ASPD_ARCFU
ID ASPD_ARCFU Reviewed; 236 AA.
AC O28440;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=L-aspartate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01265, ECO:0000305};
DE Short=L-aspDH {ECO:0000303|PubMed:16731057};
DE EC=1.4.1.21 {ECO:0000255|HAMAP-Rule:MF_01265};
GN Name=nadX {ECO:0000255|HAMAP-Rule:MF_01265}; OrderedLocusNames=AF_1838;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-6, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=16731057; DOI=10.1016/j.bbapap.2006.04.006;
RA Yoneda K., Kawakami R., Tagashira Y., Sakuraba H., Goda S., Ohshima T.;
RT "The first archaeal L-aspartate dehydrogenase from the hyperthermophile
RT Archaeoglobus fulgidus: gene cloning and enzymological characterization.";
RL Biochim. Biophys. Acta 1764:1087-1093(2006).
RN [3] {ECO:0007744|PDB:2DC1}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RX PubMed=17651440; DOI=10.1111/j.1742-4658.2007.05961.x;
RA Yoneda K., Sakuraba H., Tsuge H., Katunuma N., Ohshima T.;
RT "Crystal structure of archaeal highly thermostable L-aspartate
RT dehydrogenase/NAD/citrate ternary complex.";
RL FEBS J. 274:4315-4325(2007).
CC -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC dehydrogenation of L-aspartate to iminoaspartate. {ECO:0000255|HAMAP-
CC Rule:MF_01265, ECO:0000269|PubMed:16731057}.
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:16731057};
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:16731057};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 mM for L-aspartate (in the presence of NAD)
CC {ECO:0000269|PubMed:16731057};
CC KM=4.3 mM for L-aspartate (in the presence of NADP)
CC {ECO:0000269|PubMed:16731057};
CC KM=0.11 mM for NAD {ECO:0000269|PubMed:16731057};
CC KM=0.32 mM for NADP {ECO:0000269|PubMed:16731057};
CC KM=1.2 mM for oxaloacetate (in the presence of NADH and NH(3))
CC {ECO:0000269|PubMed:16731057};
CC KM=0.014 mM for NADH (in the presence of oxaloacetate and NH(3))
CC {ECO:0000269|PubMed:16731057};
CC KM=167 mM for NH(3) (in the presence of oxaloacetate and NADH)
CC {ECO:0000269|PubMed:16731057};
CC pH dependence:
CC Optimum pH is around 11.6. {ECO:0000269|PubMed:16731057};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:16731057};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (dehydrogenase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01265, ECO:0000305|PubMed:16731057}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16731057,
CC ECO:0000269|PubMed:17651440}.
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; AE000782; AAB89415.1; -; Genomic_DNA.
DR PIR; E69479; E69479.
DR RefSeq; WP_010879332.1; NC_000917.1.
DR PDB; 2DC1; X-ray; 1.90 A; A/B=1-236.
DR PDBsum; 2DC1; -.
DR AlphaFoldDB; O28440; -.
DR SMR; O28440; -.
DR STRING; 224325.AF_1838; -.
DR EnsemblBacteria; AAB89415; AAB89415; AF_1838.
DR GeneID; 24795582; -.
DR KEGG; afu:AF_1838; -.
DR eggNOG; arCOG00254; Archaea.
DR HOGENOM; CLU_089550_0_0_2; -.
DR OMA; ECAGHSA; -.
DR OrthoDB; 50102at2157; -.
DR PhylomeDB; O28440; -.
DR BRENDA; 1.4.1.21; 414.
DR SABIO-RK; O28440; -.
DR UniPathway; UPA00253; UER00456.
DR EvolutionaryTrace; O28440; -.
DR Proteomes; UP000002199; 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; 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 Pfam; PF01958; DUF108; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03855; NAD_NadX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; NADP; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..236
FT /note="L-aspartate dehydrogenase"
FT /id="PRO_0000144894"
FT ACT_SITE 189
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17651440,
FT ECO:0007744|PDB:2DC1"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17651440,
FT ECO:0007744|PDB:2DC1"
FT BINDING 58..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17651440,
FT ECO:0007744|PDB:2DC1"
FT BINDING 66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17651440,
FT ECO:0007744|PDB:2DC1"
FT BINDING 80..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17651440,
FT ECO:0007744|PDB:2DC1"
FT BINDING 111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265,
FT ECO:0000269|PubMed:17651440, ECO:0007744|PDB:2DC1"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265,
FT ECO:0000269|PubMed:17651440, ECO:0007744|PDB:2DC1"
FT BINDING 212..215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2DC1"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:2DC1"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:2DC1"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2DC1"
SQ SEQUENCE 236 AA; 26208 MW; 29218ACC7F919F52 CRC64;
MLVGLIGYGA IGKFLAEWLE RNGFEIAAIL DVRGEHEKMV RGIDEFLQRE MDVAVEAASQ
QAVKDYAEKI LKAGIDLIVL STGAFADRDF LSRVREVCRK TGRRVYIASG AIGGLDAIFS
ASELIEEIVL TTRKNWRQFG RKGVIFEGSA SEAAQKFPKN LNVAATLSIA SGKDVKVRLV
ADEVEENIHE ILVRGEFGEM EIRVRNRPMR ENPKTSYLAA LSVTRILRNL KEGLVV
