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Database: UniProt
Entry: N9EYG8_ACIHA
LinkDB: N9EYG8_ACIHA
Original site: N9EYG8_ACIHA 
ID   N9EYG8_ACIHA            Unreviewed;       263 AA.
AC   N9EYG8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, 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=F927_03307 {ECO:0000313|EMBL:ENW15568.1};
OS   Acinetobacter haemolyticus CIP 64.3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW15568.1, ECO:0000313|Proteomes:UP000017667};
RN   [1] {ECO:0000313|EMBL:ENW15568.1, ECO:0000313|Proteomes:UP000017667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW15568.1,
RC   ECO:0000313|Proteomes:UP000017667};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL   Submitted (FEB-2013) 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:ENW15568.1}.
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DR   EMBL; APQQ01000032; ENW15568.1; -; Genomic_DNA.
DR   RefSeq; WP_005084794.1; NZ_KB849804.1.
DR   EnsemblBacteria; ENW15568; ENW15568; F927_03307.
DR   PATRIC; fig|1217659.3.peg.3248; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000017667; 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:UP000017667};
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        8    116       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      164    251       DUF108. {ECO:0000259|Pfam:PF01958}.
FT   ACT_SITE    216    216       {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     120    120       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     186    186       NAD. {ECO:0000256|HAMAP-Rule:MF_01265}.
SQ   SEQUENCE   263 AA;  28073 MW;  16DF27D69521998C CRC64;
     MKQLMMIGFG AMAAEVYAHM PQDLQLKWIV VPARSVEKVQ AQVAPDVQVI SSIDQCQGTP
     DYVIEVAGQA AVKEHAQKVL EKGWTIGLIS VGTLADNEFL IQLKNTAEQH DAHLHLLAGA
     IAGIDGISAA KEGGLEKVTY KGCKSPRSWR GSYAEQLVDL DQVSEATVFF RGTAREAALK
     FPANANVAAT IALAGLGMDE TMVELTVDPN INKNKHTIVA EGVFGEMTIE LVGVPLASNP
     KTSTLAALSV IRACRNSVQA IQI
//
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