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DHAS_MYCSM
ID   DHAS_MYCSM              Reviewed;         346 AA.
AC   P41404;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 102.
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};
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692;
RX   PubMed=7910936; DOI=10.1111/j.1365-2958.1994.tb00342.x;
RA   Cirillo J.D., Weisbrod T.R., Pascopella L., Bloom B.R., Jacobs W.R. Jr.;
RT   "Isolation and characterization of the aspartokinase and aspartate
RT   semialdehyde dehydrogenase operon from mycobacteria.";
RL   Mol. Microbiol. 11:629-639(1994).
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}.
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DR   EMBL; Z17372; CAA78986.1; -; Genomic_DNA.
DR   PIR; S42423; S42423.
DR   AlphaFoldDB; P41404; -.
DR   SMR; P41404; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
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   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   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.
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..346
FT                   /note="Aspartate-semialdehyde dehydrogenase"
FT                   /id="PRO_0000141382"
FT   ACT_SITE        131
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT   ACT_SITE        257
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT   BINDING         10..13
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         98
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT   BINDING         161..162
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT   BINDING         228
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT   BINDING         326
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
SQ   SEQUENCE   346 AA;  36559 MW;  F4E552F2B193A27F CRC64;
     MVNIGVVGAT GQGRQVMRNL LEQRNFPATS VRFFASPRSE GKKLTFRGQE IEVENAETAD
     PSGLDIALFS AGATMSRVQA PRFAEAGVIV VDNSSAFRKD PDVPLVVSEV NFDRDVRGKK
     LAKGIIANPN CTTMAAMPVL KPLHEEAGLQ RLIVSSYQAV SGSGIAGVEE LAGQARPVID
     GVEQLVHDGS ALQYPAPNKY VAPIAFNIVP LAGNYVDDGS GETDEDQKLR NESRKILGIP
     ELLVSGTCVR VPVFSGHSLS INAEFSQPIS VERTKELLSA AAGVKLVDVP TPLAAAGIDD
     CLVGRIRQDP GVPDGRGLAL FVSGDNLRKG AALNTIQIAE LLAADL
 
 
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