ID   ASPD_METHJ              Reviewed;         252 AA.
AC   Q2FSK9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Probable L-aspartate dehydrogenase;
DE            EC=1.4.1.21;
GN   Name=nadX; OrderedLocusNames=Mhun_2354;
OS   Methanospirillum hungatei (strain JF-1 / DSM 864).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D.,
RA   Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J.,
RA   Stams A.J.M., Boone D.R., Richardson P.;
RT   "Complete sequence of Methanospirillum hungatei JF-1.";
RL   Submitted (JAN-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; CP000254; ABD42058.1; -; Genomic_DNA.
DR   RefSeq; YP_503777.1; -.
DR   GeneID; 3923251; -.
DR   GenomeReviews; CP000254_GR; Mhun_2354.
DR   KEGG; mhu:Mhun_2354; -.
DR   NMPDR; fig|323259.5.peg.2478; -.
DR   HOGENOM; Q2FSK9; -.
DR   OMA; Q2FSK9; ECAGHSA.
DR   BioCyc; MHUN323259:MHUN_2354-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    252       Probable L-aspartate dehydrogenase.
FT                                /FTId=PRO_1000067305.
FT   ACT_SITE    203    203       By similarity.
FT   BINDING     119    119       NAD; via amide nitrogen (By similarity).
FT   BINDING     175    175       NAD (By similarity).
SQ   SEQUENCE   252 AA;  27227 MW;  DB0A2E0F122E4710 CRC64;
     MVRIGLLGCG NVGRIIATHQ DGFTVEALFD RLPDHAEELA RMCGAPAYAD FQEFISQDFD
     ICVEAASVLA VREYAPKILE NGKHVLILSV GALSDTNFRK ILLDVARSQG KKIHIPSGAI
     MGLDNLKVGG ISRIDSVLLR TTKSPASLGM QVSHRTLAFR GKANECIKQF PKNINVSVAL
     ALAVHHDVDV ELWADPEVDR NIHDIFVSGE FGEASIRVVN HPSPDNPATS YLAALSVLSL
     LKNLDSPLVI GS
//