AK_CHLMU
ID AK_CHLMU Reviewed; 437 AA.
AC Q9PK32;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Aspartokinase;
DE EC=2.7.2.4;
DE AltName: Full=Aspartate kinase;
GN Name=lysC; OrderedLocusNames=TC_0641;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39470.1; -; Genomic_DNA.
DR PIR; D81681; D81681.
DR RefSeq; WP_010231084.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PK32; -.
DR SMR; Q9PK32; -.
DR STRING; 243161.TC_0641; -.
DR EnsemblBacteria; AAF39470; AAF39470; TC_0641.
DR GeneID; 1246002; -.
DR KEGG; cmu:TC_0641; -.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_6_0_0; -.
DR OMA; ESVTIWK; -.
DR OrthoDB; 1067792at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000000800; 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 Gene3D; 1.20.120.1320; -; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR Pfam; PF00696; AA_kinase; 1.
DR SUPFAM; SSF53633; SSF53633; 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..437
FT /note="Aspartokinase"
FT /id="PRO_0000066673"
SQ SEQUENCE 437 AA; 47795 MW; 3E74D659E04906FA CRC64;
MFKEKKAPLV CKFGGTSVGT SSSIQRVCEI IRKEKPSFVV VSAVAGVTDL LEEFCRAPVG
QKSQFTAMIR EKHESIAKEL GIDVAIEPFL GPLKQFEGAG HLQQEDQAKI LAIGEDLSAS
LICSYCRANS LQLEQLEARQ VILTDSQFLR AEPDLALMQT MWGELVLKEN TIYLMQGFLG
ATASGATTVL GRGGSDFSAS LVGELCEARE LRIYTDVRGV HTADPKILKD TQLIDFLTFE
EMQELASSGS KVLHQDMLKP CIRAKVPIFV TSTFDLTKEG TWICASLNEG VEGPEIKALS
LKANQALWFV EYHSPLMRLE NVLRCVRGLG SIPGVVMAQN SGVYFTVDWE ENNQSMTEAL
REFGAVSCEG PVSLVALVGA KLTSWSMTGV FDALQGTPVL YWSQTDTVIN LIINEESGVV
VTKLLHDYVL GLNRSGL