ID   D5MES8_9BACT            Unreviewed;       412 AA.
AC   D5MES8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   12-AUG-2020, entry version 48.
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., 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|ARBA:ARBA00000709,
CC         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|ARBA:ARBA00004766, ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004986, ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139,
CC       ECO:0000256|RuleBase:RU004249}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|ARBA:ARBA00010122, ECO:0000256|RuleBase:RU003448}.
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DR   EMBL; FP565575; CBE68257.1; -; Genomic_DNA.
DR   STRING; 671143.DAMO_1197; -.
DR   KEGG; mox:DAMO_1197; -.
DR   PATRIC; fig|671143.5.peg.1048; -.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_009116_3_2_0; -.
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   CDD; cd04261; AAK_AKii-LysC-BS; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_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   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|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000726-
KW   1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448,
KW   ECO:0000313|EMBL:CBE68257.1};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000726-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448,
KW   ECO:0000313|EMBL:CBE68257.1}.
FT   DOMAIN          264..347
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   NP_BIND         7..10
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   NP_BIND         173..174
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   NP_BIND         209..210
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         47
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         74
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         179
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
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
//