ID A7HLE7_FERNB Unreviewed; 294 AA. AC A7HLE7; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 02-SEP-2026, entry version 104. 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 OrderedLocusNames=Fnod_0878 {ECO:0000313|EMBL:ABS60730.1}; OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1). OC Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales; OC Fervidobacteriaceae; Fervidobacterium. OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS60730.1, ECO:0000313|Proteomes:UP000002415}; RN [1] {ECO:0000313|EMBL:ABS60730.1, ECO:0000313|Proteomes:UP000002415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1 RC {ECO:0000313|Proteomes:UP000002415}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.; RT "Complete sequence of Fervidobacterium nodosum Rt17-B1."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABS60730.1, ECO:0000313|Proteomes:UP000002415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1 RC {ECO:0000313|Proteomes:UP000002415}; RX PubMed=19307556; DOI=10.1073/pnas.0901260106; RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M., RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P., RA Noll K.M.; RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of RT the Thermotogales."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009). 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=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: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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP000771; ABS60730.1; -; Genomic_DNA. DR RefSeq; WP_011994046.1; NC_009718.1. DR AlphaFoldDB; A7HLE7; -. DR STRING; 381764.Fnod_0878; -. DR KEGG; fno:Fnod_0878; -. DR eggNOG; COG0171; Bacteria. DR HOGENOM; CLU_059327_0_0_0; -. DR OrthoDB; 9803818at2; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000002415; 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 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; 2. 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|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00193}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00193}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00193}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00193}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00193}; Reference proteome {ECO:0000313|Proteomes:UP000002415}. FT DOMAIN 10..94 FT /note="NAD/GMP synthase" FT /evidence="ECO:0000259|Pfam:PF02540" FT DOMAIN 142..269 FT /note="NAD/GMP synthase" FT /evidence="ECO:0000259|Pfam:PF02540" FT BINDING 31..38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 37 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 151 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 171 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 176 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 184 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 191 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 200 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" FT BINDING 222 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00193" SQ SEQUENCE 294 AA; 33841 MW; 77A2C74519E0C8AE CRC64; MIFNPKDEII RIEKFIKRTM ETYNFKGAVI GISGGVDSAV VLALLTRTIE KENILALILP ERDSSKESVR DAKLVCNYFG VNYKIFPITG ALRKLGAYSL FPPALFIPES IKISYSKKRW ERYQDPYIMD LKNEGDELFL KGLAYYRIKH RVRMCKLYME AEKRGYCVVG TTNKTELALG LYVKWGDDAV DIEPIKHLYK TQVFELAKHL GVPEKIINKK PTPDLIPGIN DEDAFGIEYS KLDKILFSIE SNEGKVEDID EKLLSKVKEI MRFTKIRELK GLGIDDISNQ KDRW //