ID   AKLYS_PSEU5             Reviewed;         412 AA.
AC   A4VJB4;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Aspartate kinase Ask_LysC;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartokinase;
GN   Name=lysC; Synonyms=ask_lysC; OrderedLocusNames=PST_1370;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
RN   [2]
RP   PROTEIN SEQUENCE OF 248-255, FUNCTION, CATALYTIC ACTIVITY, INDUCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=21725014; DOI=10.1128/jb.00345-11;
RA   Stoveken N., Pittelkow M., Sinner T., Jensen R.A., Heider J., Bremer E.;
RT   "A specialized aspartokinase enhances the biosynthesis of the
RT   osmoprotectants ectoine and hydroxyectoine in Pseudomonas stutzeri A1501.";
RL   J. Bacteriol. 193:4456-4468(2011).
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:21725014}.
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:21725014};
CC   -!- ACTIVITY REGULATION: Allosterically and strongly feedback inhibited by
CC       tryptophan. Addition of lysine alone slightly enhances activity. The
CC       simultaneous addition of lysine and tryptophan leads to very strong
CC       feedback inhibition of the enzyme. The feedback control by tryptophan
CC       is reduced in the presence of the compatible solutes hydroxyectoine or
CC       ectoine. {ECO:0000269|PubMed:21725014}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.8 mM for ATP {ECO:0000269|PubMed:21725014};
CC         KM=21.6 mM for L-aspartate {ECO:0000269|PubMed:21725014};
CC         Vmax=5.1 umol/min/mg enzyme {ECO:0000269|PubMed:21725014};
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   -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR   EMBL; CP000304; ABP79065.1; -; Genomic_DNA.
DR   RefSeq; WP_011912547.1; NC_009434.1.
DR   AlphaFoldDB; A4VJB4; -.
DR   SMR; A4VJB4; -.
DR   STRING; 379731.PST_1370; -.
DR   EnsemblBacteria; ABP79065; ABP79065; PST_1370.
DR   KEGG; psa:PST_1370; -.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_009116_3_2_6; -.
DR   OMA; DMIVQTI; -.
DR   SABIO-RK; A4VJB4; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000000233; 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:0019877; P:diaminopimelate biosynthetic process; 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;
KW   Diaminopimelate biosynthesis; Direct protein sequencing; Kinase;
KW   Lysine biosynthesis; Methionine biosynthesis; Nucleotide-binding;
KW   Reference proteome; Threonine biosynthesis; Transferase.
FT   CHAIN           1..412
FT                   /note="Aspartate kinase Ask_LysC"
FT                   /id="PRO_0000428882"
FT   DOMAIN          265..332
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   412 AA;  44316 MW;  3B299ACBD542B8C8 CRC64;
     MALIVQKFGG TSVGTVERIE QVAEKVKKFR DGGDDIVVVV SAMSGETNRL IDLAKQISEQ
     PVPRELDVMV STGEQVTIAL LAMALIKRGV PAVSYTGNQV RILTDSAHTK ARILQIDAQR
     IQRDIKAGRV VVVAGFQGVD EKGNITTLGR GGSDTTGVAL AAALKADECQ IYTDVDGVYT
     TDPRVVAKAQ RLDKITFEEM LEMASLGSKV LQIRAVEFAG KYSVPLRVLH SFQEGPGTLI
     TLDEEESMEQ PIISGIAFNR DEAKLTIRGV PDTPGVAFKI LGPISAANVE VDMIVQNVAH
     DNTTDFTFTV HRNDYNNALQ VLQGIAAEMG AREAIGDTNI AKVSIVGVGM RSHAGVASRM
     FEALAKENIN IQMISTSEIK VSVVIEEKYL ELAVRALHTA FELDAPAGNT AE