ID   DHAS_AQUAE              Reviewed;         340 AA.
AC   O67716;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=aq_1866;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07674.1; -; Genomic_DNA.
DR   PIR; B70461; B70461.
DR   RefSeq; NP_214284.1; -.
DR   GeneID; 1193523; -.
DR   GenomeReviews; AE000657_GR; aq_1866.
DR   KEGG; aae:aq_1866; -.
DR   NMPDR; fig|224324.1.peg.1299; -.
DR   HOGENOM; O67716; -.
DR   OMA; O67716; YLFASKR.
DR   BioCyc; AAEO224324:AQ_1866-MON; -.
DR   BRENDA; 1.2.1.11; 189781.
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; Complete proteome;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    340       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141359.
FT   ACT_SITE    131    131       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   340 AA;  37799 MW;  5B2172ABA2AC190D CRC64;
     MGYRVAIVGA TGEVGRTFLK VLEERNFPVD ELVLYASERS EGKVLTFKGK EYTVKALNKE
     NSFKGIDIAL FSAGGSTSKE WAPKFAKDGV VVIDNSSAWR MDPDVPLVVP EVNPEDVKDF
     KKKGIIANPN CSTIQMVVAL KPIYDKAGIK RVVVSTYQAV SGAGAKAIED LKNQTKAWCE
     GKEMPKAQKF PHQIAFNALP HIDVFFEDGY TKEENKMLYE TRKIMHDENI KVSATCVRIP
     VFYGHSESIS METEKEISPE EAREVLKNAP GVIVIDNPQN NEYPMPIMAE GRDEVFVGRI
     RKDRVFEPGL SMWVVADNIR KGAATNAVQI AELLVKEGLI
//