AK_PSEFS
ID AK_PSEFS Reviewed; 413 AA.
AC C3JXY0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Aspartate kinase;
DE EC=2.7.2.4 {ECO:0000269|PubMed:4357740, ECO:0000269|PubMed:4357741};
DE AltName: Full=Aspartokinase {ECO:0000303|PubMed:4357740};
GN OrderedLocusNames=PFLU_4747;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=P-14;
RX PubMed=4357740; DOI=10.1016/s0021-9258(19)43166-9;
RA Dungan S.M., Katta P.;
RT "Concerted feedback inhibition. Purification and some properties of
RT aspartokinase from Pseudomonas fluorescens.";
RL J. Biol. Chem. 248:8534-8540(1973).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=P-14;
RX PubMed=4357741; DOI=10.1016/s0021-9258(19)43167-0;
RA Dungan S.M., Datta P.;
RT "Concerted feedback inhibition. Modifier-induced oligomerization of the
RT Pseudomonas fluorescens aspartokinase.";
RL J. Biol. Chem. 248:8541-8546(1973).
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:4357740,
CC ECO:0000269|PubMed:4357741}.
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:4357740, ECO:0000269|PubMed:4357741};
CC -!- ACTIVITY REGULATION: Activated by L-lysine, L-methionine, and L-
CC isoleucine. L-threonine, at low concentrations, is a mild activator and
CC has a weak inhibitory effect only at concentrations over 10 mM.
CC Strongly feedback inhibited by the concerted combination of L-lysine
CC and L-threonine and slightly feedback inhibited by the concerted
CC combination of L-threonine and L-methionine. Activated by the
CC combination of L-methionine and L-lysine, L-methionine and L-isoleucine
CC and L-lysine and L-isoleucine. {ECO:0000269|PubMed:4357740,
CC ECO:0000269|PubMed:4357741}.
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 -!- SUBUNIT: Homotrimer (Probable). In the presence of inhibitory amino
CC acids the Stokes radius of the protein increases, suggesting its
CC oligomeric state may change (PubMed:4357741).
CC {ECO:0000269|PubMed:4357741, ECO:0000305|PubMed:4357740}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR EMBL; AM181176; CAY51568.1; -; Genomic_DNA.
DR RefSeq; WP_010208327.1; NC_012660.1.
DR AlphaFoldDB; C3JXY0; -.
DR SMR; C3JXY0; -.
DR STRING; 294.SRM1_04222; -.
DR PRIDE; C3JXY0; -.
DR EnsemblBacteria; CAY51568; CAY51568; PFLU_4747.
DR GeneID; 45624879; -.
DR KEGG; pfs:PFLU_4747; -.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_3_2_6; -.
DR OMA; DMIVQTI; -.
DR OrthoDB; 1067792at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000002332; 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; 2.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis;
KW Methionine biosynthesis; Nucleotide-binding; Reference proteome; Repeat;
KW Threonine biosynthesis; Transferase.
FT CHAIN 1..413
FT /note="Aspartate kinase"
FT /id="PRO_0000428879"
FT DOMAIN 267..341
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 347..413
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 413 AA; 44532 MW; ED1AFA9F32F4147C CRC64;
MALIVQKFGG TSVGSVERIE QVADKVKKFR DAGDDLVVVL SAMSGETNRL IDLAKAISGD
QQPLPRELDV IVSTGEQVTI ALLAMALNKR GVPAVSYTGS QVRILTDSAH TKARILQIDD
QKIRTDLKAG RVVVVAGFQG VDEQGNITTL GRGGSDTTGV ALAAALKADE CQIYTDVDGV
YTTDPRVVSV AQRLDKITFE EMLEMASLGS KVLQIRAVEF AGKYNVPLRV LHSFKEGPGT
LITIDEEESM EQPIISGIAF NRDEAKLTIR GVPDTPGVAF KILGPISGAN IEVDMIVQNV
SHDNTTDFTF TVHRNEYDAA ERILQNTAKE IGAREVVGDT KIAKVSIVGV GMRSHAGVAS
RMFEALAKES INIQMISTSE IKVSVVIEEK YLELAVRALH TAFELDAPAR QGE
