(data stored in SCRATCH zone)

SWISSPROT: C8U177_ECO10

ID   C8U177_ECO10            Unreviewed;       820 AA.
AC   C8U177;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
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:BAI28885.1};
GN   OrderedLocusNames=ECO103_0002 {ECO:0000313|EMBL:BAI28885.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28885.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28885.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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|PIRNR:PIRNR000727};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={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|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       aspartokinase family. {ECO:0000256|PIRNR:PIRNR000727}.
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DR   EMBL; AP010958; BAI28885.1; -; Genomic_DNA.
DR   RefSeq; WP_001264697.1; NC_013353.1.
DR   SMR; C8U177; -.
DR   EnsemblBacteria; BAI28885; BAI28885; ECO103_0002.
DR   KEGG; eoh:ECO103_0002; -.
DR   HOGENOM; HOG000271593; -.
DR   KO; K12524; -.
DR   OMA; CNKIACS; -.
DR   BioCyc; ECOL585395:ECO103_RS00010-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000000959; 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:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04257; AAK_AK-HSDH; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR002912; ACT_dom.
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   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF13840; ACT_7; 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; PS51671; ACT; 2.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U177.
DR   SWISS-2DPAGE; C8U177.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000727};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:BAI28885.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727}.
FT   DOMAIN      320    394       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      401    478       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   820 AA;  89051 MW;  BC9FE2F1CAB31C22 CRC64;
     MRVLKFGGTS VANAERFLRV ADILESNARQ GQVATVLSAP AKITNHLVAM IEKTISGQDA
     LPNISDAERI FAELLTGLAA AQPGFPLAQL KTFVDQEFAQ IKHVLHGISL LGQCPDSINA
     ALICRGEKMS IAIMAGVLEA RGHNVTVIDP VEKLLAVGHY LESTVDIAES TRRIAASRIP
     ADHMVLMAGF TAGNEKGELV VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRQV
     PDARLLKSMS YQEAMELSYF GAKVLHPRTI TPIAQFQIPC LIKNTGNPQA PGTLIGASRD
     EDELPVKGIS NLNNMAMFSV SGPGMKGMVG MAARVFAAMS RARISVVLIT QSSSEYSISF
     CVPQSDCVRA ERAMQEEFYL ELKEGLLEPL AVTERLAIIS VVGDGMRTLR GISAKFFAAL
     ARANINIVAI AQGSSERSIS VVVNNDDATT GVRVTHQMLF NTDQVIEVFV IGVGGVGGAL
     LEQLKRQQSW LKNKHIDLRV CGVANSKALL TNVHGLNLEN WQEELAQAKE PFNLGRLIRL
     VKEYHLLNPV IVDCTSSQAV ADQYADFLRE GFHVVTPNKK ANTSSMDYYH LLRHAAEKSR
     RKFLYDTNVG AGLPVIENLQ NLLNAGDELM KFSGILSGSL SYIFGKLDEG MSFSEATTLA
     REMGYTEPDP RDDLSGMDVA RKLLILARET GRELELADIE IEPVLPAEFN AEGDVAAFMA
     NLSQLDDLFA ARVAKARDEG KVLRYVGNID EDGACRVKIA EVDGNDPLFK VKNGENALAF
     YSHYYQPLPL VLRGYGAGND VTAAGVFADL LRTLSWKLGV
//

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