ASPD_PSEAE
ID ASPD_PSEAE Reviewed; 267 AA.
AC Q9HYA4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=L-aspartate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01265};
DE EC=1.4.1.21 {ECO:0000255|HAMAP-Rule:MF_01265};
GN Name=nadX {ECO:0000255|HAMAP-Rule:MF_01265}; OrderedLocusNames=PA3505;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000255|HAMAP-
CC 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; EC=1.4.1.21;
CC Evidence={ECO:0000255|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; EC=1.4.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01265};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (dehydrogenase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01265}.
CC -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous
CC solution and can decompose to oxaloacetate and ammonia.
CC {ECO:0000255|HAMAP-Rule:MF_01265}.
CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01265}.
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DR EMBL; AE004091; AAG06893.1; -; Genomic_DNA.
DR PIR; G83206; G83206.
DR RefSeq; NP_252195.1; NC_002516.2.
DR RefSeq; WP_003112905.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HYA4; -.
DR SMR; Q9HYA4; -.
DR STRING; 208964.PA3505; -.
DR PaxDb; Q9HYA4; -.
DR EnsemblBacteria; AAG06893; AAG06893; PA3505.
DR GeneID; 879175; -.
DR KEGG; pae:PA3505; -.
DR PATRIC; fig|208964.12.peg.3669; -.
DR PseudoCAP; PA3505; -.
DR HOGENOM; CLU_089550_0_0_6; -.
DR InParanoid; Q9HYA4; -.
DR OMA; ECAGHSA; -.
DR PhylomeDB; Q9HYA4; -.
DR BioCyc; PAER208964:G1FZ6-3573-MON; -.
DR BRENDA; 1.4.1.21; 5087.
DR UniPathway; UPA00253; UER00456.
DR Proteomes; UP000002438; 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 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 NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1..267
FT /note="L-aspartate dehydrogenase"
FT /id="PRO_0000144890"
FT ACT_SITE 220
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
SQ SEQUENCE 267 AA; 27920 MW; 208FBC975A872F86 CRC64;
MLNIVMIGCG AIGAGVLELL ENDPQLRVDA VIVPRDSETQ VRHRLASLRR PPRVLSALPA
GERPDLLVEC AGHRAIEQHV LPALAQGIPC LVVSVGALSE PGLVERLEAA AQAGGSRIEL
LPGAIGAIDA LSAARVGGLE SVRYTGRKPA SAWLGTPGET VCDLQRLEKA RVIFDGSARE
AARLYPKNAN VAATLSLAGL GLDRTQVRLI ADPESCENVH QVEASGAFGG FELTLRGKPL
AANPKTSALT VYSVVRALGN HAHAISI
