ID   DHAS_HELPJ              Reviewed;         346 AA.
AC   Q9ZK28;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=jhp_1114;
OS   Helicobacter pylori J99 (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=99120557; PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G.,
RA   Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C.,
RA   Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F.,
RA   Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human
RT   gastric pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD06695.1; -; Genomic_DNA.
DR   PIR; C71847; C71847.
DR   RefSeq; NP_223831.1; -.
DR   HSSP; P00353; 1BRM.
DR   GeneID; 889756; -.
DR   GenomeReviews; AE001439_GR; jhp_1114.
DR   KEGG; hpj:jhp1114; -.
DR   NMPDR; fig|85963.1.peg.1109; -.
DR   HOGENOM; Q9ZK28; -.
DR   OMA; Q9ZK28; VFYGHAE.
DR   BioCyc; HPYL85963:JHP1114-MON; -.
DR   BRENDA; 1.2.1.11; 295085.
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; Complete proteome;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    346       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141377.
FT   ACT_SITE    131    131       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   346 AA;  38131 MW;  76A7A7C3C4EF6287 CRC64;
     MKTYNVAIVG ASGAVGQELI KGLENSFFPI KKFVPLASAR SAGKKIRAFN KDYEILETTH
     EVFEKEEIDI AFFSAGGSVS EEFAISASKT ALVIDNTSFF RLNKDVPLVV PEINAQEIFN
     APLNIIANPN CSTIQMTQIL NPLHLHFKIK SVIVSTYQAV SGAGNKGIES LKNELKTALE
     HLEKDPAIDL NQVLQAGAFA YPIAFNAIAH IDTFKENGYT KEELKMVHET HKIMGVDFPI
     SATCVRVPVL RSHSESLSIA FEKEFDLKEV YEVLKNAPSV VVCDDPSHNL YPTPLKASHT
     DSVFIGRLRK DLFDKKTLHG FCVADQLRVG AATNALKIAL HYIKNA
//