ID A0A0T9PAV0_YERKR Unreviewed; 819 AA. AC A0A0T9PAV0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 28-MAR-2018, entry version 17. DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727}; DE Includes: DE RecName: Full=Aspartokinase {ECO:0000256|PIRNR:PIRNR000727}; DE EC=2.7.2.4 {ECO:0000256|PIRNR:PIRNR000727}; DE Includes: DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727}; DE EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR000727}; GN Name=thrA {ECO:0000313|EMBL:CNH54703.1}; GN ORFNames=ERS008472_01715 {ECO:0000313|EMBL:CNH54703.1}; OS Yersinia kristensenii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=28152 {ECO:0000313|EMBL:CNH54703.1, ECO:0000313|Proteomes:UP000041882}; RN [1] {ECO:0000313|EMBL:CNH54703.1, ECO:0000313|Proteomes:UP000041882} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP6945 {ECO:0000313|EMBL:CNH54703.1, RC ECO:0000313|Proteomes:UP000041882}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. {ECO:0000256|PIRNR:PIRNR000727}. CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. {ECO:0000256|PIRNR:PIRNR000727}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. CC {ECO:0000256|PIRNR:PIRNR000727}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 1/3. CC {ECO:0000256|PIRNR:PIRNR000727}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 3/3. CC {ECO:0000256|PIRNR:PIRNR000727}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 1/5. CC {ECO:0000256|PIRNR:PIRNR000727}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 3/5. CC {ECO:0000256|PIRNR:PIRNR000727}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR000727}. CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000727}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC aspartokinase family. {ECO:0000256|PIRNR:PIRNR000727}. 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; CQAW01000006; CNH54703.1; -; Genomic_DNA. DR RefSeq; WP_050113652.1; NZ_CQAW01000006.1. DR EnsemblBacteria; CNH54703; CNH54703; ERS008472_01715. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000041882; Unassembled WGS sequence. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.1160.10; -; 2. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR001341; Asp_kinase. DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH. DR InterPro; IPR027795; CASTOR_ACT_dom. DR InterPro; IPR001342; HDH_cat. DR InterPro; IPR019811; HDH_CS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF13840; ACT_7; 1. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF000727; ThrA; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS51671; ACT; 2. DR PROSITE; PS00324; ASPARTOKINASE; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000727}; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Complete proteome {ECO:0000313|Proteomes:UP000041882}; KW Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:CNH54703.1}; KW NADP {ECO:0000256|PIRNR:PIRNR000727}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727, KW ECO:0000313|EMBL:CNH54703.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR000727}. FT DOMAIN 320 394 ACT. {ECO:0000259|PROSITE:PS51671}. FT DOMAIN 401 478 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 819 AA; 88935 MW; 761A2848BF910454 CRC64; MRVLKFGGTS VANAERFMRV ADIIESNARQ GQVATVLSAP AKITNHLVAM IDKMVAGQDI SPNISDAERI FSELLRGLSD AQPGFDYERL KALVAHEFAQ LKHVLHGISL LGQCPDSINA AIICRGEKLS IAIMEALFQA KGYQVSVINP VEKLLAQGHY LESTVDITES TRRIGSSKIP ADHIILMAGF TAGNDKGELV VLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYTCDPRVV PDARLLKSMS YQEAMELSYF GASVLHPRTI APIAQFQIPC LIKNTSNPQA PGTLIGGESS DDGFPVKGIT NLNNMAMINV SGPGMKGMVG MAARVFAVMS RSGISVVLIT QSSSEYSISF CVPQSELIRA RNALEEEFYL ELKDGLLEPL DVMEHLAVIS VVGDGMRTLR GISARFFSAL ARANINIIAI AQGSSERSIS VVVSNDSATT GVRVCHQMLF NTDQVIEVFV IGVGGVGGAL IEQIYRQQPW LKQRHIDLRV CGIANSKAML TNVHGIALDN WRYELAEVKE PFNLSRLIRL VKEYHLLNPV IVDCTSSQAV ADQYADFLAD GFHVVTPNKK ANTSSMNYYR QMRAAAAKSC RKFLYDTNVG AGLPVIENLQ NLLNAGDELM RFSGILSGSL SFIFGKLDEG MTLSEATLQA KALGYTEPDP RDDLSGMDVA RKLLILAREA GYKLELADID VESVLPANFD ASGDVDSFLA RLPLLDAEFS RLVANAAEQG KVLRYVGVIE EGRCIVRMDA VDGNDPLYKV KNGENALAFY THYYQPIPLV LRGYGAGNDV TAAGVFADLL RTLSWKLGV //