ID A0A2W6W578_ACTSX Unreviewed; 367 AA. AC A0A2W6W578; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 28-JUN-2023, entry version 13. 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 ORFNames=DI576_09605 {ECO:0000313|EMBL:PZU32151.1}; OS Actinomyces sp. OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=29317 {ECO:0000313|EMBL:PZU32151.1, ECO:0000313|Proteomes:UP000248873}; RN [1] {ECO:0000313|EMBL:PZU32151.1, ECO:0000313|Proteomes:UP000248873} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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-sourced RT 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-aspartyl- CC 4-phosphate. {ECO:0000256|HAMAP-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: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 AlphaFoldDB; A0A2W6W578; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000248873; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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|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 Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP- KW Rule:MF_02121}. FT DOMAIN 24..139 FT /note="Semialdehyde dehydrogenase NAD-binding" FT /evidence="ECO:0000259|SMART:SM00859" FT ACT_SITE 149 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT ACT_SITE 276 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 31..34 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 59..60 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 119 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 176 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 179..180 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 269 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 345 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="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 //