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-MAY-2019, entry version 4. 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; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; 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=10.1038/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 RT substantially 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|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: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 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:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.1160.10; -; 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; 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:UP000263796}; KW Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:HCH01213.1}; KW NADP {ECO:0000256|PIRNR:PIRNR000727}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727, KW ECO:0000313|EMBL:HCH01213.1}; KW Transferase {ECO:0000256|PIRNR:PIRNR000727, KW ECO:0000313|EMBL:HCH01213.1}. FT DOMAIN 5 274 AA_kinase. {ECO:0000259|Pfam:PF00696}. FT DOMAIN 457 593 NAD_binding_3. {ECO:0000259|Pfam: FT PF03447}. FT DOMAIN 601 796 Homoserine_dh. {ECO:0000259|Pfam: FT 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 //