ID NADE_BACAH Reviewed; 272 AA. AC A0RCZ8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 02-SEP-2026, entry version 98. 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=BALH_1767; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam; RX PubMed=17337577; DOI=10.1128/jb.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). 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; CP000485; ABK85091.1; -; Genomic_DNA. DR RefSeq; WP_000174879.1; NC_008600.1. DR AlphaFoldDB; A0RCZ8; -. DR SMR; A0RCZ8; -. DR GeneID; 75085226; -. DR KEGG; btl:BALH_1767; -. DR HOGENOM; CLU_059327_3_0_9; -. DR UniPathway; UPA00253; UER00333. 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 FunFam; 3.40.50.620:FF:000015; NH(3)-dependent NAD(+) synthetase; 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. FT CHAIN 1..272 FT /note="NH(3)-dependent NAD(+) synthetase" FT /id="PRO_1000077532" FT BINDING 45..52 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 51 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 138 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 158 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 163 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 171 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 178 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 258..259 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" SQ SEQUENCE 272 AA; 30101 MW; B58A9792E8075B98 CRC64; MTLQEQIMKA LHVQPVIDPK AEIRKRVDFL KDYVKKTGAK GFVLGISGGQ DSTLAGRLAQ LAVEEIRNEG GNATFIAVRL PYKVQKDEDD AQLALQFIQA DQSVAFDIAS TVDAFSNQYE NLLDESLTDF NKGNVKARIR MVTQYAIGGQ KGLLVIGTDH AAEAVTGFFT KFGDGGADLL PLTGLTKRQG RALLQELGAD ERLYLKMPTA DLLDEKPGQA DETELGITYD QLDDYLEGKT VPADVAEKIE KRYTVSEHKR QVPASMFDDW WK //