ID   DHAS_BACSU              Reviewed;         346 AA.
AC   Q04797;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=BSU16750;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=93252813; PubMed=8098035;
RA   Chen N.-Y., Jiang S.-Q., Klein D.A., Paulus H.;
RT   "Organization and nucleotide sequence of the Bacillus subtilis
RT   diaminopimelate operon, a cluster of genes encoding the first three
RT   enzymes of diaminopimelate synthesis and dipicolinate synthase.";
RL   J. Biol. Chem. 268:9448-9465(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.
RX   MEDLINE=93347235; PubMed=8345520; DOI=10.1006/jmbi.1993.1403;
RA   Daniel R.A., Errington J.;
RT   "Cloning, DNA sequence, functional analysis and transcriptional
RT   regulation of the genes encoding dipicolinic acid synthetase required
RT   for sporulation in Bacillus subtilis.";
RL   J. Mol. Biol. 232:468-483(1993).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND TYR-146, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17218307; DOI=10.1074/mcp.M600464-MCP200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
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; L08471; AAA22383.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13548.1; -; Genomic_DNA.
DR   EMBL; Z22554; CAA80276.1; -; Genomic_DNA.
DR   PIR; F69590; F69590.
DR   RefSeq; NP_389557.1; -.
DR   PhosSite; Q04797; -.
DR   GeneID; 939654; -.
DR   GenomeReviews; AL009126_GR; BSU16750.
DR   KEGG; bsu:BSU16750; -.
DR   NMPDR; fig|224308.1.peg.1678; -.
DR   SubtiList; BG10783; asd.
DR   HOGENOM; Q04797; -.
DR   OMA; Q04797; LELWLCG.
DR   BioCyc; BSUB224308:BSU1676-MON; -.
DR   BioCyc; MetaCyc:MON-6564; -.
DR   BRENDA; 1.2.1.11; 150.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NADP;
KW   Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    346       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141361.
FT   ACT_SITE    130    130       Acyl-thioester intermediate (By
FT                                similarity).
FT   MOD_RES      98     98       Phosphoserine.
FT   MOD_RES     146    146       Phosphotyrosine.
FT   CONFLICT     42     42       S -> A (in Ref. 3; CAA80276).
FT   CONFLICT     77     77       S -> T (in Ref. 3; CAA80276).
SQ   SEQUENCE   346 AA;  37847 MW;  C3548164085143CD CRC64;
     MGRGLHVAVV GATGAVGQQM LKTLEDRNFE MDTLTLLSSK RSAGTKVTFK GQELTVQEAS
     PESFEGVNIA LFSAGGSVSQ ALAPEAVKRG AIVIDNTSAF RMDENTPLVV PEVNEADLHE
     HNGIIANPNC STIQMVAALE PIRKAYGLNK VIVSTYQAVS GAGNEAVKEL YSQTQAILNK
     EEIEPEIMPV KGDKKHYQIA FNAIPQIDKF QDNGYTFEEM KMINETKKIM HMPDLQVAAT
     CVRLPIQTGH SESVYIEIDR DDATVEDIKN LLKEAPGVTL QDDPSQQLYP MPADAVGKND
     VFVGRIRKDL DRANGFHLWV VSDNLLKGAA WNSVQIAESL KKLNLV
//