ID DHAS_STRMU Reviewed; 358 AA. AC P10539; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2002, sequence version 2. DT 02-SEP-2026, entry version 163. 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}; OrderedLocusNames=SMU_989; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2434499; DOI=10.1016/s0021-9258(18)61509-1; RA Cardineau G.A., Curtiss R. III; RT "Nucleotide sequence of the asd gene of Streptococcus mutans. RT Identification of the promoter region and evidence for attenuator-like RT sequences preceding the structural gene."; RL J. Biol. Chem. 262:3344-3353(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.; RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental RT pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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 + phosphate + NADP(+) = 4-phospho- CC L-aspartate + NADPH + H(+); 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; J02667; AAA26850.1; -; Genomic_DNA. DR EMBL; AE014133; AAN58690.1; -; Genomic_DNA. DR PIR; A29137; A29137. DR RefSeq; WP_002263802.1; NC_004350.2. DR AlphaFoldDB; P10539; -. DR MDposit; P10539; -. DR SMR; P10539; -. DR STRING; 210007.SMU_989; -. DR GeneID; 93859500; -. DR KEGG; smu:SMU_989; -. DR PATRIC; fig|210007.7.peg.882; -. DR eggNOG; COG0136; Bacteria. DR HOGENOM; CLU_049966_0_1_9; -. DR OrthoDB; 9805684at2; -. DR PhylomeDB; P10539; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000002512; 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:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd18131; ASADH_C_bac_euk_like; 1. DR CDD; cd02316; VcASADH2_like_N; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. 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; 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 NCBIfam; NF011456; PRK14874.1; 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. DR PROSITE; PS01103; ASD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; Lysine biosynthesis; KW Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome; KW Threonine biosynthesis. FT CHAIN 1..358 FT /note="Aspartate-semialdehyde dehydrogenase" FT /id="PRO_0000141392" FT ACT_SITE 128 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT ACT_SITE 252 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 39..40 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 99 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 155 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 158..159 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 223 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT BINDING 325 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121" FT CONFLICT 64 FT /note="G -> A (in Ref. 1; AAA26850)" FT /evidence="ECO:0000305" FT CONFLICT 190 FT /note="L -> F (in Ref. 1; AAA26850)" FT /evidence="ECO:0000305" FT CONFLICT 242 FT /note="T -> H (in Ref. 1; AAA26850)" FT /evidence="ECO:0000305" FT CONFLICT 301 FT /note="Missing (in Ref. 1; AAA26850)" FT /evidence="ECO:0000305" FT CONFLICT 335..340 FT /note="VQIAES -> IITANR (in Ref. 1; AAA26850)" FT /evidence="ECO:0000305" SQ SEQUENCE 358 AA; 38903 MW; 11F5E4AD52C1A40B CRC64; MGYTVAIVGA TGAVGTRMIQ QLEQSTLPVD KVRLLSSSRS AGKVLQYKDQ DVTVELTTKD SFEGVDIALF SAGGSVSAKF APYAVKAGAV VVDNTSHFRQ NPDVPLVVPE VNAYAMDAHN GIIACPNCST IQMMVALEPI RQKWGLSRVI VSTYQAVSGA GQSAINETVR EIKEVVNDGV DPKAVHADIL PSGGDKKHYP IAFNALAQID VFTDNDYTYE EMKMTNETKK IMEEPELPVS ATCVRVPILF SHSEAVYIET KDVAPIEEVK AAIAAFPGAV LEDDIKHQIY PQAANAVGSR ETFVGRIRKD LDIENGIHMW VVSDNLLKGA AWNSVQIAES LHERGLVRST SELKFELK //