ID AKLYS_STUS1 Reviewed; 412 AA.
AC A4VJB4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
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 Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Stutzerimonas.
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 KEGG; psa:PST_1370; -.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_3_2_6; -.
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 CDD; cd04923; ACT_AK-LysC-DapG-like_2; 1.
DR CDD; cd04913; ACT_AKii-LysC-BS-like_1; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.30.2130.10; VC0802-like; 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 NCBIfam; TIGR00656; asp_kin_monofn; 1.
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 Pfam; PF01842; ACT; 1.
DR Pfam; PF13840; ACT_7; 1.
DR PIRSF; PIRSF000726; Asp_kin; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 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
//
