ID   A0A3V7PJP1_SALET        Unreviewed;       810 AA.
AC   A0A3V7PJP1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   12-AUG-2020, entry version 8.
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=C7S57_21015 {ECO:0000313|EMBL:EAA8831237.1}, DAC29_21870
GN   {ECO:0000313|EMBL:ECS8567283.1}, DPP52_16880
GN   {ECO:0000313|EMBL:EBS3854368.1}, DQK05_10770
GN   {ECO:0000313|EMBL:EBW8004562.1}, DS608_03790
GN   {ECO:0000313|EMBL:EBS3546838.1}, E0S35_14545
GN   {ECO:0000313|EMBL:ECF0700486.1}, E1K69_18055
GN   {ECO:0000313|EMBL:ECF1873541.1}, EWZ46_17175
GN   {ECO:0000313|EMBL:ECE9222769.1}, EZ740_16090
GN   {ECO:0000313|EMBL:ECB6142602.1};
OS   Salmonella enterica subsp. enterica serovar Javiana.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=363569 {ECO:0000313|EMBL:EAA8831237.1};
RN   [1] {ECO:0000313|EMBL:EAA8831237.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDA00012733 {ECO:0000313|EMBL:EAA8831237.1};
RG   GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ECS8567283.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PNUSAS037112 {ECO:0000313|EMBL:ECS8567283.1};
RG   PulseNet: The National Subtyping Network for Foodborne Disease Surveillance;
RA   Tarr C.L., Trees E., Katz L.S., Carleton-Romer H.A., Stroika S.,
RA   Kucerova Z., Roache K.F., Sabol A.L., Besser J., Gerner-Smidt P.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EBS3546838.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=164838 {ECO:0000313|EMBL:EBS3546838.1}, 240207
RC   {ECO:0000313|EMBL:ECF1873541.1}, 313885
RC   {ECO:0000313|EMBL:EBS3854368.1}, 315624
RC   {ECO:0000313|EMBL:ECF0700486.1}, 352820
RC   {ECO:0000313|EMBL:ECB6142602.1}, 435450
RC   {ECO:0000313|EMBL:ECE9222769.1}, and 511866
RC   {ECO:0000313|EMBL:EBW8004562.1};
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:ARBA00000709,
CC         ECO:0000256|PIRNR:PIRNR000727};
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:ARBA00001406};
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:ARBA00000116,
CC         ECO:0000256|PIRNR:PIRNR000727};
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:EAA8831237.1}.
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DR   EMBL; AAACWO010000009; EAA8831237.1; -; Genomic_DNA.
DR   EMBL; AAGVFP010000005; EBS3546838.1; -; Genomic_DNA.
DR   EMBL; AAGVJG010000012; EBS3854368.1; -; Genomic_DNA.
DR   EMBL; AAHJGV010000016; EBW8004562.1; -; Genomic_DNA.
DR   EMBL; AAHYDB010000012; ECB6142602.1; -; Genomic_DNA.
DR   EMBL; AAIJNC010000010; ECE9222769.1; -; Genomic_DNA.
DR   EMBL; AAIJZK010000010; ECF0700486.1; -; Genomic_DNA.
DR   EMBL; AAIKIY010000015; ECF1873541.1; -; Genomic_DNA.
DR   EMBL; AAKKYF010000013; ECS8567283.1; -; Genomic_DNA.
DR   RefSeq; WP_000110811.1; NZ_MYCD01000012.1.
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   Gene3D; 1.20.120.1320; -; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
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_aspartokin/hSer_DH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR000727};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:EAA8831237.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:EBS3854368.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:EBS3854368.1}.
FT   DOMAIN          12..284
FT                   /note="AA_kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   DOMAIN          465..600
FT                   /note="NAD_binding_3"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          608..803
FT                   /note="Homoserine_dh"
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
//