ID J0ZVK9_BARTA Unreviewed; 418 AA. AC J0ZVK9; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 03-MAY-2023, entry version 44. 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=ME9_01425 {ECO:0000313|EMBL:EJF92983.1}; OS Bartonella taylorii 8TBB. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=1094560 {ECO:0000313|EMBL:EJF92983.1, ECO:0000313|Proteomes:UP000002648}; RN [1] {ECO:0000313|EMBL:EJF92983.1, ECO:0000313|Proteomes:UP000002648} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8TBB {ECO:0000313|EMBL:EJF92983.1, RC ECO:0000313|Proteomes:UP000002648}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Kirby J., Kosoy M., Birtles R., Probert W.S., RA Chiaraviglio L., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bartonella taylorii 8TBB."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EJF92983.1}. 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; AIMD01000049; EJF92983.1; -; Genomic_DNA. DR RefSeq; WP_004860722.1; NZ_JH725053.1. DR AlphaFoldDB; J0ZVK9; -. DR STRING; 1094560.ME9_01425; -. DR EnsemblBacteria; EJF92983; EJF92983; ME9_01425. DR PATRIC; fig|1094560.3.peg.1538; -. DR eggNOG; COG0527; Bacteria. DR HOGENOM; CLU_009116_3_2_5; -. DR OrthoDB; 9799110at2; -. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00461. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000002648; Unassembled WGS sequence. 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; 2. 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|RuleBase:RU003448}. FT DOMAIN 276..351 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT DOMAIN 357..418 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 75 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 174..175 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 180 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" FT BINDING 210..211 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1" SQ SEQUENCE 418 AA; 45127 MW; 6A60EED6F140F6F2 CRC64; MARIVMKFGG TSVANIECIH NVARHVKREV DAGNEVAVVV SAMAGKTNEL VQWTCDTSPI HKDAYEYDVV VASGEQVTAG LLALTLQAMG MNARSWLGWQ IPIHTDSAHS RARITDIDGS FLIQRFQEGQ VAVIAGFQGL APDNRISTLG RGGSDTSAVA IAAAVQADRC DIYTDVDGVY TTDPRIEPKA RRLPKVAFEE MLEMASLGAK VLQVRSVELA MVHKVRTFVR SSFEDPDALS MGDPMNSFGT LICDEDEIVE QQNVTGIAFA KDEAQISLRR LADRPGISAA IFGPLAEERI NVDMIVQNIS EDGSKTDMTF TVPSADVDKA VALLEKNRKE IGFDVIQFES DLAKVSVIGI GMRSHAGVAA TAFKALSEKG INIQAITTSE IKISILIDSA YTELAVRTLH AVYGLEKG //