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Database: UniProt
Entry: A0A193KEF1_9VIBR
LinkDB: A0A193KEF1_9VIBR
Original site: A0A193KEF1_9VIBR 
ID   A0A193KEF1_9VIBR        Unreviewed;       390 AA.
AC   A0A193KEF1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=A6E01_10780 {ECO:0000313|EMBL:ANO33680.1};
OS   Vibrio breoganii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=553239 {ECO:0000313|EMBL:ANO33680.1, ECO:0000313|Proteomes:UP000092018};
RN   [1] {ECO:0000313|EMBL:ANO33680.1, ECO:0000313|Proteomes:UP000092018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FF50 {ECO:0000313|EMBL:ANO33680.1,
RC   ECO:0000313|Proteomes:UP000092018};
RA   Hehemann J.-H., Arevalo P., Datta M.S., Yu X., Corzett C., Henschel A.,
RA   Preheim S.P., Timberlake S., Alm E.J., Polz M.F.;
RT   "Adaptive Radiation by Waves of Gene Transfer Leads to Fine-Scale Resource
RT   Partitioning in Marine Microbes.";
RL   Submitted (JUN-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|ARBA:ARBA00004986, ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139,
CC       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; CP016177; ANO33680.1; -; Genomic_DNA.
DR   RefSeq; WP_065210206.1; NZ_SYVS01000155.1.
DR   AlphaFoldDB; A0A193KEF1; -.
DR   STRING; 553239.A6E01_10780; -.
DR   GeneID; 77304847; -.
DR   KEGG; vbr:A6E01_10780; -.
DR   eggNOG; COG0527; Bacteria.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000092018; Chromosome 1.
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   CDD; cd04261; AAK_AKii-LysC-BS; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR041740; AKii-LysC-BS.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   NCBIfam; TIGR00657; asp_kinases; 1.
DR   PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR   PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:ANO33680.1};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN          5..231
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
SQ   SEQUENCE   390 AA;  42370 MW;  9A101B26B33D3DF3 CRC64;
     MKNRLIVQKF GGTSVGSVER IRAVAEQVIK TKEQGNQVVV VVSAMSGETN RLQGLAYEVD
     SVPNSRELDV ILSAGEQVTI ALLAMTLNKL GHKATSLTGW QAGIVTDDMH NQATIQSVDN
     EKFNQLLNDD QIVIVAGFQG VNQAGAITTL GRGGSDTSAV TLAGLLGASE CQIFTDVDGV
     YSCDPRVVES ALKLEHVDFD DMQTMARHGA KVLHEPCVEF AAKYNLDIRV LSSFSPKQGT
     LVTRLQSKKN VCGLALQREL ARLIVNEDKA EQVAMQCQLL GIAVHSQTTK HLIVNNNDVS
     KLLQILSEDV NNVEPISALT IVGAELEGLH LNVLPQLLAK DIKVLDSFRC DRVVKLLLLP
     EHLDRAANFI HAQYIEQSHS VATDKKALIL
//
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