ID ASPD_THEMA Reviewed; 241 AA.
AC Q9X1X6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=L-aspartate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000305};
DE EC=1.4.1.21 {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000269|PubMed:12496312};
GN Name=nadX {ECO:0000255|HAMAP-Rule:MF_01265}; OrderedLocusNames=TM_1643;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga
RT maritima at 1.9 A resolution.";
RL Submitted (JUL-2002) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-241 IN COMPLEX WITH NAD,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND ACTIVE SITE.
RX PubMed=12496312; DOI=10.1074/jbc.m211892200;
RA Yang Z., Savchenko A., Yakunin A.F., Zhang R., Edwards A.M.,
RA Arrowsmith C.H., Tong L.;
RT "Aspartate dehydrogenase, a novel enzyme identified from structural and
RT functional studies of TM1643.";
RL J. Biol. Chem. 278:8804-8808(2003).
CC -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC dehydrogenation of L-aspartate to iminoaspartate. Does not show
CC aspartate oxidase activity. Is also able to catalyze the reverse
CC reaction, i.e. the reductive amination of oxaloacetate.
CC {ECO:0000269|PubMed:12496312}.
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 ECO:0000269|PubMed:12496312};
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 ECO:0000269|PubMed:12496312};
CC -!- ACTIVITY REGULATION: Competitively inhibited by L-malate and NH(4)(+).
CC {ECO:0000269|PubMed:12496312}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.067 mM for L-aspartate (in the presence of NAD)
CC {ECO:0000269|PubMed:12496312};
CC KM=1.20 mM for L-aspartate (in the presence of NADP)
CC {ECO:0000269|PubMed:12496312};
CC KM=0.25 mM for NAD {ECO:0000269|PubMed:12496312};
CC KM=0.72 mM for NADP {ECO:0000269|PubMed:12496312};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (dehydrogenase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01265}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:12496312}.
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, ECO:0000305}.
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DR EMBL; AE000512; AAD36710.1; -; Genomic_DNA.
DR PIR; H72226; H72226.
DR RefSeq; NP_229443.1; NC_000853.1.
DR RefSeq; WP_004082138.1; NZ_CP011107.1.
DR PDB; 1H2H; X-ray; 2.60 A; A=1-241.
DR PDB; 1J5P; X-ray; 1.90 A; A=1-241.
DR PDBsum; 1H2H; -.
DR PDBsum; 1J5P; -.
DR AlphaFoldDB; Q9X1X6; -.
DR SMR; Q9X1X6; -.
DR STRING; 243274.TM_1643; -.
DR PaxDb; 243274-THEMA_06030; -.
DR EnsemblBacteria; AAD36710; AAD36710; TM_1643.
DR KEGG; tma:TM1643; -.
DR eggNOG; COG1712; Bacteria.
DR InParanoid; Q9X1X6; -.
DR OrthoDB; 1906017at2; -.
DR BioCyc; MetaCyc:MONOMER-21958; -.
DR BRENDA; 1.4.1.21; 6331.
DR SABIO-RK; Q9X1X6; -.
DR UniPathway; UPA00253; UER00456.
DR EvolutionaryTrace; Q9X1X6; -.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 3D-structure; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1..241
FT /note="L-aspartate dehydrogenase"
FT /id="PRO_0000144893"
FT ACT_SITE 193
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265,
FT ECO:0000305|PubMed:12496312"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT BINDING 28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT BINDING 56..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT BINDING 63..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT BINDING 78..79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT BINDING 109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265,
FT ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265,
FT ECO:0000269|PubMed:12496312, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:1H2H, ECO:0007744|PDB:1J5P"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 192..201
FT /evidence="ECO:0007829|PDB:1J5P"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1J5P"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:1J5P"
SQ SEQUENCE 241 AA; 26640 MW; AF52221512C3DE2E CRC64;
MTVLIIGMGN IGKKLVELGN FEKIYAYDRI SKDIPGVVRL DEFQVPSDVS TVVECASPEA
VKEYSLQILK NPVNYIIIST SAFADEVFRE RFFSELKNSP ARVFFPSGAI GGLDVLSSIK
DFVKNVRIET IKPPKSLGLD LKGKTVVFEG SVEEASKLFP RNINVASTIG LIVGFEKVKV
TIVADPAMDH NIHIVRISSA IGNYEFKIEN IPSPENPKTS MLTVYSILRT LRNLESKIIF
G
//
