ID A0A0E3LIX5_9EURY Unreviewed; 265 AA. AC A0A0E3LIX5; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 20-DEC-2017, entry version 13. 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; Methanomicrobia; Methanosarcinales; OC 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 CC form NAD. Uses ammonia as a nitrogen source. {ECO:0000256|HAMAP- CC Rule:MF_00193}. CC -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + NH(3) = AMP + CC diphosphate + NAD(+). {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|HAMAP-Rule:MF_00193, 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 EnsemblBacteria; AKB46781; AKB46781; MSKOL_1004. DR KEGG; mek:MSKOL_1004; -. DR PATRIC; fig|1434099.4.peg.1219; -. DR KO; K01916; -. DR OrthoDB; POG093Z07V0; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000033075; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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; -; 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 PANTHER; PTHR23090; PTHR23090; 1. DR Pfam; PF02540; NAD_synthase; 1. DR TIGRFAMs; TIGR00552; nadE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00193, KW ECO:0000256|RuleBase:RU003811}; KW Complete proteome {ECO:0000313|Proteomes:UP000033075}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00193, KW ECO:0000256|RuleBase:RU003811, ECO:0000313|EMBL:AKB46781.1}; 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|HAMAP-Rule:MF_00193, KW ECO:0000256|RuleBase:RU003811}. FT DOMAIN 18 260 NAD_synthase. {ECO:0000259|Pfam:PF02540}. FT NP_BIND 39 46 ATP. {ECO:0000256|HAMAP-Rule:MF_00193}. FT NP_BIND 255 256 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_00193}. FT METAL 45 45 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00193}. FT METAL 150 150 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00193}. FT BINDING 125 125 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_00193}. FT BINDING 145 145 ATP. {ECO:0000256|HAMAP-Rule:MF_00193}. FT BINDING 158 158 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_00193}. FT BINDING 165 165 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_00193}. FT BINDING 174 174 ATP. {ECO:0000256|HAMAP-Rule:MF_00193}. FT BINDING 196 196 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT 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 //