ID A0A0E3LIX5_9EURY Unreviewed; 265 AA. AC A0A0E3LIX5; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 13-SEP-2023, entry version 35. DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003812}; DE EC=6.3.1.5 {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003812}; GN Name=nadE {ECO:0000256|HAMAP-Rule:MF_00193}; GN ORFNames=MSKOL_1004 {ECO:0000313|EMBL:AKB46781.1}; OS Methanosarcina sp. Kolksee. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=1434099 {ECO:0000313|EMBL:AKB46781.1, ECO:0000313|Proteomes:UP000033075}; RN [1] {ECO:0000313|EMBL:AKB46781.1, ECO:0000313|Proteomes:UP000033075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kolksee {ECO:0000313|EMBL:AKB46781.1, RC ECO:0000313|Proteomes:UP000033075}; RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D., RA Metcalf M.E., Whitaker R.J., Metcalf W.W.; RT "Methanogenic archaea and the global carbon cycle."; RL Submitted (JUL-2014) 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:0000256|HAMAP- CC Rule:MF_00193}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + CC NAD(+); 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:0000256|HAMAP-Rule:MF_00193, CC ECO:0000256|RuleBase:RU003812}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_00193, ECO:0000256|RuleBase:RU004252}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00193}. CC -!- SIMILARITY: Belongs to the NAD synthetase family. CC {ECO:0000256|ARBA:ARBA00005859, ECO:0000256|HAMAP-Rule:MF_00193, CC ECO:0000256|RuleBase:RU003811}. 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; CP009524; AKB46781.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0E3LIX5; -. DR EnsemblBacteria; AKB46781; AKB46781; MSKOL_1004. DR KEGG; mek:MSKOL_1004; -. DR PATRIC; fig|1434099.4.peg.1219; -. DR HOGENOM; CLU_059327_1_1_2; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000033075; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00193}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003811}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00193}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00193}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00193, ECO:0000256|RuleBase:RU003811}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00193}. FT DOMAIN 18..260 FT /note="NAD/GMP synthase" FT /evidence="ECO:0000259|Pfam:PF02540" FT BINDING 39..46 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 45 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 125 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 150 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 158 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 165 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 174 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 196 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 255..256 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" SQ SEQUENCE 265 AA; 28870 MW; 46CAD3F32EC8E0E4 CRC64; MPDEYQGIDS MNLEIAQNRI IDFIRNETRK AGVDGAVVGI SGGIDSALAA TLTVKALGKD KVLGIHMPES GLTTSEDSKD AKTLADWLGI EFQTIGISGI ISAFMAAVPE SESADRLSKG NLKARIRMSL LYFHANRMNR MVIGTGNKTE ILLGYFTKYG DGGVDLEPIG GLYKTEVWEL SRRLGVPDSL ITKKPSAGLW AGQTDEAELG ISYLKVDEVL KRLEQNEDPE TILKTPGISA EQLNSVMNRI ERSEHKRNAP PVPPN //