ID NADE_BURL3 Reviewed; 282 AA. AC Q39AM3; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 02-SEP-2026, entry version 102. DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193}; DE EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193}; GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193}; GN OrderedLocusNames=Bcep18194_B0372; OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / OS R18194 / 383). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; OC Burkholderia cepacia complex. OX NCBI_TaxID=482957; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 2 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form CC NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP- CC Rule:MF_00193}. CC -!- CATALYTIC ACTIVITY: CC Reaction=deamido-NAD(+) + NH4(+) + ATP = AMP + diphosphate + NAD(+) + CC H(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00193}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00193}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00193}. CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP- CC Rule:MF_00193}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000152; ABB10488.1; -; Genomic_DNA. DR RefSeq; WP_011353986.1; NC_007511.1. DR AlphaFoldDB; Q39AM3; -. DR SMR; Q39AM3; -. DR GeneID; 45096760; -. DR KEGG; bur:Bcep18194_B0372; -. DR PATRIC; fig|482957.22.peg.3956; -. DR HOGENOM; CLU_059327_3_0_4; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000002705; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004359; F:glutaminase activity; IEA:InterPro. DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0008795; F:NAD+ synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009435; P:NAD+ biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00553; NAD_synthase; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00193; NadE_ammonia_dep; 1. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR003694; NAD_synthase. DR InterPro; IPR022926; NH(3)-dep_NAD(+)_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00552; nadE; 1. DR NCBIfam; NF001979; PRK00768.1; 1. DR PANTHER; PTHR23090; NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE; 1. DR PANTHER; PTHR23090:SF7; NH(3)-DEPENDENT NAD(+) SYNTHETASE; 1. DR Pfam; PF02540; NAD_synthase; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. PE 3: Inferred from homology; KW ATP-binding; Ligase; Magnesium; Metal-binding; NAD; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..282 FT /note="NH(3)-dependent NAD(+) synthetase" FT /id="PRO_1000099014" FT BINDING 51..58 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 57 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 148 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 168 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 173 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 181 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 188 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 197 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 219 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 268..269 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" SQ SEQUENCE 282 AA; 30798 MW; 405CA09F0D6180D8 CRC64; MTSADYASRQ RAIIAELNVA SEFDAEAEIA RRVEFLAQYL RSTGLRTYVL GISGGVDSST AGRLAQLSVE KLRADGYDAR FVAMRLPNGV QNDEADAQRA LAFVRADEEL TVNVKPAADA MLGALAASGH AFETPAQQDF VHGNIKARER MIAQYAVAGA RRGIVIGTDH AAESLMGFFT KFGDGGADIL PLAGLNKRRV RAVARALGGE ELIVMKVPTA DLEELRPLRP DEHAYGVSYD EIDDFLEGKP VADNVYETVL RFYDASRHKR ALPYTMFDWP TA //