ID   DHAS_METTH              Reviewed;         347 AA.
AC   O26890;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=MTH_799;
OS   Methanobacterium thermoautotrophicum.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Delta H;
RX   MEDLINE=98037514; PubMed=9371463;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: This enzyme catalyzes the second step in the common
CC       metabolic pathway to synthesize Thr and Met from Asp.
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   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
CC       family.
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DR   EMBL; AE000666; AAB85299.1; -; Genomic_DNA.
DR   PIR; E69206; E69206.
DR   RefSeq; NP_275938.1; -.
DR   GeneID; 1471207; -.
DR   GenomeReviews; AE000666_GR; MTH_799.
DR   KEGG; mth:MTH799; -.
DR   NMPDR; fig|187420.1.peg.793; -.
DR   HOGENOM; O26890; -.
DR   OMA; O26890; GHTECIS.
DR   BioCyc; MTHE187420:MTH799-MON; -.
DR   BRENDA; 1.2.1.11; 270.
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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR   InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR   InterPro; IPR012080; Asp_semialdehyde_DH.
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; TIGR00978; asd_EA; 1.
DR   PROSITE; PS01103; ASD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Methionine biosynthesis;
KW   NADP; Oxidoreductase; Threonine biosynthesis.
FT   CHAIN         1    347       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141398.
FT   ACT_SITE    147    147       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   347 AA;  38031 MW;  F0CCFA7D4B3531D3 CRC64;
     MVNVGVLGAT GMVGQRFIQM LDKHPEFELT TLAASSRSAG KPYGEVANWY LDCEMPESVR
     DMEVVETDPS AVGDVDILFS ALPADVARKV EPKFAEKYIV ASNASAMRME PDVPLVIPEV
     NPEFLDLIEV QQRRRGWDGF IVTNPNCSTI ALTLTLKPIY DAYTIKRVYV STMQAVSGAG
     YNGVPSMAIL DNLVPFIGGE EEKIETETLH LLGELDEGVV KPASFGVSAS CHRVPVVDGH
     TEAVFIELDD EFDIDDVREA MDKFRGLPQK LGLHSAPEKP VVVRDEENRP QPRMDRDMDG
     GMAVTVGRLR EDAAFKNSLR YVLVGHNTVR GAAGASILNA ELINEIL
//