ID A0A066UK11_9VIBR Unreviewed; 372 AA. AC A0A066UK11; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 25-OCT-2017, entry version 18. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {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|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 ORFNames=VFDL14_01900 {ECO:0000313|EMBL:KDN27756.1}; OS Vibrio fortis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; 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. CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L- CC aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. {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|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. {ECO:0000256|HAMAP- CC Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_02121, CC ECO:0000256|SAAS:SAAS00827794}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}. 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: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; JFFR01000025; KDN27756.1; -; Genomic_DNA. DR RefSeq; WP_032551976.1; NZ_JFFR01000025.1. 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 GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. 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; PTHR10174:SF116; PTHR10174:SF116; 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 Complete proteome {ECO:0000313|Proteomes:UP000027219}; KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW 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|HAMAP-Rule:MF_02121}. FT DOMAIN 2 122 Semialdhyde_dh. {ECO:0000259|SMART: FT SM00859}. FT NP_BIND 9 12 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 36 37 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 165 166 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 135 135 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 275 275 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 73 73 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT BINDING 102 102 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 162 162 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 241 241 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 244 244 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 268 268 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 351 351 NADP. {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 //