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Database: UniProt
Entry: J3CKS4_9BURK
LinkDB: J3CKS4_9BURK
Original site: J3CKS4_9BURK 
ID   J3CKS4_9BURK            Unreviewed;       265 AA.
AC   J3CKS4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   16-JAN-2019, entry version 31.
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=PMI12_03491 {ECO:0000313|EMBL:EJL73516.1};
OS   Variovorax sp. CF313.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1144315 {ECO:0000313|EMBL:EJL73516.1, ECO:0000313|Proteomes:UP000007277};
RN   [1] {ECO:0000313|EMBL:EJL73516.1, ECO:0000313|Proteomes:UP000007277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF313 {ECO:0000313|EMBL:EJL73516.1,
RC   ECO:0000313|Proteomes:UP000007277};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL73516.1}.
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DR   EMBL; AKIW01000068; EJL73516.1; -; Genomic_DNA.
DR   RefSeq; WP_007834764.1; NZ_AKIW01000068.1.
DR   EnsemblBacteria; EJL73516; EJL73516; PMI12_03491.
DR   PATRIC; fig|1144315.3.peg.3435; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000007277; 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:UP000007277};
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}.
FT   DOMAIN       11    117       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      167    253       DUF108. {ECO:0000259|Pfam:PF01958}.
FT   ACT_SITE    218    218       {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   265 AA;  26783 MW;  222C91AB4DA7489F CRC64;
     MPAITRIALI GCGAIGTSVL ELLRGDPALE VVAIVVPAEG VAAAQKAAPD AQVGSAVPAA
     GIDLVVETAG HAAIEEHVLP ALARGTPCVV ASVGALSATG FAEKLEAAAI AGNTQVQLIP
     GAIGAIDALA AARIGGLDSV RYTGRKPPQA WKGTPAEQGR DLDRLAQETV IFEGSAREAA
     LLFPKNANVA ATVSLAGLGL DKTLVRLIAD PATTENVHTV EAEGAFGSFE LTMRNKPLAA
     NPKTSALTVY SAVRALRNRV AALAI
//
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