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Database: UniProt
Entry: A0A0Q9IDT5_9BRAD
LinkDB: A0A0Q9IDT5_9BRAD
Original site: A0A0Q9IDT5_9BRAD 
ID   A0A0Q9IDT5_9BRAD        Unreviewed;       264 AA.
AC   A0A0Q9IDT5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   10-APR-2019, entry version 14.
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   ORFNames=ASE66_13990 {ECO:0000313|EMBL:KRE14908.1};
OS   Bosea sp. Root483D1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bosea.
OX   NCBI_TaxID=1736544 {ECO:0000313|EMBL:KRE14908.1, ECO:0000313|Proteomes:UP000051771};
RN   [1] {ECO:0000313|EMBL:KRE14908.1, ECO:0000313|Proteomes:UP000051771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root483D1 {ECO:0000313|EMBL:KRE14908.1,
RC   ECO:0000313|Proteomes:UP000051771};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE14908.1, ECO:0000313|Proteomes:UP000051771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root483D1 {ECO:0000313|EMBL:KRE14908.1,
RC   ECO:0000313|Proteomes:UP000051771};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRE14908.1}.
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DR   EMBL; LMJW01000020; KRE14908.1; -; Genomic_DNA.
DR   RefSeq; WP_057191922.1; NZ_LMJW01000020.1.
DR   EnsemblBacteria; KRE14908; KRE14908; ASE66_13990.
DR   OrthoDB; 1670363at2; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000051771; Unassembled WGS sequence.
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:UP000051771};
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   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01265};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051771}.
FT   DOMAIN       12    119       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      167    251       DUF108. {ECO:0000259|Pfam:PF01958}.
FT   ACT_SITE    217    217       {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     122    122       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     188    188       NAD. {ECO:0000256|HAMAP-Rule:MF_01265}.
SQ   SEQUENCE   264 AA;  27443 MW;  E974B2D811D5A75E CRC64;
     MASERRIGLI GFGTIARDIQ ARLGDDGFAF ACLLRPDSPS RAGMPDGVTL LASVDELLAW
     RPALVVEAAG HAAVLQLLPA ILAAGIPALP ASTGALADDD LLSRLTEAAE QGRTRLIVPS
     GAVGGLDYLA ALRETADASI RYTSRKPPAA WGPELAAAGL TEKAAQAEIL LYEGTAREAA
     QLYPKNLNVG LTIALAVGHD RLSVRIVSDP EAAGNKHEIE AMSALGTARL SFVNLPSPAN
     PKTSALTAAS LTATIRRQFD RIAV
//
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