ID NADE_BURMA Reviewed; 284 AA. AC Q62CU8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 105. 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=BMAA0760; OS Burkholderia mallei (strain ATCC 23344). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=243160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23344; RX PubMed=15377793; DOI=10.1073/pnas.0403306101; RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S., RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y., RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C., RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.; RT "Structural flexibility in the Burkholderia mallei genome."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004). 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; CP000011; AAU46930.1; -; Genomic_DNA. DR RefSeq; WP_004201926.1; NC_006349.2. DR AlphaFoldDB; Q62CU8; -. DR SMR; Q62CU8; -. DR GeneID; 92976563; -. DR KEGG; bma:BMAA0760; -. DR PATRIC; fig|243160.12.peg.4281; -. DR eggNOG; COG0171; Bacteria. DR HOGENOM; CLU_059327_3_0_4; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000006693; 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..284 FT /note="NH(3)-dependent NAD(+) synthetase" FT /id="PRO_1000099008" 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 284 AA; 30863 MW; 8AE2C18E0B0BCEAF CRC64; MSRPDQAARR RAIAAELHVS PTFDARDEAE RRIGFVADYL RTAGLRACVL GISGGIDSST AGRLAQLAVE RLRASGYDAR FVAMRLPYGA QHDEADARRA LAFVRADETL TVDVKPAADA MLAALAAGGL AYLDHAQQDF VLGNIKARER MIAQYAVAGA RNGVVIGTDH AAESVMGFFT KFGDGGADVL PLAGLTKRRV RALARMLGAD EPLVLKTPTA DLETLRPQRP DEHAYGITYE QIDDFLEGKP MDDAVAETVL RFYDATHHKR ALPYTMFDWP GHPA //