ID   DHAS_RICFE              Reviewed;         338 AA.
AC   Q4UM57;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=RF_0512;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61363.1; -; Genomic_DNA.
DR   RefSeq; YP_246528.1; -.
DR   GeneID; 3401174; -.
DR   GenomeReviews; CP000053_GR; RF_0512.
DR   KEGG; rfe:RF_0512; -.
DR   NMPDR; fig|315456.3.peg.346; -.
DR   HOGENOM; Q4UM57; -.
DR   OMA; Q4UM57; KPLDNEI.
DR   BioCyc; RFEL315456:RF_0512-MON; -.
DR   BRENDA; 1.2.1.11; 297363.
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; 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_0000280939.
FT   ACT_SITE    132    132       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   338 AA;  37174 MW;  2E74BE813861FBD5 CRC64;
     MTKKYNIAVI GATGNVGRET LNILAERNFP VNKIYAIASD NSIGREISYG EKILKISSLT
     NLNFDDIDIA FFCAGSEVSK EFVPKATASS CVVIDKSSLF RVDNQVPLIV PEVNLSTLTE
     FNTKNIIANP NCIVIPLAVA LKPLDNEIKI KRVVISTYQS VSGAGKAGMD ELYDQTKSKY
     VFGENDPKKF PKQITFNLFP HIGDLNKDGY TSEEAKIAFE LNKIMGNHFK ASVTSVRVPV
     FIGHSISVNI EFNDKMDANI AEEILQDADG IVTISNNNDL AYISPVEVVG EDAVYVSRIR
     NDVSKPNAIN LWITCDNLRK GAALNSVQIA EELINNYL
//