ID A0A085FZD6_9ENTR Unreviewed; 810 AA. AC A0A085FZD6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 08-MAY-2019, entry version 26. 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=metL {ECO:0000313|EMBL:KFC76831.1}; GN ORFNames=GBAG_4289 {ECO:0000313|EMBL:KFC76831.1}; OS Buttiauxella agrestis ATCC 33320. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Buttiauxella. OX NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC76831.1, ECO:0000313|Proteomes:UP000028653}; RN [1] {ECO:0000313|EMBL:KFC76831.1, ECO:0000313|Proteomes:UP000028653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC76831.1, RC ECO:0000313|Proteomes:UP000028653}; RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.; RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction RT of the evolutionary history of the Enterobacteriaceae."; RL Submitted (MAY-2014) 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:KFC76831.1}. 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; JMPI01000074; KFC76831.1; -; Genomic_DNA. DR RefSeq; WP_034500063.1; NZ_JMPI01000074.1. DR STRING; 1006004.GBAG_4289; -. DR EnsemblBacteria; KFC76831; KFC76831; GBAG_4289. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000028653; 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 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 Complete proteome {ECO:0000313|Proteomes:UP000028653}; KW Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:KFC76831.1}; KW NADP {ECO:0000256|PIRNR:PIRNR000727}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727, KW ECO:0000313|EMBL:KFC76831.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000028653}; KW Transferase {ECO:0000256|PIRNR:PIRNR000727, KW ECO:0000313|EMBL:KFC76831.1}. 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; 89054 MW; 282E42FA383203A3 CRC64; MSVSAPTGAS GRQLHKFGGS SLADVKCYLR VAGIMAEYSK LGDMMVVSAA GSTTNQLINW LKLSQSDRLS AHQVQQALRR YQSDLISGLV AADVADTLIG QFVHDLERLA GLLDGKMTDA VYAEVVGHGE IWSARLMSAV LNQLGHPAAW LDAREFMRAE RSAQPQVNEG LSWPLLQELM AQHPHKRLVV TGFICRNDAG ETVLLGRNGS DYSATQIGAL AGVSRVTIWS DVAGVYSADP RKVKDACLLP LLRLDEASEL ARLAAPVLHA RTLQPVSGSD IDLQLRCSYS PEQGSTRIER VLASGTGARI VTSHDDVCLI ELEVAPQQDF KLAHKELDTL LKRAQIRPLS IGVHPDRNLL QLCYTSEVAG SVLQTLQDAN LPGELRLREG LALVAMVGAG VCRNPLHSHR FWQQLKDQPV EFIWQSEDGI SLVAVLRVGP TENLIKGLHK SLFRAEKRIG LVLFGKGNIG SRWLELFSRE QETLSARTGF EFVLSGVVDS RRSLLNYEGL DASRALAFFN DEAVEQDEES LFQWMRAHPY DDLVVLDVTA SEQLADQYLD FASHGFHVIS ANKVAGASTG QKYREIRNAF TKTGRHWLYN ATVGAGLPVN HTVRDLRESG DSILAISGIF SGTLSWLFLQ FDGTVPFTDL VDQAWQQGLT EPDPRVDLSG KDVMRKLVIL AREAGYDIEP DQVRVESLVT SGSETGSIDH FFENGDEINE QMLQRFEAAQ EMGLLLRYVA RFDANGKARV GVEAVRPEHP LASLLPCDNV FAIESRWYRD NPLVIRGPGA GRDVTAGAIQ SDLNRLAQLL //