ID   DHAS_PROMA              Reviewed;         343 AA.
AC   P49420;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=Pro_1814;
OS   Prochlorococcus marinus.
OC   Bacteria; Cyanobacteria; Prochlorophytes; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=1219;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   MEDLINE=22810154; PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F.,
RA   Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B.,
RA   Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P.,
RA   Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120,
RT   a nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 238-343.
RC   STRAIN=SARG / CCMP1375 / SS120;
RA   Lorenz M., Boerner T., Hess W.R.;
RT   "Molecular cloning and characterization of a dihydrodipicolinate
RT   synthase (DHDPS) gene from the photoautotrophic prokaryote
RT   Prochlorococcus marinus CCMP 1375 (Prochlorophyta).";
RL   Endocyt. Cell Res. 11:59-68(1995).
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; AE017126; AAQ00858.1; -; Genomic_DNA.
DR   EMBL; Z68126; CAA92210.1; -; Genomic_DNA.
DR   RefSeq; NP_876205.1; -.
DR   GeneID; 1463197; -.
DR   GenomeReviews; AE017126_GR; Pro_1814.
DR   KEGG; pma:Pro1814; -.
DR   HOGENOM; P49420; -.
DR   OMA; P49420; LELWLCG.
DR   BioCyc; PMAR167539:PRO_1814-MON; -.
DR   BRENDA; 1.2.1.11; 141456.
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    343       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141386.
FT   ACT_SITE    137    137       Acyl-thioester intermediate (By
FT                                similarity).
FT   CONFLICT    238    238       T -> P (in Ref. 2; CAA92210).
FT   CONFLICT    244    246       VPV -> GPA (in Ref. 2; CAA92210).
FT   CONFLICT    253    254       SI -> AT (in Ref. 2; CAA92210).
FT   CONFLICT    257    260       EFAE -> VFSG (in Ref. 2; CAA92210).
FT   CONFLICT    269    270       KI -> QN (in Ref. 2; CAA92210).
FT   CONFLICT    286    286       N -> D (in Ref. 2; CAA92210).
FT   CONFLICT    297    297       K -> Q (in Ref. 2; CAA92210).
FT   CONFLICT    305    305       I -> K (in Ref. 2; CAA92210).
FT   CONFLICT    324    324       I -> K (in Ref. 2; CAA92210).
SQ   SEQUENCE   343 AA;  37557 MW;  E20036130DB7403B CRC64;
     MTLQKPFPDR PLTLAVLGSS GAVGAEILKI LEERSFPIRE LRLLASERSA GQVQFFKGED
     LVVKKVSPEG FEDVDLVLAS AGGSISRKWR KVINSAGAVI VDNSNAYRME PDVPLVVPEV
     NPSQVFTHKG LIANPNCTTI LLALVLAPLS AQLPIKRVVV STYQSASGAG ARAMNELKQL
     SQDVLNGNIP KSEILPYSLA FNLFLHNSPL QSNNYCEEEM KMINETRKIL NQSELAITAT
     CVRVPVLRAH SESINIEFAE PFPVEEARKI LSNASGIKLL EDIQMNRFPM PIDVTGKDDI
     AVGRIRQDLS NPKALELWLC GDQIRKGAAL NAIQIAELLL TRS
//