ID   DHAS_RICPR              Reviewed;         338 AA.
AC   Q9ZDL2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-NOV-2008, entry version 47.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=RP316;
OS   Rickettsia prowazekii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=782;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   MEDLINE=99039499; PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O.,
RA   Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K.,
RA   Eriksson A.-S., Winkler H.H., Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(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; AJ235271; CAA14776.1; -; Genomic_DNA.
DR   PIR; F71687; F71687.
DR   RefSeq; NP_220699.1; -.
DR   GeneID; 883494; -.
DR   GenomeReviews; AJ235269_GR; RP316.
DR   KEGG; rpr:RP316; -.
DR   HOGENOM; Q9ZDL2; -.
DR   BioCyc; RPRO272947:RP316-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP 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_DHase_CS.
DR   InterPro; IPR012080; Asp_semialdehyde_DHase.
DR   InterPro; IPR005986; Asp_semialdehyde_DHase_bac.
DR   InterPro; IPR000534; Semialdehyde_DHase_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DHase_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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    338       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141388.
FT   ACT_SITE    132    132       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   338 AA;  37668 MW;  61E4CE8DDAD7A20E CRC64;
     MTKKYNIAVI GATGNVGRET LNILAERHFP INKIYAIASD NSLGREVRFG EKILHINSIK
     IFNFHDIEIA FFCAGSNVSK EFIPKATSCN CIVIDKTSLF RADNQVPLIV PEVNLSTLKE
     FNTKNIIANP NCIVIPLVVV LKPLDNEIKI KRVVISTYQS VSGAGKAGMD ELYNQTKSKY
     VFRENNPKKF PKQIAFNLFP YIGDLNKDGY TSEETKIAFE LNKIMGNHFK TSVTSVRVPV
     FIGHAISVNI EFSDKIYAKD VEEILQDADG IVTISNNNGL AYISPIEVVG EDAVYVSRIR
     NDLSKDNTIN LWITCDNLRK GAALNSVQIA EALINNYL
//