ID AK3_ECOLI Reviewed; 449 AA. AC P08660; Q2M6T0; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 2. DT 16-JUN-2009, entry version 86. DE RecName: Full=Lysine-sensitive aspartokinase 3; DE EC=2.7.2.4; DE AltName: Full=Lysine-sensitive aspartokinase III; DE AltName: Full=Aspartate kinase III; GN Name=lysC; Synonyms=apk; OrderedLocusNames=b4024, JW3984; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=86111734; PubMed=3003049; RA Cassan M., Parsot C., Cohen G.N., Patte J.-C.; RT "Nucleotide sequence of lysC gene encoding the lysine-sensitive RT aspartokinase III of Escherichia coli K12. Evolutionary pathway RT leading to three isofunctional enzymes."; RL J. Biol. Chem. 261:1052-1057(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=94089392; PubMed=8265357; DOI=10.1093/nar/21.23.5408; RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., RA Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the RT region from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. RX MEDLINE=84015362; PubMed=6312411; DOI=10.1093/nar/11.18.6157; RA Cassan M., Ronceray J., Patte J.-C.; RT "Nucleotide sequence of the promoter region of the E. coli lysC RT gene."; RL Nucleic Acids Res. 11:6157-6166(1983). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. CC -!- ENZYME REGULATION: Synthesis and activity are sensitive to lysine, CC which is one of the end metabolites of the aspartic acid family CC branched pathway. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; tetrahydrodipicolinate from L-aspartate: step 1/4. CC -!- SUBUNIT: Homodimer. CC -!- MISCELLANEOUS: Aspartokinases I and II also catalyze the same CC reaction(s). CC -!- SIMILARITY: Belongs to the aspartokinase family. CC -!- SIMILARITY: Contains 1 ACT domain. 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; M11812; AAA24095.1; -; Genomic_DNA. DR EMBL; U00006; AAC43118.1; -; Genomic_DNA. DR EMBL; U00096; AAC76994.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78026.1; -; Genomic_DNA. DR EMBL; X00008; CAA24910.1; ALT_SEQ; Genomic_DNA. DR PIR; G65209; KIECD3. DR RefSeq; AP_004525.1; -. DR RefSeq; NP_418448.1; -. DR PDB; 2J0W; X-ray; 2.50 A; A=1-449. DR PDB; 2J0X; X-ray; 2.80 A; A/B=1-449. DR PDBsum; 2J0W; -. DR PDBsum; 2J0X; -. DR GeneID; 948531; -. DR GenomeReviews; AP009048_GR; JW3984. DR GenomeReviews; U00096_GR; b4024. DR KEGG; ecj:JW3984; -. DR KEGG; eco:b4024; -. DR EchoBASE; EB0545; -. DR EcoGene; EG10550; lysC. DR HOGENOM; P08660; -. DR OMA; P08660; GFIGADE. DR BioCyc; EcoCyc:ASPKINIII-MON; -. DR BioCyc; MetaCyc:ASPKINIII-MON; -. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004072; F:aspartate kinase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR002912; ACT_bd. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kin_reg. DR InterPro; IPR018042; Aspartate_kinase_CS. DR Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 1. DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Complete proteome; KW Kinase; Lysine biosynthesis; Nucleotide-binding; Transferase. FT CHAIN 1 449 Lysine-sensitive aspartokinase 3. FT /FTId=PRO_0000066676. FT DOMAIN 309 386 ACT. FT REGION 1 245 Aspartokinase. FT REGION 246 449 Interface. FT CONFLICT 58 58 G -> C (in Ref. 1; AAA24095). FT CONFLICT 401 401 G -> A (in Ref. 1; AAA24095). FT HELIX 68 82 FT STRAND 87 90 FT HELIX 93 103 FT HELIX 109 119 FT HELIX 122 133 FT TURN 150 152 FT HELIX 161 168 FT STRAND 176 179 FT STRAND 181 186 FT STRAND 190 192 FT STRAND 196 198 FT HELIX 201 212 FT STRAND 216 220 FT STRAND 222 231 FT HELIX 236 245 FT HELIX 250 264 FT STRAND 269 277 SQ SEQUENCE 449 AA; 48532 MW; 5B41CE3A6E4D984B CRC64; MSEIVVSKFG GTSVADFDAM NRSADIVLSD ANVRLVVLSA SAGITNLLVA LAEGLEPGER FEKLDAIRNI QFAILERLRY PNVIREEIER LLENITVLAE AAALATSPAL TDELVSHGEL MSTLLFVEIL RERDVQAQWF DVRKVMRTND RFGRAEPDIA ALAELAALQL LPRLNEGLVI TQGFIGSENK GRTTTLGRGG SDYTAALLAE ALHASRVDIW TDVPGIYTTD PRVVSAAKRI DEIAFAEAAE MATFGAKVLH PATLLPAVRS DIPVFVGSSK DPRAGGTLVC NKTENPPLFR ALALRRNQTL LTLHSLNMLH SRGFLAEVFG ILARHNISVD LITTSEVSVA LTLDTTGSTS TGDTLLTQSL LMELSALCRV EVEEGLALVA LIGNDLSKAC GVGKEVFGVL EPFNIRMICY GASSHNLCFL VPGEDAEQVV QKLHSNLFE //