ID D3S1Q0_FERPA Unreviewed; 245 AA.
AC D3S1Q0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=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=Ferp_0170 {ECO:0000313|EMBL:ADC64357.1};
OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Ferroglobus.
OX NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC64357.1, ECO:0000313|Proteomes:UP000002613};
RN [1] {ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT "Complete sequence of Ferroglobus placidus DSM 10642.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC64357.1, ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX PubMed=22180810; DOI=10.4056/sigs.2225018;
RA Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA Lovley D., Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL Stand. Genomic Sci. 5:50-60(2011).
CC -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000256|HAMAP-
CC 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: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; EC=1.4.1.21;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01265};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (dehydrogenase route): step 1/1. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01265}.
CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008331, ECO:0000256|HAMAP-Rule:MF_01265}.
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DR EMBL; CP001899; ADC64357.1; -; Genomic_DNA.
DR RefSeq; WP_012964704.1; NC_013849.1.
DR AlphaFoldDB; D3S1Q0; -.
DR STRING; 589924.Ferp_0170; -.
DR PaxDb; 589924-Ferp_0170; -.
DR GeneID; 8777664; -.
DR KEGG; fpl:Ferp_0170; -.
DR eggNOG; arCOG00254; Archaea.
DR HOGENOM; CLU_089550_0_0_2; -.
DR OrthoDB; 15415at2157; -.
DR UniPathway; UPA00253; UER00456.
DR Proteomes; UP000002613; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01265; NadX; 1.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR002811; Asp_DH.
DR InterPro; IPR022487; Asp_DH_arc.
DR InterPro; IPR020626; Asp_DH_prok.
DR InterPro; IPR011182; L-Asp_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR03855; NAD_NadX; 1.
DR PANTHER; PTHR31873:SF6; ASPARTATE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31873; L-ASPARTATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01958; Asp_DH_C; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01265};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01265};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01265};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_01265};
KW Reference proteome {ECO:0000313|Proteomes:UP000002613}.
FT DOMAIN 7..116
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 153..232
FT /note="Aspartate dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01958"
FT ACT_SITE 198
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
SQ SEQUENCE 245 AA; 27265 MW; 211C5B868725D82A CRC64;
MRVGLLGCGN LGRIIVENSK KFGVEIVSLY DKEFSKAVEL SKICGKPCKS FEDFIKGEFD
FVIEAASAEA VREYGKKILD GRKNLVILST AALIDEDLLK KLRRKAKEVG KKIYIPSGAI
VGLDGLSVLK FFESKIKLIT RKNPKALGRN LGLIFKGFVK DAVKKFPRNL NVAATLSLAT
GKDVEVEVFA ENLERNIHEI LAKWEFGEIY VRVENVPSKN VKSSHLAALS VLSLLRNLEE
EVVVW
//
