ID   ASPD_METMA              Reviewed;         271 AA.
AC   Q8PV99;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Probable L-aspartate dehydrogenase;
DE            EC=1.4.1.21;
GN   Name=nadX; OrderedLocusNames=MM_2072;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   MEDLINE=22120827; PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC       dehydrogenation of L-aspartate to iminoaspartate (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate
CC       + NH(3) + NAD(P)H.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis;
CC       iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.
CC   -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous
CC       solution and can decompose to oxaloacetate and ammonia (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
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DR   EMBL; AE008384; AAM31768.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_634096.1; -.
DR   HSSP; Q9X1X6; 1J5P.
DR   GeneID; 1480414; -.
DR   GenomeReviews; AE008384_GR; MM_2072.
DR   KEGG; mma:MM_2072; -.
DR   NMPDR; fig|192952.1.peg.2072; -.
DR   HOGENOM; Q8PV99; -.
DR   BioCyc; MMAZ192952:MM2072-MON; -.
DR   BRENDA; 1.4.1.21; 261165.
DR   GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:HAMAP.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-N...; IEA:HAMAP.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006742; P:NADP catabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01265; -; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR002811; Asp_DH.
DR   InterPro; IPR011182; Asp_DH_NAD_syn.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01958; DUF108; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR   ProDom; PD017325; Asp_dh; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; NADP; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN         1    271       Probable L-aspartate dehydrogenase.
FT                                /FTId=PRO_0000144898.
FT   ACT_SITE    222    222       By similarity.
FT   BINDING     124    124       NAD; via amide nitrogen (By similarity).
FT   BINDING     192    192       NAD (By similarity).
SQ   SEQUENCE   271 AA;  28615 MW;  466E329688C58EC3 CRC64;
     MLKIGIIGCG FIGGQICRAI DSGEIDAELY ALCDSSESKA FGLAKSLNTC KPAYMKIEEL
     ISSVDLVVES ASQNAVRFIV PQALKAGCSV MVLSVGALAD KELRETLFGL AKKHNCKLYF
     PSGAVVGIDG INSAHAAGIS SVTLTTRKPP SGLMGAPYVV EHGIELEKLE KETILFEGTA
     SEAVKAFPAN VNVAATISLA GIGFERTMVR VIADPSLSRN IHEINVEGEF GKFCTKVENL
     PSPENPKTSY LAALSAISTL KKILNPVQIG T
//