ID A0A1U9JT14_9HYPH Unreviewed; 418 AA. AC A0A1U9JT14; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 22-FEB-2023, entry version 21. DE RecName: Full=Aspartokinase {ECO:0000256|ARBA:ARBA00016273, ECO:0000256|RuleBase:RU003448}; DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059, ECO:0000256|RuleBase:RU003448}; GN ORFNames=BHV28_02830 {ECO:0000313|EMBL:AQS41005.1}; OS Candidatus Tokpelaia hoelldoblerii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Candidatus Tokpelaia. OX NCBI_TaxID=1902579 {ECO:0000313|EMBL:AQS41005.1, ECO:0000313|Proteomes:UP000188912}; RN [1] {ECO:0000313|EMBL:AQS41005.1, ECO:0000313|Proteomes:UP000188912} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hsal {ECO:0000313|EMBL:AQS41005.1}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(2010). RN [2] {ECO:0000313|EMBL:AQS41005.1, ECO:0000313|Proteomes:UP000188912} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hsal {ECO:0000313|EMBL:AQS41005.1}; RX PubMed=27976703; DOI=10.1038/srep39197; RA Neuvonen M.M., Tamarit D., Naslund K., Liebig J., Feldhaar H., Moran N.A., RA Guy L., Andersson S.G.; RT "The genome of Rhizobiales bacteria in predatory ants reveals urease gene RT functions but no genes for nitrogen fixation."; RL Sci. Rep. 6:39197-39197(2016). 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; CP017315; AQS41005.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1U9JT14; -. DR STRING; 1902579.BHV28_02830; -. DR EnsemblBacteria; AQS41005; AQS41005; BHV28_02830. DR KEGG; thd:BHV28_02830; -. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00461. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000188912; 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: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 PANTHER; PTHR21499; ASPARTATE KINASE; 1. DR PANTHER; PTHR21499:SF3; ASPARTOKINASE 1; 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 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}; 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 Reference proteome {ECO:0000313|Proteomes:UP000188912}; KW Transferase {ECO:0000256|RuleBase:RU003448}. FT DOMAIN 275..359 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 184 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 418 AA; 44996 MW; 199690390B3344A7 CRC64; MARIVMKFGG SSVADIERIR NVARHVKREV DAGNQVAVVV SAMAGTTNQL IAWVRQANDN YDPREYDSVV ASGEQVTSGL LALALQAIGV DARSWLGWQI PLRTDGNHNS ARITDIDGTD LIACLEKGQV AVIAGFQGIA PENRMTTLGR GGSDTSGVAV AAAMSADRCD IYTDVDGVYT TDPRIEPKAR RLNRIAFEEM LEMASLGAKV LQVRSVELAM VHKVRTFVRS SFNAPDAPGM DDPLNPPGTL ICDEDEIMEQ QVVTGIAFAR DEAQISLRRL DDKPGISAAI FGPLAEASIN VDMIVQNISE DGSKTDMTFT VPTVDLDKAV RILEKNRRSI TSEVIQSEKG LAKVSVIGIG MRSHAGVAAT AFRALAEKSI NIRAITTSEI KISILIDSAY TELAVRTLHT VYGLDKAS //