ID A0A066UK11_9VIBR Unreviewed; 372 AA. AC A0A066UK11; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-AUG-2020, entry version 28. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120, ECO:0000256|HAMAP-Rule:MF_02121}; DE Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; DE Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121}; DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120, ECO:0000256|HAMAP-Rule:MF_02121}; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; GN Name=asd {ECO:0000256|HAMAP-Rule:MF_02121, GN ECO:0000313|EMBL:KAB0290200.1}; GN ORFNames=F2P58_04520 {ECO:0000313|EMBL:KAB0290200.1}, F2Z80_03915 GN {ECO:0000313|EMBL:KAB0303155.1}, VFDL14_01900 GN {ECO:0000313|EMBL:KDN27756.1}; OS Vibrio fortis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=212667 {ECO:0000313|EMBL:KDN27756.1, ECO:0000313|Proteomes:UP000027219}; RN [1] {ECO:0000313|EMBL:KDN27756.1, ECO:0000313|Proteomes:UP000027219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Dalian14 {ECO:0000313|EMBL:KDN27756.1, RC ECO:0000313|Proteomes:UP000027219}; RA Wang Y., Song L., Liu G., Ding J.; RT "Vibrio fortis Dalian14 Genome Sequencing."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAB0303155.1, ECO:0000313|Proteomes:UP000326687} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S7-72 {ECO:0000313|EMBL:KAB0303155.1, RC ECO:0000313|Proteomes:UP000326687}; RA Das S.K.; RT "Vibrio Fortis S7-72."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KAB0290200.1, ECO:0000313|Proteomes:UP000326789} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AN60 {ECO:0000313|EMBL:KAB0290200.1, RC ECO:0000313|Proteomes:UP000326789}; RA Das S.K.; RT "Whole genome sequence of Vibrio fortis."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- CC 4-phosphate. {ECO:0000256|ARBA:ARBA00002492, ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho- CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11; CC Evidence={ECO:0000256|ARBA:ARBA00001636, ECO:0000256|HAMAP- CC Rule:MF_02121}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. CC {ECO:0000256|ARBA:ARBA00005076, ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000256|ARBA:ARBA00005021, ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097, CC ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00010584, ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}. 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:KDN27756.1}. 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; VWSE01000003; KAB0290200.1; -; Genomic_DNA. DR EMBL; VXDD01000001; KAB0303155.1; -; Genomic_DNA. DR EMBL; JFFR01000025; KDN27756.1; -; Genomic_DNA. DR RefSeq; WP_032551976.1; NZ_VXDD01000001.1. DR EnsemblBacteria; KDN27756; KDN27756; VFDL14_01900. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000027219; Unassembled WGS sequence. DR Proteomes; UP000326687; Unassembled WGS sequence. DR Proteomes; UP000326789; Unassembled WGS sequence. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. 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 HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR011534; Asp_ADH_gamma-type. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR PANTHER; PTHR46278:SF4; PTHR46278:SF4; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01745; asd_gamma; 1. DR PROSITE; PS01103; ASD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915, KW ECO:0000256|HAMAP-Rule:MF_02121}; KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP- KW Rule:MF_02121}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_02121}; NADP {ECO:0000256|HAMAP-Rule:MF_02121}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121, KW ECO:0000313|EMBL:KDN27756.1}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP- KW Rule:MF_02121}. FT DOMAIN 2..122 FT /note="Semialdhyde_dh" FT /evidence="ECO:0000259|SMART:SM00859" FT NP_BIND 9..12 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT NP_BIND 36..37 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT NP_BIND 165..166 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT ACT_SITE 135 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT ACT_SITE 275 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 73 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 102 FT /note="Phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 162 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 241 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 244 FT /note="Phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 268 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 351 FT /note="NADP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" SQ SEQUENCE 372 AA; 40359 MW; ADB9DEB581265CC6 CRC64; MRVGLVGWRG MVGSVLMQRM VEERDFDLIE PVYYSTSQIG IPAPVLGGKD AGLLQDAFDI DSLKQLDAVI TCQGGDYTSK VYPALRQAGW KGYWIDAAST LRMDADSIIT LDPVNLAQIQ QGIHGGTNTF VGGNCTVSLM LMALGGLYEK GMVEWMSAMT YQAASGAGAK NMRELISQMG VINDSVSSEL ANPASSILDI DKKVADTIRS ESFPTDQFGA PLAGSLIPWI DVKRENGQSK EEWKAGVEAN KILGLDGQPI PIDGTCVRIG AMRCHAQALT IKLKQDVPMD EIEEIIATHN DWVKVIPNDR DITAQELTPA KVTGTMSVPV GRLRKMSMGN DFLNAFTVGD QLLWGAAEPL RRTLRIILAE KA //