{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A3P4L6","uniProtkbId":"ASPD_BURP0","entryAudit":{"firstPublicDate":"2008-02-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-04-03","entryVersion":91,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Burkholderia pseudomallei (strain 1106a)","taxonId":357348,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Burkholderia","pseudomallei group"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"value":"L-aspartate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"value":"1.4.1.21"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"value":"nadX"},"orderedLocusNames":[{"value":"BURPS1106A_A1241"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"value":"Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartate + NADP(+) + H2O = oxaloacetate + NH4(+) + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11784"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16452"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.4.1.21","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartate + NAD(+) + H2O = oxaloacetate + NH4(+) + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11788"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16452"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.4.1.21","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"value":"Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"value":"The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"value":"Belongs to the L-aspartate dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"L-aspartate dehydrogenase","featureId":"PRO_1000067297"},{"type":"Active site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}]},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01265"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}}],"keywords":[{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0521","category":"Ligand","name":"NADP"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0662","category":"Biological process","name":"Pyridine nucleotide biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"20333227","citationType":"journal article","authors":["Losada L.","Ronning C.M.","DeShazer D.","Woods D.","Fedorova N.","Kim H.S.","Shabalina S.A.","Pearson T.R.","Brinkac L.","Tan P.","Nandi T.","Crabtree J.","Badger J.","Beckstrom-Sternberg S.","Saqib M.","Schutzer S.E.","Keim P.","Nierman W.C."],"citationCrossReferences":[{"database":"PubMed","id":"20333227"},{"database":"DOI","id":"10.1093/gbe/evq003"}],"title":"Continuing evolution of Burkholderia mallei through genome reduction and large-scale rearrangements.","publicationDate":"2010","journal":"Genome Biol. Evol.","firstPage":"102","lastPage":"116","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"1106a","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP000573","properties":[{"key":"ProteinId","value":"ABN94857.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_004195445.1","properties":[{"key":"NucleotideSequenceId","value":"NC_009078.1"}]},{"database":"AlphaFoldDB","id":"A3P4L6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A3P4L6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"93063067","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"bpl:BURPS1106A_A1241","properties":[{"key":"Description","value":"-"}]},{"database":"HOGENOM","id":"CLU_089550_0_0_4","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00253","properties":[{"key":"RectionId","value":"UER00456"}]},{"database":"GO","id":"GO:0033735","properties":[{"key":"GoTerm","value":"F:L-aspartate dehydrogenase [NAD(P)+] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009435","properties":[{"key":"GoTerm","value":"P:NAD+ biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.360.10","properties":[{"key":"EntryName","value":"Dihydrodipicolinate Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01265","properties":[{"key":"EntryName","value":"NadX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005106","properties":[{"key":"EntryName","value":"Asp/hSer_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR002811","properties":[{"key":"EntryName","value":"Asp_DH"}]},{"database":"InterPro","id":"IPR020626","properties":[{"key":"EntryName","value":"Asp_DH_prok"}]},{"database":"InterPro","id":"IPR011182","properties":[{"key":"EntryName","value":"L-Asp_DH"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"NF009826","properties":[{"key":"EntryName","value":"PRK13303.1-1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009827","properties":[{"key":"EntryName","value":"PRK13303.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009828","properties":[{"key":"EntryName","value":"PRK13303.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31873:SF6","properties":[{"key":"EntryName","value":"ASPARTATE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31873","properties":[{"key":"EntryName","value":"L-ASPARTATE DEHYDROGENASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01958","properties":[{"key":"EntryName","value":"Asp_DH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03447","properties":[{"key":"EntryName","value":"NAD_binding_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005227","properties":[{"key":"EntryName","value":"Asp_dh_NAD_syn"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRNAHAPVDVAMIGFGAIGAAVYRAVEHDAALRVAHVIVPEHQCDAVRGALGERVDVVSSVDALACRPQFALECAGHGALVDHVVPLLKAGTDCAVASIGALSDLALLDALSNAADAGGATLTLLSGAIGGIDALAAARQGGLDEVRYIGRKPPLGWLGTPAEAICDLRAMAAEQTIFEGSARDAAQLYPRNANVAATVALAGVGLDATRVCLIADPAVTRNVHRIVARGAFGEMSIEMSGKPLPDNPKTSALTAFSAIRALRNRASHCVI","length":271,"molWeight":27747,"crc64":"5703F6D14871D311","md5":"8D3C51007CD5B5E279F117E0CFA6D06C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":2},"uniParcId":"UPI0000441401"}}