ID A0A510I5X9_9VIBR Unreviewed; 819 AA. AC A0A510I5X9; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 07-APR-2021, entry version 8. 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; Proteobacteria; 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 -!- 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 --------------------------------------------------------------------------- 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 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: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; 1.20.120.1320; -; 1. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR002912; ACT_dom. 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_aspartokin/hSer_DH. DR InterPro; IPR027795; CASTOR_ACT_dom. DR InterPro; IPR001342; HDH_cat. DR InterPro; IPR019811; HDH_CS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43070; PTHR43070; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF13840; ACT_7; 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; 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 ECO:0000313|EMBL:BBL87820.1}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; 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}; 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 //