ID AK_RICPR Reviewed; 446 AA. AC Q9ZCI7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 02-SEP-2026, entry version 127. DE RecName: Full=Aspartokinase; DE EC=2.7.2.4; DE AltName: Full=Aspartate kinase; GN Name=lysC; OrderedLocusNames=RP753; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). RN [2] RP DOMAIN RPE1. RX PubMed=11030655; DOI=10.1126/science.290.5490.347; RA Ogata H., Audic S., Barbe V., Artiguenave F., Fournier P.-E., Raoult D., RA Claverie J.-M.; RT "Selfish DNA in protein-coding genes of Rickettsia."; RL Science 290:347-350(2000). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate + ATP = 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 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-homoserine from L-aspartate: step 1/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 1/5. CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}. 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; AJ235273; CAA15181.1; -; Genomic_DNA. DR PIR; E71635; E71635. DR RefSeq; WP_004596996.1; NC_000963.1. DR AlphaFoldDB; Q9ZCI7; -. DR SMR; Q9ZCI7; -. DR STRING; 272947.gene:17555823; -. DR EnsemblBacteria; CAA15181; CAA15181; CAA15181. DR GeneID; 57569875; -. DR KEGG; rpr:RP753; -. DR PATRIC; fig|272947.5.peg.787; -. DR eggNOG; COG0527; Bacteria. DR HOGENOM; CLU_009116_3_2_5; -. DR OrthoDB; 9799110at2; -. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00461. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000002480; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0009090; P:L-homoserine biosynthetic process; IEA:TreeGrafter. DR GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd04261; AAK_AKii-LysC-BS; 1. DR FunFam; 3.40.1160.10:FF:000002; Aspartokinase; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1. DR Gene3D; 3.30.2130.10; VC0802-like; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR045865; ACT-like_dom_sf. DR InterPro; IPR054352; ACT_Aspartokinase. DR InterPro; IPR041740; AKii-LysC-BS. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kinase. DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR NCBIfam; TIGR00657; asp_kinases; 1. DR NCBIfam; NF005158; PRK06635.2-2; 1. DR PANTHER; PTHR21499; ASPARTATE KINASE; 1. DR PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF22468; ACT_9; 1. DR PIRSF; PIRSF000726; Asp_kin; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF55021; ACT-like; 1. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Diaminopimelate biosynthesis; Kinase; KW Lysine biosynthesis; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..446 FT /note="Aspartokinase" FT /id="PRO_0000066680" FT DOMAIN 250..294 FT /note="RPE1 insert" SQ SEQUENCE 446 AA; 49773 MW; 76E118506A4E3D86 CRC64; MALIIQKFGG TSVANVERIK KLVPIIKAEI AKNNQVIVVV SAMAGVTNQL VTLCNEVSSL NKRSQFAEYD VALSSGEIVT ASLLALALQE EEIKAQSLLA WQLPIRTNNN YSKALVEFIT TDLLEKYLQL KIIPIIAGFQ GINKSNRVTT LGRGGSDTTA ALIAAAMKAD RCDIYTDVDG IFTADPRIIP NAKRIKEIDF LEMLELASSG AKVLHPRAVE LVMRYKIDMR VLSTFSPNTE GTLITSKDTI PLVKSTYMEE SALNTKHSTK IDIPEDASGS TYKLPIELAL QNRYNMENCV VRCITSNKNL LKVSVNSISL SFLQVANMIT YNNNCIEFMQ EIENNIEYNF ITNLTDKNNL QTLLTKCKNN KQIQDFTFDT EIATISLIGY GIKNDCKLLT MILSQLTQDN INVHMMQLSE VKITLLINDK DVEKTIFNLY NLFKIS //