ID NADE_METMA Reviewed; 256 AA. AC Q8PZP6; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 02-SEP-2026, entry version 134. 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=MM_0446; OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM OS 11833 / OCM 88) (Methanosarcina frisia). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=192952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88; RX PubMed=12125824; RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., RA Fritz H.-J., Gottschalk G.; RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer RT between Bacteria and Archaea."; RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002). 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; AE008384; AAM30142.1; -; Genomic_DNA. DR RefSeq; WP_011032399.1; NC_003901.1. DR AlphaFoldDB; Q8PZP6; -. DR SMR; Q8PZP6; -. DR GeneID; 24850488; -. DR KEGG; mma:MM_0446; -. DR PATRIC; fig|192952.21.peg.538; -. DR eggNOG; arCOG00069; Archaea. DR HOGENOM; CLU_059327_1_1_2; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000000595; Chromosome. 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:000106; Glutamine-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; NF010587; PRK13980.1; 1. DR PANTHER; PTHR23090:SF9; GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE; 1. DR PANTHER; PTHR23090; NH 3 /GLUTAMINE-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..256 FT /note="NH(3)-dependent NAD(+) synthetase" FT /id="PRO_0000152226" FT BINDING 29..36 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 35 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 115 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 135 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 140 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 155 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 164 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 186 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 245..246 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" SQ SEQUENCE 256 AA; 27786 MW; 679195AE15E1D9C9 CRC64; MDLENAQNRI IDFIRDETGR AGVKGVVVGI SGGIDSALTA TLAVKALGKD RVLGIHMPES SLTPAVDSED AEALADWLGI EYRTIDISGI ISAFMAAVPE SESADRLTKG NLKARTRMSL LYFHANRLNR MVIGTGNKTE ILLGYYTKYG DGGVDLEPIG GLYKTGVWEL SSRLGIPESL ITKKPSAGLW AGQTDEADLG ISYVKVDEVL KMIEDGVEPE VILDKTGISA DQLNSVTRRI ERNEHKRKAP PVPELY //