ID   DHAS_ARCFU              Reviewed;         343 AA.
AC   O28766;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=AF_1506;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(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; AE000782; AAB89738.1; -; Genomic_DNA.
DR   PIR; A69438; A69438.
DR   RefSeq; NP_070335.1; -.
DR   GeneID; 1484733; -.
DR   GenomeReviews; AE000782_GR; AF_1506.
DR   KEGG; afu:AF1506; -.
DR   NMPDR; fig|224325.1.peg.1496; -.
DR   TIGR; AF_1506; -.
DR   HOGENOM; O28766; -.
DR   OMA; O28766; TIGAVIS.
DR   BioCyc; AFUL224325:AF_1506-MON; -.
DR   BRENDA; 1.2.1.11; 7576.
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    343       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141396.
FT   ACT_SITE    148    148       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   343 AA;  37697 MW;  A6C9F5D045CBFC21 CRC64;
     MRYSVGVLGA TGMVGQKFIQ MLAEHPWFKL TSLAASERRV GKKYGEEVDW IVSREVPDIA
     KDIEMVPMDP KHVDADIVFS ALPSDIAREV EPKFAEAGFV VASNASAYRM AEDVPLVIPE
     VNPEHLGLIE VQKKNRGWDG FIVTNPNCTT IVLVLSLKPL MDLGLRTVRV ASMQALSGAG
     YPGVPSLAIT DNVIPFIKGE EDKVEEEPLK LLGKFNGRKI EFADIKVSAS CHRVPVIDGH
     TEAVWVEFDR EVSVEEAKAA FESLKPLDLP TSPEKVIIVR EEPDRPQPRL DRDAGNGMSI
     TVGRIRKDGE RGLKYIVLGH NTVRGAAGAS ILNAELMIKE KII
//