ID A0A510I5X9_9VIBR Unreviewed; 819 AA. AC A0A510I5X9; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 27-NOV-2024, entry version 23. 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:BBL87820.1}; GN ORFNames=VroAM7_04730 {ECO:0000313|EMBL:BBL87820.1}; OS Vibrio rotiferianus. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=190895 {ECO:0000313|EMBL:BBL87820.1, ECO:0000313|Proteomes:UP000315115}; RN [1] {ECO:0000313|Proteomes:UP000315115} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM7 {ECO:0000313|Proteomes:UP000315115}; RA Miyazaki K., Wiseschart A., Pootanakit K., Ishimori K., Kitahara K.; RT "Complete Genome Sequences of Vibrion rotiferianus strain AM7."; RL Submitted (JUL-2019) 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 --------------------------------------------------------------------------- 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; AP019798; BBL87820.1; -; Genomic_DNA. DR RefSeq; WP_045386586.1; NZ_VTXT01000001.1. DR AlphaFoldDB; A0A510I5X9; -. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000315115; Chromosome 1. 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; cd04921; ACT_AKi-HSDH-ThrA-like_1; 1. DR CDD; cd04922; ACT_AKi-HSDH-ThrA_2; 1. DR FunFam; 3.30.2130.10:FF:000001; Bifunctional aspartokinase/homoserine dehydrogenase; 1. DR FunFam; 3.30.360.10:FF:000006; Bifunctional aspartokinase/homoserine dehydrogenase; 1. DR FunFam; 3.40.1160.10:FF:000016; Bifunctional aspartokinase/homoserine dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000083; 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 Gene3D; 3.30.2130.10; VC0802-like; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR045865; ACT-like_dom_sf. DR InterPro; IPR054352; ACT_Aspartokinase. DR InterPro; IPR002912; ACT_dom. 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:SF3; HOMOSERINE DEHYDROGENASE; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF22468; ACT_9; 2. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF000727; ThrA; 1. DR SUPFAM; SSF55021; ACT-like; 2. 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; 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|ARBA:ARBA00022605, KW ECO:0000256|PIRNR:PIRNR000727}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR000727}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000727}; Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000727}. FT DOMAIN 320..394 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT DOMAIN 401..473 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" SQ SEQUENCE 819 AA; 88184 MW; DC657B47F49A9A18 CRC64; MRVLKFGGSS LADADRFLRA ADIIANNAQQ EEVAVVLSAP GKTTNKLVAV IEGALRNGEA ELQINELEAS FKALFADIQG VLPNIDGAAF DNQVKTSLSQ LRQFVHGINL LGMCPNNVNA RIISKGERIS IQLMKAVLEA KGQPAHLIDP VEYLYAKGDH LEAMVDVDVS TQNFRQNPLP QGHVNIMPGF TAGNEKGELV TLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYNCDPRLV EDARLLKSLS YQEAMELSYF GASVLHPKTI APIAQFHIPC LIKNSFNPQG AGTLIGQDTG EDNLAIKGIT TLNDLTMVNV SGPGMKGMVG MASRVFGAMS SAGVSIVLIT QSSSEYSISF CIEAQDKAKA QQVLADAFEL ELKDGLLEPV DFIDDVSIVT LVGDGMRTSR GVASRFFSSL AEVNVNIVAI AQGSSERAIS AVIPEDKISE AIKACHENLF NSKHFLDVFV VGVGGVGGEL VDQIERQQAK LAEKGIVIRV CGLANSKGLL LDSEGLPLEH WRDRMSASTE EFSLARLISL VQRNHIINPV LVDCTSSEAI ANQYADFLAA GFHVVTPNKK ANTASMAYYH QLRGVARSSR RKLLYETTVG AGLPVIENLQ NLIAAGDELE RFSGILSGSL SYIFGKLDEG MSLSEATNIA KQNGFTEPDP RDDLSGMDVA RKLLILAREA GMSLELEDVV VDQALPPGFD DSGSVDEFMA RLPEADAYFK ELSAKAAEEG KVLRYVGEII DGKCKVSIAA VDENDPMFKI KDGENALAFY SRYYQPIPLV LRGYGAGTEV TAAGVFSDVM RTLGWKLGV //