ID A0A2W6W578_ACTSX Unreviewed; 367 AA. AC A0A2W6W578; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 10-OCT-2018, entry version 2. 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=DI576_09605 {ECO:0000313|EMBL:PZU32151.1}; OS Actinomyces sp. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=29317 {ECO:0000313|EMBL:PZU32151.1}; RN [1] {ECO:0000313|EMBL:PZU32151.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S2_006_000_R1_54 {ECO:0000313|EMBL:PZU32151.1}; RA Brooks B., Olm M.R., Firek B.A., Baker R., Thomas B.C., Morowitz M.J., RA Banfield J.F.; RT "Infants hospitalized years apart are colonized by the same room- RT sourced microbial strains."; RL Submitted (AUG-2017) 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:PZU32151.1}. 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; QFPC01000162; PZU32151.1; -; Genomic_DNA. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. 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; TIGR01296; asd_B; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; 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 Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}. FT DOMAIN 24 139 Semialdhyde_dh. {ECO:0000259|SMART: FT SM00859}. FT NP_BIND 31 34 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 59 60 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 179 180 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 149 149 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 276 276 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 119 119 Phosphate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 176 176 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 269 269 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_02121}. FT BINDING 345 345 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 367 AA; 37822 MW; 4A0A07723F4D02B7 CRC64; MSTSTQSTQH RPVNEYVGPA DGVAVAVVGA TGQVGRVMRA MLAERDFPAR AVRFFSSARS AGTVVDFRGA AVEVEDVAIA DPAGVDVAIF SAGGAASREH APRFAAAGAV VVDNSSAWRK DPEVPLVVSE VNPHALRERP KGIIANPNCT TMAIMPALKA LHDEAGLVRF FASTYQAVSG SGRAGVAELA GQVRAVADQD IEALALDGRA VAFPAPGVYV DTIAFNAVAW AGADAGDGSG ETDEEQKLRN ESRKILEIPD LAVSGTCVRI PVFSGHGVSV SAELAREIGP ERARELLAGA PGVTLQDVPS PLGSAGRDGT FVGRVRADRG FAPGHGIAFF AVGDNLRKGA ALNAVELAEL VAAELRA //