ID AK_CHLTR Reviewed; 431 AA. AC O84367; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 16-JUN-2009, entry version 49. DE RecName: Full=Aspartokinase; DE EC=2.7.2.4; DE AltName: Full=Aspartate kinase; GN Name=lysC; OrderedLocusNames=CT_362; OS Chlamydia trachomatis. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx; RX MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., RA Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: RT Chlamydia trachomatis."; RL Science 282:754-759(1998). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; tetrahydrodipicolinate from L-aspartate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 1/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 1/5. 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; AE001273; AAC67958.1; -; Genomic_DNA. DR PIR; G71524; G71524. DR RefSeq; NP_219871.1; -. DR GeneID; 884754; -. DR GenomeReviews; AE001273_GR; CT_362. DR KEGG; ctr:CT362; -. DR HOGENOM; O84367; -. DR OMA; O84367; RERHESI. DR BioCyc; CTRA315277:CT362-MON; -. DR BRENDA; 2.7.2.4; 108. DR GO; GO:0004072; F:aspartate kinase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. 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 TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; KW Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis; KW Nucleotide-binding; Transferase. FT CHAIN 1 431 Aspartokinase. FT /FTId=PRO_0000066675. SQ SEQUENCE 431 AA; 47648 MW; 170F9B7DB1DCC919 CRC64; MLRQETAPLV CKFGGTSVGT AQSIRRVCEI IQEERPSFVV VSAVAGVTDW LEEFCRLPKG KRAALTEKIR ERHESIAKEL GIEVSLAIFW EILEHFEDVE ELFSEDQARI LAIGEDLSST LICSYCCTYV LPLKRLEARQ VILTDSQFLR AVPDLALMQT AWGELALQED TIYLMQGFLG ATSSGKTTVL GRGGSDFSAS LIGELCKARE LRIYTDVCGV HTADPKILKD TQLIDSLTFE EMQELASSGA KVLHQDMLKP CVRAKVPIFV TSTFNVTKEG TWICASLNES TEGPVIKALS LKSNQALWFV EYNSPLVRLE DVLGCVRSLG FVPGVVMAQS LGVYFTIDWE EYPQTITKAL EAFGTVSCEG PLSLVALVGA KLASWSMSRV FEALHRTPVL CWSQTDTVIN LIINKDFGVA VTELLHDCLF K //