         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|ARBA:ARBA00004766, 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}.
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DR   EMBL; CP019335; AUC16334.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8VFE2; -.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000232695; Chromosome.
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; 3.40.1160.10; 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; IPR001048; Asp/Glu/Uridylate_kinase.
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   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:AUC16334.1};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232695};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          3..274
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
SQ   SEQUENCE   418 AA;  47268 MW;  A330AE5961FEC379 CRC64;
     MRIFKFGGAS VKSPDAVRNL ARVLQHEGIE NTLVVISAMG KMTNAFERLI KAYVDGSDDL
     NEALQAIKDF HTFMMDGLFD KNDEIYNKVT YLFGELAGRM AINTSKDYNY IYDQLVGFGE
     LLSTTIVSAY LANIGVDNKW LDVREYVKTD SNYRDAKINW ELTEKIIKEK VDTSKLNITQ
     GFLGNNGEYT TTLGREGSDY TAGIFAYCLN ADSVTIWKDV QGVLNADPRV FEDTELLRNI
     SYTEAIEMAF YGASVIHPKT IQPLEQKQIP LSVRSFEDLN LEGTAVTGSA KGIEPEIPCY
     IVKKNQTLVS VSAKDFSFMV EDNISAVFKK LHDYKLKVNL IQNSAISFSV CIEDKFNNFD
     KFYNDLKSSF NMKSYKDVTL YTVRHFNDQA IESIKSKGRA IIRQINTETA QLVIQEKT
//
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