ID   ASPD_POLSJ              Reviewed;         267 AA.
AC   Q126F5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Probable L-aspartate dehydrogenase;
DE            EC=1.4.1.21;
GN   Name=nadX; OrderedLocusNames=Bpro_3686;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591;
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   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I., Richardson P.;
RT   "Complete sequence of chromosome of Polaromonas sp. JS666.";
RL   Submitted (APR-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; CP000316; ABE45587.1; -; Genomic_DNA.
DR   RefSeq; YP_550485.1; -.
DR   GeneID; 4013636; -.
DR   GenomeReviews; CP000316_GR; Bpro_3686.
DR   KEGG; pol:Bpro_3686; -.
DR   NMPDR; fig|296591.1.peg.1652; -.
DR   HOGENOM; Q126F5; -.
DR   OMA; Q126F5; ECAGHSA.
DR   BioCyc; PSP296591:BPRO_3686-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    267       Probable L-aspartate dehydrogenase.
FT                                /FTId=PRO_1000067310.
FT   ACT_SITE    220    220       By similarity.
FT   BINDING     124    124       NAD; via amide nitrogen (By similarity).
FT   BINDING     190    190       NAD (By similarity).
SQ   SEQUENCE   267 AA;  27568 MW;  F1000ACBA87EB262 CRC64;
     MLKIAMIGCG AIGASVLELL HGDSDVVVDR VITVPEARDR TEIAVARWAP RARVLEVLAA
     DDAPDLVVEC AGHGAIAAHV VPALERGIPC VVTSVGALSA PGMAQLLEQA ARRGKTQVQL
     LSGAIGGIDA LAAARVGGLD SVVYTGRKPP MAWKGTPAEA VCDLDSLTVA HCIFDGSAEQ
     AAQLYPKNAN VAATLSLAGL GLKRTQVQLF ADPGVSENVH HVAAHGAFGS FELTMRGRPL
     AANPKTSALT VYSVVRALLN RGRALVI
//