ID   D5MES8_9BACT            Unreviewed;       412 AA.
AC   D5MES8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   10-APR-2019, entry version 44.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   Name=lysC {ECO:0000313|EMBL:CBE68257.1};
GN   ORFNames=DAMO_1197 {ECO:0000313|EMBL:CBE68257.1};
OS   Candidatus Methylomirabilis oxyfera.
OC   Bacteria; candidate division NC10; Candidatus Methylomirabilis.
OX   NCBI_TaxID=671143 {ECO:0000313|EMBL:CBE68257.1, ECO:0000313|Proteomes:UP000006898};
RN   [1] {ECO:0000313|EMBL:CBE68257.1, ECO:0000313|Proteomes:UP000006898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20336137; DOI=10.1038/nature08883;
RA   Ettwig K.F., Butler M.K., Le Paslier D., Pelletier E., Mangenot S.,
RA   Kuypers M.M.M., Schreiber F., Dutilh B.E., Zedelius J., de Beer D.,
RA   Gloerich J., Wessels H.J.C.T., van Allen T., Luesken F., Wu M.,
RA   van de Pas-Schoonen K.T., Op den Camp H.J.M., Janssen-Megens E.M.,
RA   Francoijs K-J., Stunnenberg H., Weissenbach J., Jetten M.S.M.,
RA   Strous M.;
RT   "Nitrite-driven anaerobic methane oxidation by oxygenic bacteria.";
RL   Nature 464:543-548(2010).
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         Evidence={ECO:0000256|RuleBase:RU003448};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|RuleBase:RU003448}.
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DR   EMBL; FP565575; CBE68257.1; -; Genomic_DNA.
DR   ProteinModelPortal; D5MES8; -.
DR   STRING; 671143.DAMO_1197; -.
DR   KEGG; mox:DAMO_1197; -.
DR   PATRIC; fig|671143.5.peg.1048; -.
DR   KO; K00928; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000006898; 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:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR002912; ACT_dom.
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; IPR027795; CASTOR_ACT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 2.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00656; asp_kin_monofn; 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 {ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006898};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:CBE68257.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Transferase {ECO:0000256|RuleBase:RU003448,
KW   ECO:0000313|EMBL:CBE68257.1}.
FT   DOMAIN      264    347       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       7     10       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     173    174       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     209    210       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   BINDING      47     47       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING      74     74       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING     179    179       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000726-
FT                                1}.
SQ   SEQUENCE   412 AA;  44104 MW;  A8C4D33C066BFD45 CRC64;
     MSLIVQKYGG SSVADVERIT NVAHRVVETK VQGNDLVVVV SAMAGETDRL LGLAAKISDR
     PDERELDVIV ATGEQISIGL LSLAIQHYGH KARSFTGAQV RIQTDTAHTK AKIVSVEVDR
     VQQALREGAI VIVAGFQGVT AEEDVTTLGR GGSDLTAVAM AAALKADLCE IYTDVEGVYT
     ADPNIVPEAR KLGKISYDEM LELASLGAKV LQARSVEYAK NYAVPIHVRS SFNTNQGTLV
     VQEDAEMERV VVSGIACDRN EAKITVLRVA DRPGIAAKLF GQVAEANIVV DMIVQNISQD
     GTTDISFTVP KSDFSKAMSL VNAVAKEIGA QQVMGDDRVA KVSIVGVGMR THSGVAAKMF
     EVLSCENINI MMISTSEIKV SCVIDAKYGE LAVRVLHEAF GLAEYKPVEE RA
//