ID   DHAS_CORML              Reviewed;         344 AA.
AC   P0C1D9; P26511; Q46062;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd;
OS   Corynebacterium melassecola.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=41643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17965 / AS B-4821;
RX   MEDLINE=96099312; PubMed=8522535;
RA   Serebrijski I., Wojcik F., Reyes O., Leblon G.;
RT   "Multicopy suppression by asd gene and osmotic stress-dependent
RT   complementation by heterologous proA in proA mutants.";
RL   J. Bacteriol. 177:7255-7260(1995).
CC   -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate +
CC       NADP(+) = L-4-aspartyl phosphate + NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 2/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 2/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 2/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
CC       family.
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DR   EMBL; X82928; CAA58101.1; -; Genomic_DNA.
DR   PIR; S49978; S49978.
DR   HSSP; P00353; 1BRM.
DR   BRENDA; 1.2.1.11; 294761.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR   InterPro; IPR012080; Asp_semialdehyde_DH.
DR   InterPro; IPR005986; Asp_semialdehyde_DH_bac.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_C.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF000148; ASA_dh; 1.
DR   TIGRFAMs; TIGR01296; asd_B; 1.
DR   PROSITE; PS01103; ASD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; NADP; Oxidoreductase.
FT   CHAIN         1    344       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000236032.
FT   ACT_SITE    131    131       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   344 AA;  36226 MW;  3933583CE88E41F8 CRC64;
     MTTIAVVGAT GQVGQVMRTL LEERNFPADT VRFFASPRSA GRKIEFRGTE IEVEDITQAT
     EESLKDIDVA LFSAGGTASK QYAPLFAAAG ATVVDNSSAW RKDDEVPLIV SEVNPSDKDS
     LVKGIIANPN CTTMAAMPVL KPLHDAAGLV KLHVSSYQAV SGSGLAGVET LAKQVAAVGD
     HNVEFVHDGQ AADAGDVGPY VSPIAYNVLP FAGNLVDDGT FETDEEQKLR NESRKILGLP
     DLKVSGTCVR VPVFTGHTLT IHAEFDKAIT VEQAQEILGA ASGVKLVDVP TPLAAAGIDE
     SLVGRIRQDS TVDDNRGLVL VVSGDNLRKG AALNTIQIAE LLVK
//