ID D0U4N0_9GAMM Unreviewed; 341 AA. AC D0U4N0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 13-SEP-2023, entry version 57. 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=Sup05_1334 {ECO:0000313|EMBL:EEZ80090.1}, SUP05_FGYC65E210007 GN {ECO:0000313|EMBL:ACX30562.1}; OS uncultured Candidatus Thioglobus sp. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus; OC environmental samples. OX NCBI_TaxID=655186 {ECO:0000313|EMBL:ACX30562.1}; RN [1] {ECO:0000313|EMBL:EEZ80090.1, ECO:0000313|Proteomes:UP000009383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19900896; DOI=10.1126/science.1175309; RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., Tringe S.G., RA Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic dead RT zones."; RL Science 326:578-582(2009). RN [2] {ECO:0000313|EMBL:ACX30562.1} RP NUCLEOTIDE SEQUENCE. RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., Tringe S.G., RA Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oxygen RT minimum zones."; RL Science 326:578-582(2009). 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 --------------------------------------------------------------------------- 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; GQ351269; ACX30562.1; -; Genomic_DNA. DR EMBL; GG730003; EEZ80090.1; -; Genomic_DNA. DR AlphaFoldDB; D0U4N0; -. DR STRING; 655186.Sup05_1334; -. DR PATRIC; fig|655186.3.peg.620; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000009383; 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 NCBIfam; TIGR01296; asd_B; 1. 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. 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 Reference proteome {ECO:0000313|Proteomes:UP000009383}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP- KW Rule:MF_02121}. FT DOMAIN 6..121 FT /note="Semialdehyde dehydrogenase NAD-binding" FT /evidence="ECO:0000259|SMART:SM00859" FT ACT_SITE 132 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT ACT_SITE 246 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 13..16 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 41..42 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 101 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 162..163 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 239 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" FT BINDING 320 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121" SQ SEQUENCE 341 AA; 37274 MW; 79A54BF5014C0711 CRC64; MSKKYNVAVV GATGAVGETI LSILEQRNFP IDNLYPLASA NSAGKKVFCQ GKSWTVQDLD TFDFSQAQIG LFSAGGNISE KYAPIAAEAG CVVIDNTAHF RRDEGIPLVV PEVNPHAISG YTKRNIIANP NCSTIQMLVA LKPIYDAVGI ERINVATYQA VSGSGKEAIS ELIEQTTKLL GGNTEVDVEV YPKQIAFNVI PHIDVFQDNG YTKEEMKMVW ETQKIFEDDN ILVNPTAVRV PVIYGHSEAI NIETKTKITA AEAVEVLSKA NGVTVLDKRE DGGYATPFVE ATNHDDTFVS RIREDISHEK GLNLWVVSDN IRKGAALNSI QIAEILIEEY L //