ID   D3DYW9_METRM            Unreviewed;       349 AA.
AC   D3DYW9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   11-JUL-2012, entry version 22.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
DE   AltName: Full=Aspartate-beta-semialdehyde dehydrogenase;
GN   Name=asd; OrderedLocusNames=mru_1669;
OS   Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM
OS   13430 / M1) (Methanobacterium ruminantium).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=634498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / M1;
RX   PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA   Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA   Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA   Janssen P.H., Dey D., Attwood G.T.;
RT   "The genome sequence of the rumen methanogen Methanobrevibacter
RT   ruminantium reveals new possibilities for controlling ruminant methane
RT   emissions.";
RL   PLoS ONE 5:E8926-E8926(2010).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC       semialdehyde (L-ASA) by the reductive dephosphorylation of L-
CC       aspartyl-4-phosphate (By similarity).
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; (S)-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; CP001719; ADC47519.1; -; Genomic_DNA.
DR   RefSeq; YP_003424411.1; NC_013790.1.
DR   GeneID; 8771331; -.
DR   GenomeReviews; CP001719_GR; mru_1669.
DR   KEGG; mru:mru_1669; -.
DR   HOGENOM; HOG000013358; -.
DR   KO; K00133; -.
DR   OMA; GAGYNGV; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:HAMAP.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:HAMAP.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   HAMAP; MF_02121; ASADH; 1; -.
DR   InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR   InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR   InterPro; IPR012080; Asp_semialdehyde_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF000148; ASA_dh; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   TIGRFAMs; TIGR00978; Asd_EA; 1.
DR   PROSITE; PS01103; ASD; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis;
KW   Methionine biosynthesis; NADP; Oxidoreductase; Threonine biosynthesis.
FT   NP_BIND      10     13       NADP (By similarity).
FT   NP_BIND      37     38       NADP (By similarity).
FT   NP_BIND     178    179       NADP (By similarity).
FT   NP_BIND     328    329       NADP (By similarity).
FT   ACT_SITE    148    148       Acyl-thioester intermediate (By
FT                                similarity).
FT   ACT_SITE    241    241       Proton acceptor (By similarity).
FT   BINDING     109    109       Phosphate (By similarity).
FT   BINDING     175    175       Substrate (By similarity).
FT   BINDING     201    201       Substrate (By similarity).
FT   BINDING     204    204       Phosphate (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
SQ   SEQUENCE   349 AA;  38336 MW;  30B76E17D60ABB69 CRC64;
     MVKVGVLGAT GMVGQRFIQL LADHPDFEIA ALAASSRSAG KKYEDATTWY MNDEMPESVR
     DIKVIETDPA HMDKDVEIVF SSLPADFAAK VEPEYAKDFV VASNASAMRM KKDIPLVIPE
     VNPQFLDMIE AQQKNNNWDG FIVTNPNCST IALTLTLKPI YDNFNINRIY VSTMQAVSGA
     GYNGVPSMAI LDNLVPYIGG EEEKMESETL HLLGSLDGDE VVPANFSLSA SCHRVPVIDG
     HTEAVFVELD EEADIDKIKK TMADFRGLPQ ELGLHSAPEQ PVIVKEEDDR PQPRMDRMAY
     GGMAATVGRL RKDQAFDNSF KYVLVGHNTI RGAAGASILN AELINKQIL
//