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Database: UniProt
Entry: A0A265V0B8_9FLAO
LinkDB: A0A265V0B8_9FLAO
Original site: A0A265V0B8_9FLAO 
ID   A0A265V0B8_9FLAO        Unreviewed;       416 AA.
AC   A0A265V0B8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=CA834_02550 {ECO:0000313|EMBL:OZV71014.1};
OS   Winogradskyella aurantia.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1915063 {ECO:0000313|EMBL:OZV71014.1, ECO:0000313|Proteomes:UP000216840};
RN   [1] {ECO:0000313|EMBL:OZV71014.1, ECO:0000313|Proteomes:UP000216840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WNB302 {ECO:0000313|EMBL:OZV71014.1,
RC   ECO:0000313|Proteomes:UP000216840};
RA   Sun Y., Chen B., Du Z.;
RT   "The draft genome sequence of Idiomarina salinarum WNB302.";
RL   Submitted (MAY-2017) 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}.
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:OZV71014.1}.
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DR   EMBL; NGJN01000001; OZV71014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A265V0B8; -.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000216840; 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   CDD; cd04243; AAK_AK-HSDH-like; 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; 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; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:OZV71014.1};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216840};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          2..277
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ   SEQUENCE   416 AA;  47673 MW;  BB13D1949EF704ED CRC64;
     MRVFKFGGAS VKDAEGVKNL ATVLKTTGYD NTLVVVSAMG KTTNAMERVI KNYFENKPEL
     QSSIHDVIKY HNEILMDLFE NEQHQVYGAV KSYFDELNRF LKSNKSPDYN YVYDQTIGFG
     ELISTTIVSY YLNEIGLSNQ WIDVREFIKT DNYYRRASVN WELTQEKITT GFNTSKLNLT
     QGFLGSDANN FTTTLGREGS DYTAAIFAYC LNADSVTIWK DVPGVLNADP RYFENAQLIH
     QISYREAIEL AFYGATVIHP KTLQPMQRKE IPLYVKSFLN PQDKGTCVSK GRSLDPEIPC
     FIVKKNQTLI SLSSLDFSYI VEENISDIFS LLHLYKMKVD VIQNSAISFS VCIDNLYDNL
     EKLLQHLKAK FNVTSYENVS LYTIRHYNET VIKELEKDKT VLLKQLTRET VQIVTK
//
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