ID H2J308_MARPK Unreviewed; 251 AA.
AC H2J308;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=Marpi_1296 {ECO:0000313|EMBL:AEX85699.1};
OS Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Marinitoga.
OX NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX85699.1, ECO:0000313|Proteomes:UP000007161};
RN [1] {ECO:0000313|EMBL:AEX85699.1, ECO:0000313|Proteomes:UP000007161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14283 / JCM 11233 / KA3
RC {ECO:0000313|Proteomes:UP000007161};
RX PubMed=23045491; DOI=10.1128/JB.01430-12;
RA Lucas S., Han J., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N.C., Ivanova N., Pagani I., Vannier P.,
RA Oger P., Bartlett D.H., Noll K.M., Woyke T., Jebbar M.;
RT "Complete Genome Sequence of the Thermophilic, Piezophilic, Heterotrophic
RT Bacterium Marinitoga piezophila KA3.";
RL J. Bacteriol. 194:5974-5975(2012).
RN [2] {ECO:0000313|Proteomes:UP000007161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14283 / JCM 11233 / KA3
RC {ECO:0000313|Proteomes:UP000007161};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M.,
RA Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.;
RT "Complete sequence of chromosome of Marinitoga piezophila KA3.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003257; AEX85699.1; -; Genomic_DNA.
DR RefSeq; WP_014296770.1; NC_016751.1.
DR AlphaFoldDB; H2J308; -.
DR STRING; 443254.Marpi_1296; -.
DR KEGG; mpz:Marpi_1296; -.
DR eggNOG; COG1712; Bacteria.
DR HOGENOM; CLU_089550_0_0_0; -.
DR OrthoDB; 1906017at2; -.
DR UniPathway; UPA00253; UER00456.
DR Proteomes; UP000007161; 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:UP000007161}.
FT DOMAIN 13..114
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 150..236
FT /note="Aspartate dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01958"
FT ACT_SITE 203
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
FT BINDING 118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01265"
SQ SEQUENCE 251 AA; 27974 MW; 51F00FE511455B36 CRC64;
MKIFLIGAGN SAKIILEELK EELDKVYVYD VDKSQIEKLK EFYNISYADI KDIANLDIDY
VIEVASTKAV VEYGKFVIEN NKNFIILSTG AFADRDFLND FQEALKKSNS RVYVVSGAIG
GIDLINAIND KIKSITLTTR KPPKSLGLEI DEEKVIFEGS STEAIKRFPK NVNVAVTLSL
AARDFDKVKV RIIADPKVER NIHNIKINSI AGNYEFTFEN FPSENPKTSY LAPLSVAGLL
KNINSKIKIG G
//
