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Database: UniProt
Entry: G8PFY3_PSEUV
LinkDB: G8PFY3_PSEUV
Original site: G8PFY3_PSEUV 
ID   G8PFY3_PSEUV            Unreviewed;       281 AA.
AC   G8PFY3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   16-JAN-2019, entry version 38.
DE   RecName: Full=Probable L-aspartate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01265};
DE            EC=1.4.1.21 {ECO:0000256|HAMAP-Rule:MF_01265};
GN   Name=nadX {ECO:0000256|HAMAP-Rule:MF_01265};
GN   OrderedLocusNames=PSE_1841 {ECO:0000313|EMBL:AEV36351.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV36351.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and
RT   symbiotically interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV36351.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV36351.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A.,
RA   Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria
RT   adapted for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
CC   -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC       dehydrogenation of L-aspartate to iminoaspartate.
CC       {ECO:0000256|HAMAP-Rule:MF_01265}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) +
CC         oxaloacetate; Xref=Rhea:RHEA:11788, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.4.1.21; Evidence={ECO:0000256|HAMAP-Rule:MF_01265};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) +
CC         oxaloacetate; Xref=Rhea:RHEA:11784, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.4.1.21; Evidence={ECO:0000256|HAMAP-Rule:MF_01265};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis;
CC       iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01265}.
CC   -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous
CC       solution and can decompose to oxaloacetate and ammonia.
CC       {ECO:0000256|HAMAP-Rule:MF_01265}.
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01265}.
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DR   EMBL; CP003147; AEV36351.1; -; Genomic_DNA.
DR   STRING; 911045.PSE_1841; -.
DR   EnsemblBacteria; AEV36351; AEV36351; PSE_1841.
DR   KEGG; psf:PSE_1841; -.
DR   eggNOG; ENOG4108Q27; Bacteria.
DR   eggNOG; COG1712; LUCA.
DR   KO; K06989; -.
DR   OMA; MIMSVGA; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006742; P:NADP catabolic process; IEA:InterPro.
DR   HAMAP; MF_01265; NadX; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR002811; Asp_DH.
DR   InterPro; IPR020626; Asp_DH_prok.
DR   InterPro; IPR011182; L-Asp_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01958; DUF108; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005634};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01265};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01265};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01265,
KW   ECO:0000313|EMBL:AEV36351.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   DOMAIN       20    131       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      181    267       DUF108. {ECO:0000259|Pfam:PF01958}.
FT   ACT_SITE    232    232       {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     134    134       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     202    202       NAD. {ECO:0000256|HAMAP-Rule:MF_01265}.
SQ   SEQUENCE   281 AA;  29732 MW;  DA36591ACBF36A9B CRC64;
     MYHLAYGGLM RKLESIAIAG LGAIGKRVAQ AVIKNEIPGY ELKAIAVRDI QKGKEFLKAL
     PEHSCQPLPL DELPLVADIV LECLPPQLFE KVARPTLSCG KSLIVMSTSQ LLSRMHLLDL
     AKQNGANIIV PSGAILGLDA LKAAAEGTIQ SVVVRTSKPP QGLAGAAYLI ENSIDVESSN
     VPTCILSGSV NEVAQHFPAN VNVAAALALA GLGADKTTME IWADPNLSKN THTVSVTSDS
     SDFTMTISNR PSDENPRTGR ITAQSVLAVL RTRTSHIQIG S
//
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