ID Q8Z1U8_SALTI Unreviewed; 449 AA.
AC Q8Z1U8; Q7C5P6;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 01-MAY-2013, entry version 80.
DE RecName: Full=Aspartokinase;
DE EC=2.7.2.4;
GN Name=lysC; OrderedLocusNames=STY4416, t4126;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
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.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA Whitehead S., Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella
RT enterica serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2, and Ty2;
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.,
RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT and CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC aspartate.
CC -!- SIMILARITY: Belongs to the aspartokinase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AE014613; AAO71590.1; -; Genomic_DNA.
DR EMBL; AL627282; CAD09204.1; -; Genomic_DNA.
DR RefSeq; NP_807730.1; NC_004631.1.
DR SMR; Q8Z1U8; 3-449.
DR STRING; 220341.STY4416; -.
DR EnsemblBacteria; AAO71590; AAO71590; t4126.
DR EnsemblBacteria; CAD09204; CAD09204; CAD09204.
DR GeneID; 1068481; -.
DR KEGG; stt:t4126; -.
DR PATRIC; 18547073; VBISalEnt120419_4516.
DR HOGENOM; HOG000293094; -.
DR KO; K00928; -.
DR OMA; IRLICYG; -.
DR ProtClustDB; PRK09084; -.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR Gene3D; 3.40.1160.10; -; 2.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005260; Asp_kin_monofn.
DR InterPro; IPR001341; Asp_kinase_dom.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01842; ACT; 1.
DR PIRSF; PIRSF000726; Asp_kin; 1.
DR SUPFAM; SSF53633; Aa_kinase; 1.
DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR TIGRFAMs; TIGR00657; asp_kinases; 1.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Kinase; Transferase.
SQ SEQUENCE 449 AA; 48595 MW; 2B485698881A09A8 CRC64;
MTEIVVSKFG GTSVADFDAM NRSADIVLSD ANVRLVVLSA SAGITNLLVA LAEGMEPGER
FATLDAIRKI QFDILDRLRH PNVIREEIER LLENITILAE AASLATSAAL TDELVSHGEL
MSTLLFVEIL RERDVQAHWF DVRKVMRTSD RFGRAEPDVA ALAELAAQQL LPRLSETLVI
TQGFIGSESK GRTTTLGRGG SDYTAALLAE ALHAARVDIW TDVPGIYTTD PRVVPVAQRI
DEIDFEEAAE MATFGAKVLH PATLLPAVRS DIPVFVGSSK DPQAGGTLVC NKTQNPPLFR
ALALRRNQTL LTLHSLNMLH SRGFLAEVFG ILARHNISVD LITTSEVSVA LTLDTTGSTS
TGDTLLTQSL LMELSALCRV EVEEGLALVA LIGNNLSKAC GVGKEVFGVL EPFNIRMICY
GASSHNLCFL VPGDDAEKVV QKLHQNLFE
//
