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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
 
 
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