ID   AK_PSEPK                Reviewed;         411 AA.
AC   Q88EI9;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Aspartate kinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartokinase;
GN   OrderedLocusNames=PP_4473;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND INDUCTION.
RX   PubMed=5441401; DOI=10.1016/0005-2744(70)90077-x;
RA   Robert-Gero M., Poiret M., Cohen G.N.;
RT   "The aspartate kinase of Pseudomonas putida. Regulation of synthesis and
RT   activity.";
RL   Biochim. Biophys. Acta 206:17-30(1970).
CC   -!- FUNCTION: Involved in the biosynthesis of L-aspartate-beta-semialdehyde
CC       which is a central intermediate in the biosynthesis of different amino
CC       acids (L-lysine, L-methionine, L-threonine). Catalyzes the
CC       phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-
CC       phospho-L-aspartate. {ECO:0000269|PubMed:5441401}.
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:0000269|PubMed:5441401};
CC   -!- ACTIVITY REGULATION: Allosterically feedback inhibited by L-lysine and
CC       L-threonine individually and also subject to a concerted feedback
CC       inhibition by these amino acids. {ECO:0000269|PubMed:5441401}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.35 uM for ATP {ECO:0000269|PubMed:5441401};
CC         KM=4.8 uM for L-aspartate {ECO:0000269|PubMed:5441401};
CC       pH dependence:
CC         Optimum pH is between 7.9 and 8.4. {ECO:0000269|PubMed:5441401};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Repressed by L-methionine. {ECO:0000269|PubMed:5441401}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN70048.1; -; Genomic_DNA.
DR   RefSeq; NP_746584.1; NC_002947.4.
DR   RefSeq; WP_003254504.1; NC_002947.4.
DR   AlphaFoldDB; Q88EI9; -.
DR   SMR; Q88EI9; -.
DR   STRING; 160488.PP_4473; -.
DR   EnsemblBacteria; AAN70048; AAN70048; PP_4473.
DR   KEGG; ppu:PP_4473; -.
DR   PATRIC; fig|160488.4.peg.4759; -.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_009116_3_2_6; -.
DR   OMA; DMIVQTI; -.
DR   PhylomeDB; Q88EI9; -.
DR   BioCyc; PPUT160488:G1G01-4774-MON; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004072; F:aspartate kinase activity; IDA:UniProtKB.
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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041740; AKii-LysC-BS.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005260; Asp_kin_monofn.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR027795; CASTOR_ACT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF55021; SSF55021; 2.
DR   TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW   Lysine biosynthesis; Methionine biosynthesis; Nucleotide-binding;
KW   Reference proteome; Threonine biosynthesis; Transferase.
FT   CHAIN           1..411
FT                   /note="Aspartate kinase"
FT                   /id="PRO_0000428880"
FT   DOMAIN          265..348
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   411 AA;  44605 MW;  F06EE38BAC0D3F74 CRC64;
     MALIVQKFGG TSVGSIERIE QVAEKVKKHR EAGDDLVVVL SAMSGETNRL IDLAKQITDQ
     PVPRELDVIV STGEQVTIAL LTMALIKRGV PAVSYTGNQV RILTDSSHNK ARILQIDDQK
     IRADLKEGRV VVVAGFQGVD EHGSITTLGR GGSDTTGVAL AAALKADECQ IYTDVDGVYT
     TDPRVVPQAR RLEKITFEEM LEMASLGSKV LQIRSVEFAG KYNVPLRVLH SFKEGPGTLI
     TIDEEESMEQ PIISGIAFNR DEAKLTIRGV PDTPGVAFKI LGPISASNIE VDMIVQNVAH
     DNTTDFTFTV HRNEYEKAQS VLENTAREIG AREVIGDTKI AKVSIVGVGM RSHAGVASCM
     FEALAKESIN IQMISTSEIK VSVVLEEKYL ELAVRALHTA FDLDAPARQG E