ID   Q8Z9R7_SALTI            Unreviewed;       820 AA.
AC   Q8Z9R7; A0A0C9EHY8; A0A3Y9LNU7; Q7CBW4;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 167.
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=thrA {ECO:0000313|EMBL:CAD01155.1};
GN   OrderedLocusNames=STY0002 {ECO:0000313|EMBL:CAD01155.1}, t0002
GN   {ECO:0000313|EMBL:AAO67736.1};
GN   ORFNames=CAJ76_03390 {ECO:0000313|EMBL:EDG8855988.1}, CAJ80_14445
GN   {ECO:0000313|EMBL:EDG8902601.1}, CAJ85_01460
GN   {ECO:0000313|EMBL:EDG8891190.1}, CAL67_16215
GN   {ECO:0000313|EMBL:EDG8934182.1}, CB224_16085
GN   {ECO:0000313|EMBL:EDH5802128.1}, CC884_12335
GN   {ECO:0000313|EMBL:EDI0958554.1}, CC972_03355
GN   {ECO:0000313|EMBL:EDI1137775.1}, D4Z37_17665
GN   {ECO:0000313|EMBL:EBS6527628.1}, D6Q30_08350
GN   {ECO:0000313|EMBL:EBS1098356.1}, DKA88_01730
GN   {ECO:0000313|EMBL:EBW2551362.1}, DNM71_08210
GN   {ECO:0000313|EMBL:EBV0720288.1}, DNV09_12690
GN   {ECO:0000313|EMBL:EBV1033518.1}, DS261_16925
GN   {ECO:0000313|EMBL:EBX7035091.1}, DUQ91_16510
GN   {ECO:0000313|EMBL:EBS0138401.1}, DUV11_16175
GN   {ECO:0000313|EMBL:EBS5365525.1}, DVG36_15140
GN   {ECO:0000313|EMBL:EBY2834950.1}, EBC38_13555
GN   {ECO:0000313|EMBL:EBZ4082832.1}, EID90_13525
GN   {ECO:0000313|EMBL:EBZ9855873.1}, ELQ62_15140
GN   {ECO:0000313|EMBL:ECA4925236.1}, EU445_15970
GN   {ECO:0000313|EMBL:ECB1385967.1}, EVI00_16015
GN   {ECO:0000313|EMBL:ECB2194196.1}, F9R11_17095
GN   {ECO:0000313|EMBL:EDB3137210.1}, F9Y21_16445
GN   {ECO:0000313|EMBL:EDB3627710.1}, FI137_10210
GN   {ECO:0000313|EMBL:EBG5394235.1}, G2227_04550
GN   {ECO:0000313|EMBL:HAE0480196.1}, G2244_09015
GN   {ECO:0000313|EMBL:HAE0416734.1}, G3982_003970
GN   {ECO:0000313|EMBL:HAE3630232.1}, G3V49_001120
GN   {ECO:0000313|EMBL:HAE1996219.1}, G4I71_001524
GN   {ECO:0000313|EMBL:HAE6054326.1}, G4L28_000908
GN   {ECO:0000313|EMBL:HAE6906362.1}, G4P30_001688
GN   {ECO:0000313|EMBL:HAE7598332.1}, G4Y41_003261
GN   {ECO:0000313|EMBL:HAE9016546.1}, G4Y55_000903
GN   {ECO:0000313|EMBL:HAE9578217.1}, G9264_001456
GN   {ECO:0000313|EMBL:HAF7398051.1}, G9C68_001876
GN   {ECO:0000313|EMBL:HAF0686332.1}, G9X37_003439
GN   {ECO:0000313|EMBL:HAF7362788.1}, GDI29_05915
GN   {ECO:0000313|EMBL:EDH3994635.1}, GND71_003213
GN   {ECO:0000313|EMBL:HAE7811301.1}, K3U68_00010
GN   {ECO:0000313|EMBL:QZA29695.1}, ZZ17_13935
GN   {ECO:0000313|EMBL:ECV8216763.1};
OS   Salmonella typhi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370 {ECO:0000313|EMBL:CAD01155.1, ECO:0000313|Proteomes:UP000000541};
RN   [1] {ECO:0000313|EMBL:CAD01155.1, ECO:0000313|Proteomes:UP000000541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18 {ECO:0000313|EMBL:CAD01155.1,
RC   ECO:0000313|Proteomes:UP000000541};
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.,
RA   Rutherford K., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2] {ECO:0000313|EMBL:AAO67736.1, ECO:0000313|Proteomes:UP000002670}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2 {ECO:0000313|Proteomes:UP000002670}, and Ty2
RC   {ECO:0000313|EMBL:AAO67736.1};
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.R., Plunkett G.III., Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
RN   [3] {ECO:0000313|EMBL:HAE0416734.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=09-1703 {ECO:0000313|EMBL:HAE3630232.1}, 09-1978
RC   {ECO:0000313|EMBL:HAE6054326.1}, 09-1979
RC   {ECO:0000313|EMBL:HAE7598332.1}, 10-1436
RC   {ECO:0000313|EMBL:HAE1996219.1}, 11-2088
RC   {ECO:0000313|EMBL:HAE6906362.1}, 12-0098
RC   {ECO:0000313|EMBL:HAF7398051.1}, 12-0437
RC   {ECO:0000313|EMBL:HAF7362788.1}, 12-2005
RC   {ECO:0000313|EMBL:HAE9016546.1}, 13-0747
RC   {ECO:0000313|EMBL:HAF0686332.1}, 13-7562
RC   {ECO:0000313|EMBL:HAE9578217.1}, IP E.88.374
RC   {ECO:0000313|EMBL:HAE7811301.1},
RC   Sam_1c96eabc-5ba9-4785-8bb4-b62bc64a6574
RC   {ECO:0000313|EMBL:HAE0416734.1}, and
RC   Sam_2e1fd039-ec06-4964-b74e-443d7665d7a0
RC   {ECO:0000313|EMBL:HAE0480196.1};
RX   PubMed=30286803;
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   [4] {ECO:0000313|EMBL:EBS0138401.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=116585 {ECO:0000313|EMBL:EDG8934182.1}, 132015
RC   {ECO:0000313|EMBL:EDG8902601.1}, 14549
RC   {ECO:0000313|EMBL:ECV8216763.1}, 186520
RC   {ECO:0000313|EMBL:EDG8891190.1}, 189261
RC   {ECO:0000313|EMBL:EDG8855988.1}, 257355
RC   {ECO:0000313|EMBL:EBW2551362.1}, 338438
RC   {ECO:0000313|EMBL:EDI1137775.1}, 339489
RC   {ECO:0000313|EMBL:EDI0958554.1}, 365365
RC   {ECO:0000313|EMBL:EDH5802128.1}, 524805
RC   {ECO:0000313|EMBL:EBY2834950.1}, 531284
RC   {ECO:0000313|EMBL:EBV1033518.1}, 539099
RC   {ECO:0000313|EMBL:EBV0720288.1}, 550116
RC   {ECO:0000313|EMBL:EBX7035091.1}, 550675
RC   {ECO:0000313|EMBL:ECB1385967.1}, 550679
RC   {ECO:0000313|EMBL:EBS5365525.1}, 568336
RC   {ECO:0000313|EMBL:EBS0138401.1}, 588927
RC   {ECO:0000313|EMBL:EBS6527628.1}, 606246
RC   {ECO:0000313|EMBL:EBS1098356.1}, 619925
RC   {ECO:0000313|EMBL:EBZ4082832.1}, 643219
RC   {ECO:0000313|EMBL:EBZ9855873.1}, 656788
RC   {ECO:0000313|EMBL:ECA4925236.1}, 673629
RC   {ECO:0000313|EMBL:ECB2194196.1}, 731618
RC   {ECO:0000313|EMBL:EBG5394235.1}, 814947
RC   {ECO:0000313|EMBL:EDB3137210.1}, 815592
RC   {ECO:0000313|EMBL:EDB3627710.1}, and 824494
RC   {ECO:0000313|EMBL:EDH3994635.1};
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.
RN   [5] {ECO:0000313|EMBL:HAE1996219.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=09-1703 {ECO:0000313|EMBL:HAE3630232.1}, 09-1978
RC   {ECO:0000313|EMBL:HAE6054326.1}, 09-1979
RC   {ECO:0000313|EMBL:HAE7598332.1}, 10-1436
RC   {ECO:0000313|EMBL:HAE1996219.1}, 11-2088
RC   {ECO:0000313|EMBL:HAE6906362.1}, 12-0098
RC   {ECO:0000313|EMBL:HAF7398051.1}, 12-0437
RC   {ECO:0000313|EMBL:HAF7362788.1}, 12-2005
RC   {ECO:0000313|EMBL:HAE9016546.1}, 13-0747
RC   {ECO:0000313|EMBL:HAF0686332.1}, 13-7562
RC   {ECO:0000313|EMBL:HAE9578217.1}, IP E.88.374
RC   {ECO:0000313|EMBL:HAE7811301.1},
RC   Sam_1c96eabc-5ba9-4785-8bb4-b62bc64a6574
RC   {ECO:0000313|EMBL:HAE0416734.1}, and
RC   Sam_2e1fd039-ec06-4964-b74e-443d7665d7a0
RC   {ECO:0000313|EMBL:HAE0480196.1};
RG   NCBI Pathogen Detection Project;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:QZA29695.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ISP2825 {ECO:0000313|EMBL:QZA29695.1};
RA   Lee G.Y., Song J.;
RT   "Complete Genome Sequence of Salmonella enterica Serovar Typhi Strain
RT   ISP2825.";
RL   Submitted (AUG-2021) 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}.
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DR   EMBL; AE014613; AAO67736.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD01155.1; -; Genomic_DNA.
DR   EMBL; AAFJDY010000013; EBG5394235.1; -; Genomic_DNA.
DR   EMBL; AAGUIA010000018; EBS0138401.1; -; Genomic_DNA.
DR   EMBL; AAGULE010000012; EBS1098356.1; -; Genomic_DNA.
DR   EMBL; AAGVVD010000018; EBS5365525.1; -; Genomic_DNA.
DR   EMBL; AAGWES010000021; EBS6527628.1; -; Genomic_DNA.
DR   EMBL; AAHEBT010000007; EBV0720288.1; -; Genomic_DNA.
DR   EMBL; AAHEEH010000017; EBV1033518.1; -; Genomic_DNA.
DR   EMBL; AAHHUX010000002; EBW2551362.1; -; Genomic_DNA.
DR   EMBL; AAHLZU010000019; EBX7035091.1; -; Genomic_DNA.
DR   EMBL; AAHNRO010000018; EBY2834950.1; -; Genomic_DNA.
DR   EMBL; AAHRAJ010000015; EBZ4082832.1; -; Genomic_DNA.
DR   EMBL; AAHSWZ010000017; EBZ9855873.1; -; Genomic_DNA.
DR   EMBL; AAHUNO010000020; ECA4925236.1; -; Genomic_DNA.
DR   EMBL; AAHWPO010000018; ECB1385967.1; -; Genomic_DNA.
DR   EMBL; AAHWWI010000017; ECB2194196.1; -; Genomic_DNA.
DR   EMBL; AAKUKE010000019; ECV8216763.1; -; Genomic_DNA.
DR   EMBL; AALNBT010000018; EDB3137210.1; -; Genomic_DNA.
DR   EMBL; AALNGB010000018; EDB3627710.1; -; Genomic_DNA.
DR   EMBL; AAMFQS010000003; EDG8855988.1; -; Genomic_DNA.
DR   EMBL; AAMFQZ010000002; EDG8891190.1; -; Genomic_DNA.
DR   EMBL; AAMFRD010000025; EDG8902601.1; -; Genomic_DNA.
DR   EMBL; AAMFRJ010000050; EDG8934182.1; -; Genomic_DNA.
DR   EMBL; AAMHNJ010000004; EDH3994635.1; -; Genomic_DNA.
DR   EMBL; AAMICL010000019; EDH5802128.1; -; Genomic_DNA.
DR   EMBL; AAMJUX010000015; EDI0958554.1; -; Genomic_DNA.
DR   EMBL; AAMJWL010000002; EDI1137775.1; -; Genomic_DNA.
DR   EMBL; DAAQQG010000008; HAE0416734.1; -; Genomic_DNA.
DR   EMBL; DAAQQU010000003; HAE0480196.1; -; Genomic_DNA.
DR   EMBL; DAARDQ010000010; HAE1996219.1; -; Genomic_DNA.
DR   EMBL; DAARRK010000050; HAE3630232.1; -; Genomic_DNA.
DR   EMBL; DAASLV010000012; HAE6054326.1; -; Genomic_DNA.
DR   EMBL; DAASSY010000006; HAE6906362.1; -; Genomic_DNA.
DR   EMBL; DAASYX010000010; HAE7598332.1; -; Genomic_DNA.
DR   EMBL; DAATAS010000018; HAE7811301.1; -; Genomic_DNA.
DR   EMBL; DAATOU010000060; HAE9016546.1; -; Genomic_DNA.
DR   EMBL; DAATPQ010000003; HAE9578217.1; -; Genomic_DNA.
DR   EMBL; DAATYW010000008; HAF0686332.1; -; Genomic_DNA.
DR   EMBL; DAAWCE010000087; HAF7362788.1; -; Genomic_DNA.
DR   EMBL; DAAWDS010000011; HAF7398051.1; -; Genomic_DNA.
DR   EMBL; CP080960; QZA29695.1; -; Genomic_DNA.
DR   RefSeq; NP_454612.1; NC_003198.1.
DR   RefSeq; WP_001264731.1; NZ_WSUR01000014.1.
DR   AlphaFoldDB; Q8Z9R7; -.
DR   SMR; Q8Z9R7; -.
DR   STRING; 220341.gene:17584057; -.
DR   KEGG; stt:t0002; -.
DR   KEGG; sty:STY0002; -.
DR   PATRIC; fig|220341.7.peg.1; -.
DR   eggNOG; COG0460; Bacteria.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_009116_7_1_6; -.
DR   OMA; VTCNKIA; -.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04257; AAK_AK-HSDH; 1.
DR   CDD; cd04921; ACT_AKi-HSDH-ThrA-like_1; 1.
DR   CDD; cd04922; ACT_AKi-HSDH-ThrA_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   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; 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_aspartokin/hSer_DH.
DR   InterPro; IPR027795; CASTOR_ACT_dom.
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:SF3; HOMOSERINE DEHYDROGENASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF13840; ACT_7; 2.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000727; ThrA; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
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; PS51671; ACT; 2.
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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000727};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000727};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000727}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000727}.
FT   DOMAIN          320..394
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          401..478
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   820 AA;  88712 MW;  ED6CDB2F6F01AC67 CRC64;
     MRVLKFGGTS VANAERFLRV ADILESNSRQ GQVATVLSAP AKITNHLVAM IEKTIGGQDA
     LPNISDAERI FSDLLAGLAS AQPGFPLARL KMVVEQEFAQ IKHVLHGISL LGQCPDSINA
     ALICRGEKMS IAIMAGLLEA RGHRVTVIDP VEKLLAVGHY LESTVDIAES TRRIAASQIP
     ADHMILMAGF TAGNEKGELV VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRQV
     PDARLLKSMS YQEAMELSYF GAKVLHPRTI TPIAQFQIPC LIKNTGNPQA PGTLIGASSD
     DDNLPVKGIS NLNNMAMFSV SGPGMKGMIG MAARVFAAMS RAGISVVLIT QSSSEYSISF
     CVPQSDCARA RRAMQDEFYL ELKEGLLEPL AVTERLAIIS VVGDGMRTLR GISAKFFAAL
     ARANINIVAI AQGSSERSIS VVVNNDDATT GVRVTHQMLF NTDQVIEVFV IGVGGVGGAL
     LEQLKRQQTW LKNKHIDLRV CGVANSKALL TNVHGLNLDN WQAELAQANA PFNLGRLIRL
     VKEYHLLNPV IVDCTSSQAV ADQYADFLRE GFHVVTPNKK ANTSSMDYYH QLRFAAAQSR
     RKFLYDTNVG AGLPVIENLQ NLLNAGDELQ KFSGILSGSL SFIFGKLEEG MSLSQATALA
     REMGYTEPDP RDDLSGMDVA RKLLILARET GRELELSDIV IEPVLPDEFD ASGDVTAFMA
     HLPQLDDAFA ARVAKARDEG KVLRYVGNIE EDGVCRVKIA EVDGNDPLFK VKNGENALAF
     YSHYYQPLPL VLRGYGAGND VTAAGVFADL LRTLSWKLGV
//