ID   ASPD_METBF              Reviewed;         271 AA.
AC   Q46BD6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Probable L-aspartate dehydrogenase;
DE            EC=1.4.1.21;
GN   Name=nadX; OrderedLocusNames=Mbar_A1866;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70806.1; -; Genomic_DNA.
DR   RefSeq; YP_305386.1; -.
DR   GeneID; 3624568; -.
DR   GenomeReviews; CP000099_GR; Mbar_A1866.
DR   KEGG; mba:Mbar_A1866; -.
DR   NMPDR; fig|269797.3.peg.2965; -.
DR   HOGENOM; Q46BD6; -.
DR   OMA; Q46BD6; ECAGHSA.
DR   BioCyc; MBAR269797:MBAR_A1866-MON; -.
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   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_1000067303.
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;  28823 MW;  868F364A30900982 CRC64;
     MLKIGVIGCG FIGGQICRAI DKGVINAELY ALSDSSESKV LELTTCLKRY SPASMTIEEL
     LQNVDFVIES ASQKAVRLIV PQALEAGRDV MVMSVGALAD EELRKRLFRL AEQNNCKLYF
     PSGAVAGIDG INSASAAEIL SVTLTTRKPP MGLAGAPHVE ALGIELETIE KETLLFEGPA
     SEAVKAFPAN VNVAATISLA GIGFERTKVR VIADPTLSRN VHEITVEGEF GKLSTRVENL
     PSPENPKTSY LAALSAISTL KKILSPVQIG T
//