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AK_RICBR
ID   AK_RICBR                Reviewed;         406 AA.
AC   Q1RGM9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Aspartokinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase;
GN   Name=lysC; OrderedLocusNames=RBE_1404;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05485.1; -; Genomic_DNA.
DR   RefSeq; WP_011478054.1; NC_007940.1.
DR   AlphaFoldDB; Q1RGM9; -.
DR   SMR; Q1RGM9; -.
DR   STRING; 336407.RBE_1404; -.
DR   EnsemblBacteria; ABE05485; ABE05485; RBE_1404.
DR   KEGG; rbe:RBE_1404; -.
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; UP000001951; 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; IPR002912; ACT_dom.
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; PS51671; ACT; 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..406
FT                   /note="Aspartokinase"
FT                   /id="PRO_0000288718"
FT   DOMAIN          342..406
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   406 AA;  44682 MW;  8A27CD8A2A864AC6 CRC64;
     MALIIQKFGG TSVTTIDRIK KIIPIIKAEI AKNNQVIIVV SAMAGVTNQL VTLCNEVSSL
     NKSSQLAEYD VALSSGEIVT ASLLALALQE ENINARSFLA WQLPILTDDN HSKALVESVD
     TNLLNECLQQ NIIPIIAGFQ GINKHNRLAT LGRGGSDTTA ALIAAAMKAD RCDIYTDVEG
     VFAADPRIIP KAKKIDEIDF SEMLELALSG AKVLHSRAAE IVMRYQIDMR ILSTFAPEAG
     CTLITSKDKI MEKRIISGIT SNKNLLYITI ESSSLNFIQV ASIIAQNNNH IEVMQEIEPN
     KRYSFITNLT DKNSLHILLT NLKNNNQISN FTFDTEIATV SIIGHGIKND LKLLEVILSK
     LAKDNINVQM VQISEIKIIL LINDKQVEKT VLDLYDLLKI SETGHC
 
 
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