ID   DHAS_SALTY              Reviewed;         368 AA.
AC   P0A1F8; O30706;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=STM3539;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Galan J., Antoine G., Curtiss R. III;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
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; AF015781; AAB69392.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE008863; AAL22399.1; -; Genomic_DNA.
DR   RefSeq; NP_462440.1; -.
DR   HSSP; P00353; 1BRM.
DR   SMR; P0A1F8; 1-368.
DR   GeneID; 1255062; -.
DR   GenomeReviews; AE006468_GR; STM3539.
DR   KEGG; stm:STM3539; -.
DR   HOGENOM; P0A1F8; -.
DR   OMA; P0A1F8; IDGLCVR.
DR   BioCyc; STYP99287:STM3539-MON; -.
DR   BRENDA; 1.2.1.11; 2.
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; IPR012080; Asp_semialdehyde_DH.
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   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    368       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141373.
FT   ACT_SITE    136    136       Acyl-thioester intermediate (By
FT                                similarity).
FT   BINDING     136    136       Cysteine (covalent); in inhibited form
FT                                (By similarity).
SQ   SEQUENCE   368 AA;  40136 MW;  08BFB3E98029A677 CRC64;
     MKNVGFIGWR GMVGSVLMQR MVEERDFDAI RPVFFSTSQF GQAAPTFGDT STGTLQDAFD
     LDALKALDII VTCQGGDYTN EIYPKLRESG WQGYWIDAAS TLRMKDDAII ILDPVNQDVI
     TDGLNNGVKT FVGGNCTVSL MLMSLGGLFA HNLVDWVSVA TYQAASGGGA RHMRELLTQM
     GQLYGHVADE LATPSSAILD IERKVTALTR SGELPVDNFG VPLAGSLIPW IDKQLDNGQS
     REEWKGQAET NKILNTASVI PVDGLCVRVG ALRCHSQAFT IKLKKEVSIP TVEELLAAHN
     PWAKVVPNDR DITMRELTPA AVTGTLTTPV GRLRKLNMGP EFLSAFTVGD QLLWGAAEPL
     RRMLRQLA
//