ID   A0A5P8YKD6_YERPE        Unreviewed;       819 AA.
AC   A0A5P8YKD6; A0A2S9PLC9; A0A3G5LDP3; A0A6B3T0I3; Q0WJK7;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 21.
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:CAL19138.1};
GN   Synonyms=thrA1 {ECO:0000313|EMBL:CAL19138.1}, thrA2
GN   {ECO:0000313|EMBL:CAL19138.1};
GN   OrderedLocusNames=YPO0459 {ECO:0000313|EMBL:CAL19138.1};
GN   ORFNames=EGX46_22600 {ECO:0000313|EMBL:AYX22224.1};
OS   Yersinia pestis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632 {ECO:0000313|EMBL:CAL19138.1, ECO:0000313|Proteomes:UP000000815};
RN   [1] {ECO:0000313|EMBL:CAL19138.1, ECO:0000313|Proteomes:UP000000815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis {ECO:0000313|Proteomes:UP000000815},
RC   and CO92 {ECO:0000313|EMBL:CAL19138.1};
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Leather S., Karlyshev A.V., Moule S.,
RA   Oyston P.C.F., Quail M., Rutherford K., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2] {ECO:0000313|EMBL:CAL19138.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CO92 {ECO:0000313|EMBL:CAL19138.1};
RX   PubMed=12834539; DOI=10.1186/1471-2180-3-13;
RA   Delihas N.;
RT   "Annotation and evolutionary relationships of a small regulatory RNA gene
RT   micF and its target ompF in Yersinia species.";
RL   BMC Microbiol. 3:13-13(2003).
RN   [3] {ECO:0000313|Proteomes:UP000275238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_601;
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Jaissle J.,
RA   Tallon L., Sadzewicz L., Zhao X., Vavikolanu K., Mehta A., Aluvathingal J.,
RA   Nadendla S., Yan Y., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AYX22224.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_601 {ECO:0000313|EMBL:AYX22224.1};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Jaissle J.,
RA   Tallon L.J., Sadzewicz L., Zhao X., Vavikolanu K., Mehta A.,
RA   Aluvathingal J., Nadendla S., Yan Y., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP033699; AYX22224.1; -; Genomic_DNA.
DR   EMBL; AL590842; CAL19138.1; -; Genomic_DNA.
DR   PIR; AH0056; AH0056.
DR   RefSeq; WP_002209237.1; NZ_WUCM01000002.1.
DR   RefSeq; YP_002345531.1; NC_003143.1.
DR   AlphaFoldDB; A0A5P8YKD6; -.
DR   GeneID; 66842977; -.
DR   KEGG; ype:YPO0459; -.
DR   KEGG; ypj:CH55_2348; -.
DR   KEGG; ypl:CH46_454; -.
DR   KEGG; ypv:BZ15_3111; -.
DR   KEGG; ypw:CH59_1401; -.
DR   PATRIC; fig|214092.21.peg.705; -.
DR   OMA; VTCNKIA; -.
DR   OrthoDB; 9799110at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000275238; Chromosome.
DR   GO; GO:0004072; F:aspartate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009090; P:homoserine biosynthetic process; IBA:GO_Central.
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; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000815};
KW   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   819 AA;  89110 MW;  E8249C805C945285 CRC64;
     MRVLKFGGTS VANAERFMRV ADIIESNARQ GQVATVLSAP AKITNHLVAM IDKMVAGQDI
     SPNISDAERI FAELLRGLAD TQPGFDYDRL KALVGHEFAQ LKHLLHGISL LGQCPDSINA
     SIICRGEKLS IAIMEALFQA KGYHVTVINP VEKLLAQGHY LESTVDITES TRRIGASGIP
     SDHIILMAGF TAGNDKGELV VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRTV
     PDARLLKSMS YQEAMELSYF GAKVLHPRTI APIARFQIPC LIKNTSNPQA PGTLIGGESI
     DEDSPVKGIT NLNNMAMINV SGPGMKGMVG MAARVFAVMS RSGISVVLIT QSSSEYSISF
     CVPQGELLRA RRALEDEFYL ELKDGVLDPL DVMEHLAIIS VVGDGMRTLR GISARFFSAL
     ARANINIIAI AQGSSERSIS VVVNNDAVTT GVRVCHQMLF NTDQVIEVFV IGVGGVGGAL
     IEQIYRQQPW LKQRHIDLRV CGIANSKAML TNVHGIALDN WRQELAEVQE PFNLSRLIRL
     VKEYHLLNPV IVDCTSSQAV ADQYADFLTD GFHVVTPNKK ANTSSMNYYR QMRAAATKSC
     RKFLYDTNVG AGLPVIENLQ NLLNAGDELM RFTGILSGSL SFIFGKLDEG MSLSEATRQA
     KALGYTEPDP RDDLSGMDVA RKLLILAREA GYKLELADIE VESVLPASFD ASGDVDTFLA
     RLPSLDAEFT RLVANAAEQG KVLRYVGVIE DGRCKVRMEA VDGNDPLYKV KNGENALAFY
     TRYYQPIPLV LRGYGAGNDV TAAGVFADLL RTLSWKLGV
//