ID A0A023X657_9ACTN Unreviewed; 600 AA. AC A0A023X657; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 16-JAN-2019, entry version 25. DE RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}; DE EC=6.3.5.1 {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}; DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}; GN Name=nadE {ECO:0000256|HAMAP-Rule:MF_02090}; GN ORFNames=RradSPS_2408 {ECO:0000313|EMBL:AHY47691.1}; OS Rubrobacter radiotolerans. OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; OC Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY47691.1}; RN [1] {ECO:0000313|EMBL:AHY47691.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY47691.1}; RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., RA Albuquerque L.L., da Costa M.M.S.; RT "Complete genome sequence of the Radio-Resistant Rubrobacter RT radiotolerans RSPS-4."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to CC form NAD. Uses L-glutamine as a nitrogen source. CC {ECO:0000256|HAMAP-Rule:MF_02090}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + CC diphosphate + H(+) + L-glutamate + NAD(+); Xref=Rhea:RHEA:24384, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; CC EC=6.3.5.1; Evidence={ECO:0000256|HAMAP-Rule:MF_02090, CC ECO:0000256|PIRNR:PIRNR006630}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}. CC -!- SIMILARITY: Belongs to the NAD synthetase family. CC {ECO:0000256|RuleBase:RU003811}. CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD CC synthetase family. {ECO:0000256|HAMAP-Rule:MF_02090, CC ECO:0000256|PIRNR:PIRNR006630}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02090}. 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; CP007514; AHY47691.1; -; Genomic_DNA. DR EnsemblBacteria; AHY47691; AHY47691; RradSPS_2408. DR KEGG; rrd:RradSPS_2408; -. DR PATRIC; fig|42256.3.peg.2452; -. DR KO; K01950; -. DR UniPathway; UPA00253; UER00334. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule. 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 Gene3D; 3.60.110.10; -; 1. DR HAMAP; MF_02090; NadE_glutamine_dep; 1. DR InterPro; IPR003010; C-N_Hydrolase. DR InterPro; IPR036526; C-N_Hydrolase_sf. DR InterPro; IPR014445; Gln-dep_NAD_synthase. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR003694; NAD_synthase. DR InterPro; IPR000132; Nitrilase/CN_hydratase_CS. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR23090; PTHR23090; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR Pfam; PF02540; NAD_synthase; 1. DR PIRSF; PIRSF006630; NADS_GAT; 1. DR SUPFAM; SSF56317; SSF56317; 1. DR TIGRFAMs; TIGR00552; nadE; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. DR PROSITE; PS00920; NITRIL_CHT_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02090, KW ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00702598}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02090, KW ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00702604}; KW NAD {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630, KW ECO:0000256|RuleBase:RU003811, ECO:0000256|SAAS:SAAS00702606}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02090, KW ECO:0000256|PIRNR:PIRNR006630, ECO:0000256|RuleBase:RU003811, KW ECO:0000256|SAAS:SAAS00702608}. FT DOMAIN 20 260 CN hydrolase. {ECO:0000259|PROSITE: FT PS50263}. FT NP_BIND 338 345 ATP. {ECO:0000256|HAMAP-Rule:MF_02090}. FT ACT_SITE 60 60 Proton acceptor. {ECO:0000256|PROSITE- FT ProRule:PRU10139}. FT ACT_SITE 60 60 Proton acceptor; for glutaminase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT ACT_SITE 127 127 For glutaminase activity. FT {ECO:0000256|HAMAP-Rule:MF_02090}. FT ACT_SITE 163 163 Nucleophile; for glutaminase activity. FT {ECO:0000256|HAMAP-Rule:MF_02090}. FT BINDING 133 133 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 190 190 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 196 196 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 421 421 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 445 445 ATP. {ECO:0000256|HAMAP-Rule:MF_02090}. FT BINDING 450 450 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 562 562 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_02090}. SQ SEQUENCE 600 AA; 65935 MW; 7291F9822B054BF2 CRC64; MKRPPLARRG HRRRGIIWRM RVALAQVNTT VGDIWGNVEK LSEALGRAVE SGADLVAFPE LALTGYPPED LLLRPGFIGD NLKALEEFRA CVPEDVVAAV GFVDLGLDLF NACAVISGGE VLDRYHKRYL PNYGVFDENR YFREGTGSSL LDLDGTLVGV NVCEDIWYPG GPGREQALGG ASVLVNVSAS PYHRLKGATR ERMLSVRASD YGCYVVMCNL VGGQDELVFD GHSVVFDPEG ELVARAKQFE EDLLLVDIFP EEALMRRLHD SRPRKEDRTG EAPCVVSVPV SVGKVSPVES EEPRREPVLP EEGEVLAALE LGLRDYFGKN GFTKAVLGLS GGVDSSLVAA VAARALGPEN VVGVLMPSRY TSDLSNTDAY ALAEALGIET KVVPIGPAFD AYREMLADLF AGTEEDITEE NLQSRVRGNI VMGLSNKFGW IVLSTGNKSE MSVGYSTLYG DMAGGFALIR DVPKTLVYRI CRYINSSEGR EVIPESVLTK EPSAELREDQ RDSDSLPPYD VLDPILEAYI EEDKGIGQIV ALGFDEADVR RVVGLVDRAE YKRRQAPVGI KVTTRSFGRD RRMPITNRYT ERERPRLKTP //