ID   DHAS_CORGL              Reviewed;         344 AA.
AC   P0C1D8; P26511; Q46062;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=Cgl0252, cg0307;
OS   Corynebacterium glutamicum (Brevibacterium flavum).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   MEDLINE=91094767; PubMed=1980002; DOI=10.1007/BF00262424;
RA   Kalinowski J., Bachmann B., Thierbach G., Puehler A.;
RT   "Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent
RT   to the aspartate beta-semialdehyde dehydrogenase gene asd in
RT   Corynebacterium glutamicum.";
RL   Mol. Gen. Genet. 224:317-324(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RA   Nakagawa S.;
RT   "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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; X57226; CAA40504.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB97645.1; -; Genomic_DNA.
DR   EMBL; BX927148; CAF18823.1; -; Genomic_DNA.
DR   PIR; S49978; S49978.
DR   RefSeq; NP_599505.1; -.
DR   RefSeq; YP_224552.1; -.
DR   HSSP; P00353; 1BRM.
DR   World-2DPAGE; 0001:P0C1D8; -.
DR   PRIDE; P0C1D8; -.
DR   GeneID; 1021315; -.
DR   GeneID; 3345564; -.
DR   GenomeReviews; BA000036_GR; Cgl0252.
DR   GenomeReviews; BX927147_GR; cg0307.
DR   KEGG; cgb:cg0307; -.
DR   KEGG; cgl:NCgl0248; -.
DR   HOGENOM; P0C1D8; -.
DR   OMA; P0C1D8; LELWLCG.
DR   BioCyc; CGLU196627-1:CG0307-MON; -.
DR   BRENDA; 1.2.1.11; 812.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    344       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141368.
FT   ACT_SITE    131    131       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   344 AA;  36212 MW;  38771D3DACCB41F8 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 VDQAQEILGA ASGVKLVDVP TPLAAAGIDE
     SLVGRIRQDS TVDDNRGLVL VVSGDNLRKG AALNTIQIAE LLVK
//