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AK_RICFE
ID   AK_RICFE                Reviewed;         401 AA.
AC   Q4UK84;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Aspartokinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase;
GN   Name=lysC; OrderedLocusNames=RF_1200;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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   -!- 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}.
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DR   EMBL; CP000053; AAY62051.1; -; Genomic_DNA.
DR   RefSeq; WP_011271504.1; NC_007109.1.
DR   AlphaFoldDB; Q4UK84; -.
DR   SMR; Q4UK84; -.
DR   STRING; 315456.RF_1200; -.
DR   EnsemblBacteria; AAY62051; AAY62051; RF_1200.
DR   KEGG; rfe:RF_1200; -.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_009116_3_2_5; -.
DR   OMA; DMIVQTI; -.
DR   OrthoDB; 1067792at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000008548; Chromosome.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04261; AAK_AKii-LysC-BS; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR045865; ACT-like_dom_sf.
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   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 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; Transferase.
FT   CHAIN           1..401
FT                   /note="Aspartokinase"
FT                   /id="PRO_0000288720"
SQ   SEQUENCE   401 AA;  44340 MW;  5492DB95BBA62FA0 CRC64;
     MALIIQKFGG TSVANIDRIK KIAPIIKAEI AKNNQVIVVV SAMAGVTNQL VTLCNEVSSL
     NNISQFAEYD VALSSGEIVT ASLLALALQE EDIKAQSFLA WQLPILTDNN HSKALVESIT
     TDLLEKYLQL NTVPIIAGFQ GTNKSNRLTT LGRGGSDTTA ALIAAAMKAK RCDIYTDVEG
     IFTADPRIIP NAKKIKEIDF LEMLELASSG AKVLHPRAVE LVMRYKIDMR VLSTFSPNTE
     GTLITSKDKN MENGIINSIT SNKNLLKISV KSISLSFLQV ANMITQNNNH IEFMQEIKNN
     EEYSFITNLT DENNLQALLT NLKNDKQIQD FTFDAEIATI SLIGYGIKND CKVLEMILSK
     LTKDNINVNM IQLSEVKITL LINDQDAEKT IFNLYNLFKI S
 
 
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