ID A0A3V7PJP1_SALET Unreviewed; 810 AA. AC A0A3V7PJP1; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. 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 ORFNames=C7S57_21015 {ECO:0000313|EMBL:EAA8831237.1}; OS Salmonella enterica subsp. enterica serovar Javiana. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=363569 {ECO:0000313|EMBL:EAA8831237.1}; RN [1] {ECO:0000313|EMBL:EAA8831237.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FDA00012733 {ECO:0000313|EMBL:EAA8831237.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (JUL-2018) 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|PIRNR:PIRNR000727}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4- CC semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:537519; EC=1.1.1.3; CC Evidence={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 -!- 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:EAA8831237.1}. 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; AAACWO010000009; EAA8831237.1; -; Genomic_DNA. DR RefSeq; WP_000110811.1; NZ_MYCD01000012.1. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00462. DR CDD; cd04257; AAK_AK-HSDH; 1. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR041743; AK-HSDH_N. 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; IPR001342; HDH_cat. DR InterPro; IPR019811; HDH_CS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR Pfam; PF00696; AA_kinase; 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; 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 Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:EAA8831237.1}; KW NADP {ECO:0000256|PIRNR:PIRNR000727}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727}; KW Transferase {ECO:0000256|PIRNR:PIRNR000727}. FT DOMAIN 12 284 AA_kinase. {ECO:0000259|Pfam:PF00696}. FT DOMAIN 465 600 NAD_binding_3. {ECO:0000259|Pfam: FT PF03447}. FT DOMAIN 608 803 Homoserine_dh. {ECO:0000259|Pfam: FT PF00742}. SQ SEQUENCE 810 AA; 88875 MW; D823F45FE694D7E1 CRC64; MSVIAQAGAK GRQLHKFGGS SLADVKCYLR VAGIMAEYSQ PDDMMVVSAA GSTTNQLISW LKLSQTDRLS AHQVLQTLRR YQCDLISGLL PADAADDLTS AFISDLERLA ALLDGGVTDA VYAEIVGHGE IWSARLMSAV LNQQGLDAAW LDARAFLRAE RAAQPQVDEG LSYPLLQQLL AQHPGKRLVV TGFISRNHDG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSD IDLQLRCSYT PDQGSTRIER VLASGTGARI VTSHDDICLI EFQVPASQDF RLAHKELDQI LKRAQARPLA VGVHRDRQLL QFCYTAEVAD SVLKLLDDVG LPGELRLRQG LALVAMVGAG VTRNPLHCHR FWQQLKGQPV EFTWQSEEGI SLVAVLRTGP TESLIQGLHQ SVFRAEKRIG LMLFGKGNIG SRWLELFARE QSTLSARTGF EFVLAGVVDS RRSLLNYEGL DASRALAFFD DEAVEQDEES LFLWMRAHPY DDLVVLDVTA SEQLADQYLD FASHGFHVIS ANKLAGASAS DKYRQIHDAF EKTGRYWLYN ATVGAGLPIN HTVRDLIDSG DTILSISGIF SGTLSWLFLQ FDGTVPFTDL VDQAWQQGLT EPDPRVDLSG KDVMRKLVIL AREAGYDIEP DQVRVESLVP AHCEEGSIDH FFENGDALNE QMVQRLEAAR ELGLVLRYVA RFDANGKARV GVEAVRPEHP LAALLPCDNV FAIESRWYRD NPLVIRGPGA GRDVTAGAIQ SDINRLAQLL //