ID NADE_STRR6 Reviewed; 274 AA. AC P65509; Q97Q13; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 106. 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=spr1276; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). 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; AE007317; AAL00080.1; -; Genomic_DNA. DR PIR; C98031; C98031. DR RefSeq; WP_000058033.1; NC_003098.1. DR AlphaFoldDB; P65509; -. DR SMR; P65509; -. DR STRING; 171101.spr1276; -. DR PaxDb; 171101-spr1276; -. DR GeneID; 45653323; -. DR KEGG; spr:spr1276; -. DR PATRIC; fig|171101.6.peg.1385; -. DR eggNOG; COG0171; Bacteria. DR HOGENOM; CLU_059327_3_0_9; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000000586; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; IBA:GO_Central. 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; KW Reference proteome. FT CHAIN 1..274 FT /note="NH(3)-dependent NAD(+) synthetase" FT /id="PRO_0000152207" FT BINDING 46..53 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 140 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 160 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 165 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 173 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 180 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 189 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 211 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" FT BINDING 260..261 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193" SQ SEQUENCE 274 AA; 30135 MW; 10972D8AF4A9044C CRC64; MSLQETIIQE LGVKPVIDAQ EEIRRSIDFL KRYLKKHPFL KTFVLGISGG QDSTLAGRLA QLAMEELRAE TGDDSYKFIA VRLPYGVQAD EADAQKALAF IQPDVSLVVN IKESADAMTA AVEATGSPVS DFNKGNIKAR CRMIAQYALA GSHSGAVIGT DHAAENITGF FTKFGDGGAD ILPLYRLNKR QGKQLLQKLG AEPALYEKIP TADLEEDKPG LADEVALGVT YAEIDDYLEG KTISPEAQAT IENWWHKGQH KRHLPITVFD DFWE //