ID   DHAS_BUCAP              Reviewed;         371 AA.
AC   Q8K9B5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 42.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=BUsg_433;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67976.1; -; Genomic_DNA.
DR   RefSeq; NP_660765.1; -.
DR   HSSP; P00353; 1BRM.
DR   GeneID; 1005553; -.
DR   GenomeReviews; AE013218_GR; BUsg_433.
DR   KEGG; bas:BUsg433; -.
DR   HOGENOM; Q8K9B5; -.
DR   BioCyc; BAPH198804:BUSG433-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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000319; Asp-semialdehyde_DHase_CS.
DR   InterPro; IPR011534; Asp_ADH_proteob.
DR   InterPro; IPR012080; Asp_semialdehyde_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR000534; Semialdehyde_DHase_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DHase_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   PIRSF; PIRSF000148; ASA_dh; 1.
DR   TIGRFAMs; TIGR01745; asd_gamma; 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    371       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141364.
FT   ACT_SITE    137    137       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   371 AA;  41785 MW;  079A0E1BEAE68318 CRC64;
     MTKSVGIIGW RGMVGSVLLK RMQEENDFSK IIPYFFSTSQ SGQDGPIINN ILSKNLKDAY
     NINLLQEMDI IITCQGSSYT EKIYPKLRNN NWQGYWIDAA STLRMEKDAT IILDPVNLNV
     INNALDKGIK TFVGGNCTVS LMLMALGGLF VNNLIDWVFV STYQAASGAG SRYVIELLKQ
     MGSLYNVVSK DLLDKSYSVL DIEKKVTQES RSKNFPLENF SVPLATSLIP WIDVEMKNGQ
     SREEWKGQAE TNKILNLKKK VLIDGTCVRI SSIRCHSQSF LIKLNKDISL ENIKKIIVNH
     NQWVDVIPNN MQKTLCNLTP SAVTDTLNIP IGRLRKLNID DRYLSAFTVG DQLLWGAAEP
     LRRMLNLLVN I
//