ID A0A085FZD6_9ENTR Unreviewed; 810 AA. AC A0A085FZD6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 27-NOV-2024, entry version 43. 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; Pseudomonadota; 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 of RT the evolutionary history of the Enterobacteriaceae."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bifunctional aspartate kinase and homoserine dehydrogenase CC that catalyzes the first and the third steps toward the synthesis of CC lysine, methionine and threonine from aspartate. CC {ECO:0000256|ARBA:ARBA00044938}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate + ATP = 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:ARBA00044882}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23777; CC Evidence={ECO:0000256|ARBA:ARBA00044882}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-homoserine + NAD(+) = L-aspartate 4-semialdehyde + NADH + CC H(+); Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00044923}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15759; CC Evidence={ECO:0000256|ARBA:ARBA00044923}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-homoserine + NADP(+) = L-aspartate 4-semialdehyde + NADPH + CC H(+); Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00044905}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15763; CC Evidence={ECO:0000256|ARBA:ARBA00044905}; CC -!- COFACTOR: CC Name=a metal cation; Xref=ChEBI:CHEBI:25213; CC Evidence={ECO:0000256|ARBA:ARBA00001920}; 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|PIRNR:PIRNR000727}. 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|PIRNR:PIRNR000727}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-homoserine from L-aspartate: step 3/3. CC {ECO:0000256|ARBA:ARBA00005062, ECO:0000256|PIRNR:PIRNR000727}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139, CC ECO:0000256|PIRNR:PIRNR000727}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056, CC ECO:0000256|PIRNR:PIRNR000727}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|PIRNR:PIRNR000727}. CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007952, CC ECO:0000256|PIRNR:PIRNR000727}. CC -!- SIMILARITY: In the N-terminal section; belongs to the aspartokinase CC family. {ECO:0000256|ARBA:ARBA00010046, ECO:0000256|PIRNR:PIRNR000727}. 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: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 AlphaFoldDB; A0A085FZD6; -. DR STRING; 1006004.GBAG_4289; -. DR eggNOG; COG0460; Bacteria. DR eggNOG; COG0527; Bacteria. DR OrthoDB; 9799110at2; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0009090; P:homoserine biosynthetic process; IEA:TreeGrafter. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd04257; AAK_AK-HSDH; 1. DR CDD; cd04892; ACT_AK-like_2; 1. DR FunFam; 3.30.360.10:FF:000006; Bifunctional aspartokinase/homoserine dehydrogenase; 1. DR FunFam; 3.40.1160.10:FF:000009; Bifunctional aspartokinase/homoserine dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000124; Bifunctional aspartokinase/homoserine dehydrogenase; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1. DR Gene3D; 1.20.120.1320; Aspartokinase, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR049638; AK-HD. 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; IPR042199; AsparK_Bifunc_asparK/hSer_DH. DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR011147; Bifunc_Aspkin/hSer_DH. DR InterPro; IPR001342; HDH_cat. DR InterPro; IPR019811; HDH_CS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR00657; asp_kinases; 1. DR PANTHER; PTHR43070; -; 1. DR PANTHER; PTHR43070:SF5; HOMOSERINE DEHYDROGENASE; 1. 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; SSF53633; Carbamate kinase-like; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, KW ECO:0000256|PIRNR:PIRNR000727}; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000727}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW NAD {ECO:0000256|ARBA:ARBA00023027}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000727}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000727}; KW Reference proteome {ECO:0000313|Proteomes:UP000028653}; KW Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}; KW Transferase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:KFC76831.1}. FT DOMAIN 12..284 FT /note="Aspartate/glutamate/uridylate kinase" FT /evidence="ECO:0000259|Pfam:PF00696" FT DOMAIN 465..600 FT /note="Aspartate/homoserine dehydrogenase NAD-binding" FT /evidence="ECO:0000259|Pfam:PF03447" FT DOMAIN 608..803 FT /note="Homoserine dehydrogenase catalytic" FT /evidence="ECO:0000259|Pfam: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 //