ID   DHAS_VIBMI              Reviewed;         316 AA.
AC   Q60080;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 48.
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   Vibrio mimicus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M547;
RX   MEDLINE=95286501; PubMed=7768818;
RA   Karaolis D.K., Lan R., Reeves P.R.;
RT   "The sixth and seventh cholera pandemics are due to independent clones
RT   separately derived from environmental, nontoxigenic, non-O1 Vibrio
RT   cholerae.";
RL   J. Bacteriol. 177:3191-3198(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; U25067; AAC43377.1; -; Genomic_DNA.
DR   BRENDA; 1.2.1.11; 38719.
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; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; NADP; Oxidoreductase.
FT   CHAIN         1   >316       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141395.
FT   ACT_SITE    132    132       Acyl-thioester intermediate (By
FT                                similarity).
FT   NON_TER     316    316
SQ   SEQUENCE   316 AA;  35139 MW;  5E27AFAD9BC63A11 CRC64;
     MSQQFNVAIF GATGAVGETM LEVLQEREFP VDELFLLASE RSEGKTYRFN GKTVRVQNVE
     EFDWSQVHIA LFSAGGELSA HWAPIRAEAG VVVIDNTSHF RYDYDIPLVI PEVNPEAIAE
     FRNRNIIANP NCSTIQMLVA LKPIYDAVGI ERINVTTYQS VSGAGKAGID ELAGQTAKLL
     NGYPAETNTF SQQIAFNCIP QIDQFMDNGY TKEEMKMVWE TQKIFNDPSI MVNPTCVRVP
     VFYGHAEAVH VETRAPIDAE QVMDMLDQTD GIELFRGADF PTQVRDAGGK DHVLVGRVRN
     DISHHSGVNL WVVADN
//