ID   DHAS_ACTPL              Reviewed;         286 AA.
AC   Q44151;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
DE   Flags: Fragment;
GN   Name=asd;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S 4074 / Serotype 1;
RA   Helie M.C., Sirois M., Ouellet C., Boissinot M.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U51440; AAB02815.1; -; Genomic_DNA.
DR   HSSP; P00353; 1BRM.
DR   SMR; Q44151; 1-286.
DR   BRENDA; 1.2.1.11; 257522.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR   InterPro; IPR011534; Asp_ADH_proteob.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_C.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   TIGRFAMs; TIGR01745; asd_gamma; 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   >286       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141358.
FT   ACT_SITE    136    136       Acyl-thioester intermediate (By
FT                                similarity).
FT   NON_TER     286    286
SQ   SEQUENCE   286 AA;  31167 MW;  FA5881D57000279F CRC64;
     MQNVGFIGWR GMVGSVLMDR MVQENDFANI NPIFFTTSQA GQKAPVFAGK DAGELKNAFD
     IEELKKLDII VTCQGGDYTN EVYPKLKATG WNGYWIDAAS ALRMEKDAII VLDPVNQHVI
     SEGLKNGIKT FVGGNCTVSL MLMAIGGLFE KDLVEWVSVA TYQAASGAGA KNMRELLSQM
     GELEASVKAE LANPASSILE IERKVTAKMR EDSFPTDNFG APLAGSLIPW IDKLLESGQT
     KEEWKGYAET NKILGLSDNP IPVDGLCVRI GALRCHSQAF TIKLKK
//