GenomeNet

Database: UniProt
Entry: Q8XA84_ECO57
LinkDB: Q8XA84_ECO57
Original site: Q8XA84_ECO57 
ID   Q8XA84_ECO57            Unreviewed;       820 AA.
AC   Q8XA84; A0A0H3JC33; Q7AHV0;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   31-JUL-2019, entry version 142.
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:BAB33425.1};
GN   ORFNames=CAM50_0024810 {ECO:0000313|EMBL:QCH85657.1}, ECs_0002
GN   {ECO:0000313|EMBL:BAB33425.1}, FGA21_24025
GN   {ECO:0000313|EMBL:QCV19515.1}, FGA23_24080
GN   {ECO:0000313|EMBL:QCV09471.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33425.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33425.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sakai {ECO:0000313|EMBL:BAB33425.1};
RX   PubMed=10734605; DOI=10.1266/ggs.74.227;
RA   Makino K., Yokoyama K., Kubota Y., Yutsudo C.H., Kimura S.,
RA   Kurokawa K., Ishii K., Hattori M., Tatsuno I., Abe H., Iida T.,
RA   Yamamoto K., Onishi M., Hayashi T., Yasunaga T., Honda T.,
RA   Sasakawa C., Shinagawa H.;
RT   "Complete nucleotide sequence of the prophage VT2-Sakai carrying the
RT   verotoxin 2 genes of the enterohemorrhagic Escherichia coli O157:H7
RT   derived from the Sakai outbreak.";
RL   Genes Genet. Syst. 74:227-239(1999).
RN   [2] {ECO:0000313|EMBL:BAB33425.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sakai {ECO:0000313|EMBL:BAB33425.1};
RX   PubMed=11111050; DOI=10.1016/S0378-1119(00)00416-9;
RA   Yokoyama K., Makino K., Kubota Y., Watanabe M., Kimura S.,
RA   Yutsudo C.H., Kurokawa K., Ishii K., Hattori M., Tatsuno I., Abe H.,
RA   Yoh M., Iida T., Ohnishi M., Hayashi T., Yasunaga T., Honda T.,
RA   Sasakawa C., Shinagawa H.;
RT   "Complete nucleotide sequence of the prophage VT1-Sakai carrying the
RT   Shiga toxin 1 genes of the enterohemorrhagic Escherichia coli O157:H7
RT   strain derived from the Sakai outbreak.";
RL   Gene 258:127-139(2000).
RN   [3] {ECO:0000313|EMBL:BAB33425.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sakai {ECO:0000313|EMBL:BAB33425.1};
RX   PubMed=11108008;
RA   Ohnishi M., Murata T., Nakayama K., Kuhara S., Hattori M.,
RA   Kurokawa K., Yasunaga T., Yokoyama K., Makino K., Shinagawa H.,
RA   Hayashi T.;
RT   "Comparative analysis of the whole set of rRNA operons between an
RT   enterohemorrhagic Escherichia coli O157:H7 Sakai strain and an
RT   Escherichia coli K-12 strain MG1655.";
RL   Syst. Appl. Microbiol. 23:315-324(2000).
RN   [4] {ECO:0000313|EMBL:BAB33425.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB33425.1};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [5] {ECO:0000313|EMBL:QCH85657.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FWSEC0004 {ECO:0000313|EMBL:QCH85657.1};
RA   Tyson S., Peterson C.-L., Olson A., Tyler S., Cabral J., Lynch T.,
RA   Knox N., Van Domselaar G., Graham M.;
RT   "Food and Water Consortium WGS.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:QCV09471.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ECP17-1298 {ECO:0000313|EMBL:QCV09471.1}, and ECP17-46
RC   {ECO:0000313|EMBL:QCV19515.1};
RA   Hoffmann M., Sanchez M., Timme R., Trees E.;
RT   "Gen-FS coordinated proficiency test data for genomic foodborne
RT   pathogen surveillance, 2017 and 2018.";
RL   Submitted (MAY-2019) 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|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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000007; BAB33425.1; -; Genomic_DNA.
DR   EMBL; CP031913; QCH85657.1; -; Genomic_DNA.
DR   EMBL; CP040570; QCV09471.1; -; Genomic_DNA.
DR   EMBL; CP040572; QCV19515.1; -; Genomic_DNA.
DR   RefSeq; NP_308029.1; NC_002695.1.
DR   RefSeq; WP_001264698.1; NZ_SDVX01000001.1.
DR   SMR; Q8XA84; -.
DR   STRING; 155864.EDL933_0002; -.
DR   EnsemblBacteria; AAG54302; AAG54302; Z0002.
DR   EnsemblBacteria; BAB33425; BAB33425; BAB33425.
DR   GeneID; 913388; -.
DR   KEGG; ecs:ECs0002; -.
DR   PATRIC; fig|386585.9.peg.99; -.
DR   eggNOG; ENOG4105CFH; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   eggNOG; COG0527; LUCA.
DR   KO; K12524; -.
DR   BioCyc; ECOO157:THRA-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000000558; 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;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000727};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:BAB33425.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:QCH85657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:QCH85657.1}.
FT   DOMAIN      320    394       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      401    478       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   820 AA;  89079 MW;  BC9FFDFEDAAC1332 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 EDGVCRVKIA EVDGNDPLFK VKNGENALAF
     YSHYYQPLPL VLRGYGAGND VTAAGVFADL LRTLSWKLGV
//
DBGET integrated database retrieval system