ASPD_BRADU
ID ASPD_BRADU Reviewed; 280 AA.
AC Q89FY1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=bll6567;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC51832.1; -; Genomic_DNA.
DR RefSeq; NP_773207.1; NC_004463.1.
DR AlphaFoldDB; Q89FY1; -.
DR SMR; Q89FY1; -.
DR STRING; 224911.27354847; -.
DR EnsemblBacteria; BAC51832; BAC51832; BAC51832.
DR KEGG; bja:bll6567; -.
DR PATRIC; fig|224911.5.peg.6724; -.
DR eggNOG; COG1712; Bacteria.
DR HOGENOM; CLU_089550_0_0_5; -.
DR InParanoid; Q89FY1; -.
DR OMA; ECAGHSA; -.
DR PhylomeDB; Q89FY1; -.
DR UniPathway; UPA00253; UER00456.
DR Proteomes; UP000002526; 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..280
FT /note="L-aspartate dehydrogenase"
FT /id="PRO_0000144887"
FT ACT_SITE 232
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01265"
SQ SEQUENCE 280 AA; 29472 MW; 545EC9E5ACBB4F75 CRC64;
MDRRWKVMTD QTASSELRVA IAGLGSIGTK IAAALDQGEG LTLSAVAVRD PAKHQAFLNG
LRRPPQVLPI DQLGEAADIV VECAPSSQLR AIVEPAVKRG KAAVVVSVGG LLDNFDLVDL
ARANGGRIIV PTGALIGLDA VNAAVIGTIH SVKMVTRKPI DGLKGAPFIV HNNIDIDTLR
EPLKLFEGTA REAAKGFPAN LNVAVALSLA GVGPDRTSVQ IWADPTVTRN VHRIEVEADS
ARFSMSIENI PSENPKTGLI TALSVIALLR KQRATLCVGT
