ID A0A0R2B502_9LACO Unreviewed; 80 AA. AC A0A0R2B502; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 18-SEP-2019, entry version 18. DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000256|RuleBase:RU003812, ECO:0000256|SAAS:SAAS00921153}; DE EC=6.3.1.5 {ECO:0000256|RuleBase:RU003812, ECO:0000256|SAAS:SAAS00921159}; GN ORFNames=FC35_GL000959 {ECO:0000313|EMBL:KRM73778.1}; OS Lactobacillus coleohominis DSM 14060. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=887896 {ECO:0000313|EMBL:KRM73778.1}; RN [1] {ECO:0000313|EMBL:KRM73778.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14060 {ECO:0000313|EMBL:KRM73778.1}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to CC form NAD. Uses ammonia as a nitrogen source. CC {ECO:0000256|SAAS:SAAS00921154}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) CC + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; CC EC=6.3.1.5; Evidence={ECO:0000256|RuleBase:RU003812, CC ECO:0000256|SAAS:SAAS01125122}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (ammonia route): step 1/1. CC {ECO:0000256|RuleBase:RU004252, ECO:0000256|SAAS:SAAS00921215}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00921152}. CC -!- SIMILARITY: Belongs to the NAD synthetase family. CC {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00921190}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM73778.1}. 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; AZEW01000353; KRM73778.1; -; Genomic_DNA. DR EnsemblBacteria; KRM73778; KRM73778; FC35_GL000959. DR PATRIC; fig|887896.3.peg.1247; -. DR UniPathway; UPA00253; UER00333. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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-EC. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR003694; NAD_synthase. 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|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00702598}; KW Ligase {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702604}; KW Magnesium {ECO:0000256|SAAS:SAAS00921194}; KW Metal-binding {ECO:0000256|SAAS:SAAS00921186}; KW NAD {ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702606}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00702608}. FT DOMAIN 2 70 NAD_synthase. {ECO:0000259|Pfam:PF02540}. FT REGION 1 30 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. SQ SEQUENCE 80 AA; 9233 MW; B8D8464B2565D51E CRC64; MEYLGAPAHL YEKTPTADLE EDRPALPDEQ ALGVSYHEID DYLEGKEVPA TAAQTIEGWF TKTRHKRHLP VSPQDEWWKK //