ID DHAS_BUCAP Reviewed; 371 AA. AC Q8K9B5; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; DE Short=ASA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; DE Short=ASADH {ECO:0000255|HAMAP-Rule:MF_02121}; DE EC=1.2.1.11 {ECO:0000255|HAMAP-Rule:MF_02121}; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; GN Name=asd {ECO:0000255|HAMAP-Rule:MF_02121}; GN OrderedLocusNames=BUsg_433; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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:0000255|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:0000255|HAMAP-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:0000255|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. {ECO:0000255|HAMAP- CC Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family. CC {ECO:0000255|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; AE013218; AAM67976.1; -; Genomic_DNA. DR RefSeq; WP_011053943.1; NC_004061.1. DR AlphaFoldDB; Q8K9B5; -. DR SMR; Q8K9B5; -. DR STRING; 198804.BUsg_433; -. DR GeneID; 75258685; -. DR KEGG; bas:BUsg_433; -. DR eggNOG; COG0136; Bacteria. DR HOGENOM; CLU_066397_0_0_6; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000000416; Chromosome. 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; 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 NCBIfam; TIGR01745; asd_gamma; 1. DR PANTHER; PTHR46278:SF4; 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 PROSITE; PS01103; ASD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; Lysine biosynthesis; KW Methionine biosynthesis; NADP; Oxidoreductase; Threonine biosynthesis. FT CHAIN 1..371 FT /note="Aspartate-semialdehyde dehydrogenase" FT /id="PRO_0000141364" FT ACT_SITE 137 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT ACT_SITE 276 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 11..14 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 38..39 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 75 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 104 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 167..168 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 243 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 246 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 269 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 352 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" SQ SEQUENCE 371 AA; 41785 MW; 079A0E1BEAE68318 CRC64; MTKSVGIIGW RGMVGSVLLK RMQEENDFSK IIPYFFSTSQ SGQDGPIINN ILSKNLKDAY NINLLQEMDI IITCQGSSYT EKIYPKLRNN NWQGYWIDAA STLRMEKDAT IILDPVNLNV INNALDKGIK TFVGGNCTVS LMLMALGGLF VNNLIDWVFV STYQAASGAG SRYVIELLKQ MGSLYNVVSK DLLDKSYSVL DIEKKVTQES RSKNFPLENF SVPLATSLIP WIDVEMKNGQ SREEWKGQAE TNKILNLKKK VLIDGTCVRI SSIRCHSQSF LIKLNKDISL ENIKKIIVNH NQWVDVIPNN MQKTLCNLTP SAVTDTLNIP IGRLRKLNID DRYLSAFTVG DQLLWGAAEP LRRMLNLLVN I //