ID J0ZVK9_BARTA Unreviewed; 418 AA. AC J0ZVK9; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 08-MAY-2019, entry version 33. DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448}; DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448}; GN ORFNames=ME9_01425 {ECO:0000313|EMBL:EJF92983.1}; OS Bartonella taylorii 8TBB. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; 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., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., 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|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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 STRING; 1094560.ME9_01425; -. DR EnsemblBacteria; EJF92983; EJF92983; ME9_01425. DR PATRIC; fig|1094560.3.peg.1538; -. DR OrthoDB; 1067792at2; -. 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: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; 2. 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:UP000002648}; KW Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:EJF92983.1}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1}; KW Transferase {ECO:0000256|RuleBase:RU003448}. FT DOMAIN 276 351 ACT. {ECO:0000259|PROSITE:PS51671}. FT DOMAIN 357 418 ACT. {ECO:0000259|PROSITE:PS51671}. FT NP_BIND 7 10 ATP. {ECO:0000256|PIRSR:PIRSR000726-1}. FT NP_BIND 174 175 ATP. {ECO:0000256|PIRSR:PIRSR000726-1}. FT NP_BIND 210 211 ATP. {ECO:0000256|PIRSR:PIRSR000726-1}. FT BINDING 47 47 Substrate. {ECO:0000256|PIRSR: FT PIRSR000726-1}. FT BINDING 75 75 Substrate. {ECO:0000256|PIRSR: FT PIRSR000726-1}. FT BINDING 180 180 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR000726- FT 1}. FT BINDING 185 185 ATP. {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 //