ID A0A3D1Z4M8_VIBSX Unreviewed; 803 AA. AC A0A3D1Z4M8; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 08-NOV-2023, entry version 16. 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:HCH01213.1}; GN Synonyms=metM {ECO:0000313|EMBL:HCH01213.1}; GN ORFNames=DEV85_04875 {ECO:0000313|EMBL:HCH01213.1}; OS Vibrio sp. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=678 {ECO:0000313|EMBL:HCH01213.1, ECO:0000313|Proteomes:UP000263796}; RN [1] {ECO:0000313|EMBL:HCH01213.1, ECO:0000313|Proteomes:UP000263796} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA10737 {ECO:0000313|EMBL:HCH01213.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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|ARBA:ARBA00000709, CC ECO:0000256|PIRNR:PIRNR000727}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + CC NADH; 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:ARBA00001406}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + CC NADPH; 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:ARBA00000116, CC 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|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:HCH01213.1}. 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; DPFO01000022; HCH01213.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3D1Z4M8; -. DR EnsemblBacteria; HCH01213; HCH01213; DEV85_04875. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00462. DR Proteomes; UP000263796; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule. 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; 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_aspartokin/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|PIRNR:PIRNR000727, ECO:0000313|EMBL:HCH01213.1}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000727}. FT DOMAIN 5..274 FT /note="Aspartate/glutamate/uridylate kinase" FT /evidence="ECO:0000259|Pfam:PF00696" FT DOMAIN 457..593 FT /note="Aspartate/homoserine dehydrogenase NAD-binding" FT /evidence="ECO:0000259|Pfam:PF03447" FT DOMAIN 601..796 FT /note="Homoserine dehydrogenase catalytic" FT /evidence="ECO:0000259|Pfam:PF00742" SQ SEQUENCE 803 AA; 87707 MW; 767CC95EEC30E5DB CRC64; MTSARQLHKF GGSSLANPEC YKRVANILKE YSSPADLVVV SAAGSTTNRL IEWITALEKD GRIAHEILQE LRQFQINLID ELLPEEKAQP LIMLVNQEFM ALGEINGPVS EVMRASILGH GEVWSSRLLA ALLSHLALEA VQLDSRDFLR AERGAQPEVD RGRSLPLLKE KLAQHGKLRV VITGFMARND TGETVLLGRN GSDYSATVIG ALAEASRVTI WSDVAGVYSA DPRKVTDACL LPLLRLDEAS ELARLAAPVL HSRTLQPVAQ SAMDLSLRCS YQPESGSTRI ERVLASGRGA KIITSLDEVL LIQIHFGAGH DFTRLESDLM RSLARAQLQP LAMQSQPDQG LVSLAYTAEI AASAMTYLQD TAVGAEIKLR EGYSMVAAVG AGVTINPNHC YGFYQQLKNA PVEFISEADS GLSLVAILRK TNVTELVVGV HSQLFQAQKR VAIALCGKGN IGSSWLALFA EQKAELEKRR GMSFDLVAVV DSQTYWLDLN GIDPTQALTR FEDESVSNDG QAWLNTLAHQ TDYHEVVVMD VTASAELARQ YEVIAEHGMH LICANKVAGS ASTQDYQRVV NAFDKTGRHW LYNATVGAGL PVNYAIRDLR NSGDQITAVS GIFSGTLSWL FQQFDGSVPF TDLVDLAWQQ GLTEPDPRSD LDGSDVMRKL VIVARESGLE IEPESVKVES LVPDELKDLS TDEFFDKGKV LNERLSERLA KAQKQGKVLR YIARLSRDGK ATVGVEALSP EHALANLLPC DNVFAIESKW YKDNPLVIKG PGAGREVTAG ALQSDLNRLS NLI //