ID   A0A3V7PJP1_SALET        Unreviewed;       810 AA.
AC   A0A3V7PJP1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   02-OCT-2024, entry version 25.
DE   RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE   Includes:
DE     RecName: Full=Aspartokinase {ECO:0000256|PIRNR:PIRNR000727};
DE              EC=2.7.2.4 {ECO:0000256|PIRNR:PIRNR000727};
DE   Includes:
DE     RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE              EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR000727};
GN   Name=metL {ECO:0000313|EMBL:EBS3854368.1};
GN   Synonyms=metM {ECO:0000313|EMBL:EBS3854368.1};
GN   ORFNames=DPP52_16880 {ECO:0000313|EMBL:EBS3854368.1}, G3331_004045
GN   {ECO:0000313|EMBL:HAE2550171.1};
OS   Salmonella enterica subsp. enterica serovar Javiana.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=363569 {ECO:0000313|EMBL:EBS3854368.1};
RN   [1] {ECO:0000313|EMBL:HAE2550171.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=11-7312 {ECO:0000313|EMBL:HAE2550171.1};
RX   PubMed=30286803; DOI=10.1186/s13059-018-1540-z;
RA   Souvorov A., Agarwala R., Lipman D.J.;
RT   "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL   Genome Biol. 19:153-153(2018).
RN   [2] {ECO:0000313|EMBL:EBS3854368.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=313885 {ECO:0000313|EMBL:EBS3854368.1};
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:HAE2550171.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=11-7312 {ECO:0000313|EMBL:HAE2550171.1};
RG   NCBI Pathogen Detection Project;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional aspartate kinase and homoserine dehydrogenase
CC       that catalyzes the first and the third steps toward the synthesis of
CC       lysine, methionine and threonine from aspartate.
CC       {ECO:0000256|ARBA:ARBA00044938}.
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:0000256|ARBA:ARBA00044882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23777;
CC         Evidence={ECO:0000256|ARBA:ARBA00044882};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC         NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00044923};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15759;
CC         Evidence={ECO:0000256|ARBA:ARBA00044923};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC         NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00044905};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15763;
CC         Evidence={ECO:0000256|ARBA:ARBA00044905};
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000256|ARBA:ARBA00001920};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004766, ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004986, ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005062, ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139,
CC       ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056,
CC       ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007952,
CC       ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase
CC       family. {ECO:0000256|ARBA:ARBA00010046, ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EBS3854368.1}.
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DR   EMBL; AAGVJG010000012; EBS3854368.1; -; Genomic_DNA.
DR   EMBL; DAARIH010000041; HAE2550171.1; -; Genomic_DNA.
DR   RefSeq; WP_000110811.1; NZ_MYCD01000012.1.
DR   AlphaFoldDB; A0A3V7PJP1; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04257; AAK_AK-HSDH; 1.
DR   CDD; cd04892; ACT_AK-like_2; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   Gene3D; 1.20.120.1320; Aspartokinase, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR049638; AK-HD.
DR   InterPro; IPR041743; AK-HSDH_N.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR011147; Bifunc_Aspkin/hSer_DH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00657; asp_kinases; 1.
DR   PANTHER; PTHR43070; -; 1.
DR   PANTHER; PTHR43070:SF5; HOMOSERINE DEHYDROGENASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000727; ThrA; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000727};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:EBS3854368.1};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000727}; Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:EBS3854368.1}.
FT   DOMAIN          12..284
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   DOMAIN          465..600
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          608..803
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
SQ   SEQUENCE   810 AA;  88875 MW;  D823F45FE694D7E1 CRC64;
     MSVIAQAGAK GRQLHKFGGS SLADVKCYLR VAGIMAEYSQ PDDMMVVSAA GSTTNQLISW
     LKLSQTDRLS AHQVLQTLRR YQCDLISGLL PADAADDLTS AFISDLERLA ALLDGGVTDA
     VYAEIVGHGE IWSARLMSAV LNQQGLDAAW LDARAFLRAE RAAQPQVDEG LSYPLLQQLL
     AQHPGKRLVV TGFISRNHDG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP
     RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSD IDLQLRCSYT PDQGSTRIER
     VLASGTGARI VTSHDDICLI EFQVPASQDF RLAHKELDQI LKRAQARPLA VGVHRDRQLL
     QFCYTAEVAD SVLKLLDDVG LPGELRLRQG LALVAMVGAG VTRNPLHCHR FWQQLKGQPV
     EFTWQSEEGI SLVAVLRTGP TESLIQGLHQ SVFRAEKRIG LMLFGKGNIG SRWLELFARE
     QSTLSARTGF EFVLAGVVDS RRSLLNYEGL DASRALAFFD DEAVEQDEES LFLWMRAHPY
     DDLVVLDVTA SEQLADQYLD FASHGFHVIS ANKLAGASAS DKYRQIHDAF EKTGRYWLYN
     ATVGAGLPIN HTVRDLIDSG DTILSISGIF SGTLSWLFLQ FDGTVPFTDL VDQAWQQGLT
     EPDPRVDLSG KDVMRKLVIL AREAGYDIEP DQVRVESLVP AHCEEGSIDH FFENGDALNE
     QMVQRLEAAR ELGLVLRYVA RFDANGKARV GVEAVRPEHP LAALLPCDNV FAIESRWYRD
     NPLVIRGPGA GRDVTAGAIQ SDINRLAQLL
//