ID D5MES8_METO1 Unreviewed; 412 AA. AC D5MES8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 29-MAY-2024, entry version 60. 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 Methylomirabilis oxygeniifera. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FP565575; CBE68257.1; -; Genomic_DNA. DR AlphaFoldDB; D5MES8; -. 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 UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00461. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000006898; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009090; P:homoserine biosynthetic process; IEA:TreeGrafter. 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 CDD; cd04923; ACT_AK-LysC-DapG-like_2; 1. DR CDD; cd04913; ACT_AKii-LysC-BS-like_1; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1. DR Gene3D; 3.30.2130.10; VC0802-like; 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 InterPro; IPR027795; CASTOR_ACT_dom. DR NCBIfam; TIGR00656; asp_kin_monofn; 1. DR NCBIfam; TIGR00657; asp_kinases; 1. DR PANTHER; PTHR21499; ASPARTATE KINASE; 1. DR PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1. 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; SSF55021; ACT-like; 2. DR SUPFAM; SSF53633; Carbamate kinase-like; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448}; 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}. FT DOMAIN 264..347 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT BINDING 7..10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 47 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 173..174 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 209..210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 //