ID   AKECT_PSEU5             Reviewed;         476 AA.
AC   A4VFY3;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Aspartate kinase Ask_Ect;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartokinase;
GN   Name=ask; Synonyms=ask_ect; OrderedLocusNames=PST_0177;
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   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   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-
CC       semialdehyde, which is an intermediate in the biosynthesis of ectoine,
CC       a highly soluble organic osmolyte, called compatible solute. Ectoine is
CC       used to avoid excessive water efflux, plasmolysis, molecular crowding
CC       of the cytoplasm, and cessation of growth in high salinity
CC       environments. Catalyzes the phosphorylation of the beta-carboxyl group
CC       of L-aspartate to yield 4-phospho-L-aspartate.
CC       {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. The presence of either 650 mM NaCl or KCl reduces the
CC       inhibition by tryptophan. {ECO:0000269|PubMed:21725014}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.3 mM for ATP {ECO:0000269|PubMed:21725014};
CC         KM=29.7 mM for L-aspartate {ECO:0000269|PubMed:21725014};
CC         Vmax=6.9 umol/min/mg enzyme {ECO:0000269|PubMed:21725014};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21725014}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Induced in response to osmotic stress.
CC       {ECO:0000269|PubMed:21725014}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP77884.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000304; ABP77884.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_013981377.1; NC_009434.1.
DR   AlphaFoldDB; A4VFY3; -.
DR   SMR; A4VFY3; -.
DR   STRING; 379731.PST_0177; -.
DR   EnsemblBacteria; ABP77884; ABP77884; PST_0177.
DR   GeneID; 66819450; -.
DR   KEGG; psa:PST_0177; -.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_047213_0_0_6; -.
DR   SABIO-RK; A4VFY3; -.
DR   UniPathway; UPA00067; -.
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:0019491; P:ectoine biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR027795; CASTOR_ACT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..476
FT                   /note="Aspartate kinase Ask_Ect"
FT                   /id="PRO_0000428881"
FT   DOMAIN          405..476
FT                   /note="ACT"
SQ   SEQUENCE   476 AA;  52466 MW;  220FD75C1C4A9AFB CRC64;
     MHTVEKIGGT SMSRFEEVLD NIFIGRREGA ALYQRIFVVS AYSGMTNLLL EHKKTGEPGV
     YQRFADAQSE GAWREALEGV RQRMLAKNAE LFSSEYELHA ANQFINSRID DASECMHSLQ
     KLCAYGHFQL SEHLMKVREM LASLGEAHSA FNSVLALKQR GVNARLADLT GWQQEAPLPF
     EEMISSHFAG FDFSRELVVA TGYTHCAEGL MNTFDRGYSE ITFAQIAAAT GAREAIIHKE
     FHLSSADPNL VGADKVVTIG RTNYDVADQL SNLGMEAIHP RAAKTLRRAG VELRIKNAFE
     PEHGGTLISQ DYKSEKPCVE IIAGRKDVFG IEVFDQDMLG DIGYDMEISK LLKQLKLYVV
     NKDSDANSIT YYASGSRKLI NRAARLIEEQ YPAAEVTVHN LAIVSAIGSD LKVKGILAKT
     VAALAEAGIS IQAIHQSIRQ VEMQCVVNEE DYDAAIAALH RALIEPENHG DVIAAA