ID   ASPD_METBU              Reviewed;         271 AA.
AC   Q12VF1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Probable L-aspartate dehydrogenase;
DE            EC=1.4.1.21;
GN   Name=nadX; OrderedLocusNames=Mbur_1681;
OS   Methanococcoides burtonii (strain DSM 6242).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcoides burtonii DSM 6242.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000300; ABE52575.1; -; Genomic_DNA.
DR   RefSeq; YP_566325.1; -.
DR   GeneID; 3998077; -.
DR   GenomeReviews; CP000300_GR; Mbur_1681.
DR   KEGG; mbu:Mbur_1681; -.
DR   NMPDR; fig|259564.8.peg.1603; -.
DR   HOGENOM; Q12VF1; -.
DR   OMA; Q12VF1; ECAGHSA.
DR   BioCyc; MBUR259564:MBUR_1681-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   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_1000067304.
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;  29094 MW;  00D97CE0518CAB6A CRC64;
     MLKIGVFGCG AIGTELCKAI DSGHIEVELY AVYDRHEQSI INLKEQLKNT DPKVLEIVEM
     VKHVDLVVEC ASQQAVYDVV PTTLHAKCDV MVISVGAFAD KKLLDTTFDI AKEYGCKIYF
     PSGAIVGLDG LKSASAASIY SVTLTTQKHP RSFEGAPYIV QNNIDLDSIK GKTVLFEGMA
     SEAVKAFPSN VNVAASLSIA GIGFDKTKVK IIANPALTRN IHEITVEGEF GMFTTRVENV
     PAPSNPKTSY LAALSAISTL KKIADPLQVG T
//