ID A0A023X657_9ACTN Unreviewed; 600 AA. AC A0A023X657; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 11-DEC-2019, entry version 28. 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; Rubrobacteraceae; OC Rubrobacter. OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY47691.1, ECO:0000313|Proteomes:UP000025229}; RN [1] {ECO:0000313|EMBL:AHY47691.1, ECO:0000313|Proteomes:UP000025229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY47691.1, RC ECO:0000313|Proteomes:UP000025229}; RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L., RA da Costa M.M.S.; RT "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans RT RSPS-4."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form CC NAD. Uses L-glutamine as a nitrogen source. {ECO:0000256|HAMAP- CC Rule:MF_02090}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + CC H(+) + L-glutamate + NAD(+); Xref=Rhea:RHEA:24384, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.5.1; CC 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 synthetase CC family. {ECO:0000256|HAMAP-Rule:MF_02090, CC ECO:0000256|PIRNR:PIRNR006630}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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 STRING; 42256.RradSPS_2408; -. 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 Proteomes; UP000025229; 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: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, ECO:0000256|PIRNR:PIRNR006630, KW ECO:0000256|RuleBase:RU003811, 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 FT /note="CN hydrolase" FT /evidence="ECO:0000259|PROSITE:PS50263" FT NP_BIND 338..345 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT ACT_SITE 60 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10139" FT ACT_SITE 60 FT /note="Proton acceptor; for glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT ACT_SITE 127 FT /note="For glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT ACT_SITE 163 FT /note="Nucleophile; for glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 133 FT /note="L-glutamine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 190 FT /note="L-glutamine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 196 FT /note="L-glutamine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 421 FT /note="Deamido-NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 445 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 450 FT /note="Deamido-NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 562 FT /note="Deamido-NAD" FT /evidence="ECO:0000256|HAMAP-Rule: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 //