ID   DHAS_BUCAI              Reviewed;         371 AA.
AC   P57523;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=BU448;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13146.1; -; Genomic_DNA.
DR   RefSeq; NP_240260.1; NC_002528.1.
DR   RefSeq; WP_010896121.1; NC_002528.1.
DR   AlphaFoldDB; P57523; -.
DR   SMR; P57523; -.
DR   STRING; 107806.10039112; -.
DR   EnsemblBacteria; BAB13146; BAB13146; BAB13146.
DR   KEGG; buc:BU448; -.
DR   PATRIC; fig|107806.10.peg.458; -.
DR   eggNOG; COG0136; Bacteria.
DR   HOGENOM; CLU_066397_0_0_6; -.
DR   OMA; MFDVPDE; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000001806; 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   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   PANTHER; PTHR46278:SF4; PTHR46278:SF4; 1.
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; TIGR01745; asd_gamma; 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..371
FT                   /note="Aspartate-semialdehyde dehydrogenase"
FT                   /id="PRO_0000141363"
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;  41473 MW;  6AAAF3A90C1B13B4 CRC64;
     MIKIVGLVGW RGMVGSVLLK RMQEENDFSR IKPVFFSTSQ FGQDGPIINN ISYNILENAY
     NIDVLKEMDI IITCQGGSYT KEIYPTLRKN GWKGYWIDAA SNLRMKNDSV IILDPVNYNV
     IEDSINKGIR TFVGGNCTIS LMLMSLGGLF QTELVEWIAV STYQAASGAG ARHMIELLNQ
     MGILYKSVET DLLKGSHSIL SIEDKVTKIS RSVNFPVKNF SVPLAASLIP WIDTEMSNGQ
     SREEWKGQAE TNKILGTKDT ILIDGTCVRI GSLRCHSQSF VIKLKKDVSL EDIEEIIRNH
     NKWVDVIPNS IQDTLLKLTP SSVTGTLNIP IGRLRKLNMG KKYLSAFTVG DQLLWGAAEP
     LRRMLNILIN I