ID   ASPD_PSYCK              Reviewed;         263 AA.
AC   Q1QBB6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   04-NOV-2008, entry version 20.
DE   RecName: Full=Probable L-aspartate dehydrogenase;
DE            EC=1.4.1.21;
GN   Name=nadX; OrderedLocusNames=Pcryo_1256;
OS   Psychrobacter cryohalolentis (strain K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=335284;
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., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
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; CP000323; ABE75037.1; -; Genomic_DNA.
DR   RefSeq; YP_580521.1; -.
DR   GeneID; 4034285; -.
DR   GenomeReviews; CP000323_GR; Pcryo_1256.
DR   KEGG; pcr:Pcryo_1256; -.
DR   NMPDR; fig|335284.3.peg.838; -.
DR   HOGENOM; Q1QBB6; -.
DR   BioCyc; PCRY335284:PCRYO_1256-MON; -.
DR   GO; GO:0051287; F:NAD binding; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01265; -; 1.
DR   InterPro; IPR005106; Asp/hSer_DHase_NAD-bd.
DR   InterPro; IPR002811; Asp_DHase.
DR   InterPro; IPR011182; Asp_DHase_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    263       Probable L-aspartate dehydrogenase.
FT                                /FTId=PRO_1000067311.
FT   ACT_SITE    216    216       By similarity.
FT   BINDING     120    120       NAD; via amide nitrogen (By similarity).
FT   BINDING     186    186       NAD (By similarity).
SQ   SEQUENCE   263 AA;  27858 MW;  47927F6132E01CA0 CRC64;
     MKNVMFIGYG SMARKVHEML PKNIILSTVL VSTRSAEIIK TELGESIAVI TSVDDLIETP
     DLAVEMSGQD GLKEHAIKIL GKSIPLGIIS VGAFTDEKFA ISLADTAEAN GVEIHILAGA
     VAGIDGIHAA SFAGLSDVVY QGKKHPSSWK GSHADRLIDY DNLVEPTVFF TGTAREAAAL
     FPDNSNVAAT IAIAGVGLDD TTVELIADPT LEYNIHHIMA KGVFGKLEIS MAGLPLVENP
     KTSSLAAFSA LRLCCQIDQV IQM
//