ID A0A3A9ZCN3_9ACTN Unreviewed; 615 AA. AC A0A3A9ZCN3; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 05-JUN-2019, entry version 5. 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=D7294_05775 {ECO:0000313|EMBL:RKN45935.1}; OS Streptomyces hoynatensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1141874 {ECO:0000313|EMBL:RKN45935.1, ECO:0000313|Proteomes:UP000272474}; RN [1] {ECO:0000313|EMBL:RKN45935.1, ECO:0000313|Proteomes:UP000272474} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 29097 {ECO:0000313|EMBL:RKN45935.1, RC ECO:0000313|Proteomes:UP000272474}; RX PubMed=24243968; DOI=10.1099/ijs.0.055640-0; RA Veyisoglu A., Sahin N.; RT "Streptomyces hoynatensis sp. nov., isolated from deep marine RT sediment."; RL Int. J. Syst. Evol. Microbiol. 64:819-826(2014). 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 -!- 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:RKN45935.1}. 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; RBAL01000002; RKN45935.1; -; Genomic_DNA. DR UniPathway; UPA00253; UER00334. DR Proteomes; UP000272474; Unassembled WGS sequence. 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 Complete proteome {ECO:0000313|Proteomes:UP000272474}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000272474}. FT DOMAIN 32 287 CN hydrolase. {ECO:0000259|PROSITE: FT PS50263}. FT NP_BIND 359 366 ATP. {ECO:0000256|HAMAP-Rule:MF_02090}. FT REGION 504 531 Disordered. {ECO:0000256|MobiDB-lite: FT A0A3A9ZCN3}. FT ACT_SITE 72 72 Proton acceptor. {ECO:0000256|PROSITE- FT ProRule:PRU10139}. FT ACT_SITE 72 72 Proton acceptor; for glutaminase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT ACT_SITE 154 154 For glutaminase activity. FT {ECO:0000256|HAMAP-Rule:MF_02090}. FT ACT_SITE 190 190 Nucleophile; for glutaminase activity. FT {ECO:0000256|HAMAP-Rule:MF_02090}. FT BINDING 160 160 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 217 217 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 223 223 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 436 436 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 465 465 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_02090}. FT BINDING 581 581 Deamido-NAD. {ECO:0000256|HAMAP-Rule: FT MF_02090}. SQ SEQUENCE 615 AA; 66634 MW; E8C0A6BACFFD64B7 CRC64; MARERRPPPG PRGRRRPHCV NRTIRLGGVP QLRLALNQID STVGDLPGNA DAVLRWTRHG VERGAHLVVF PEMMLTGYPV EDLALRSSFV SAAREALRGL AARLAAEGLG ETPVLLGYLD RAEAVPERPW QPVGTPQNAA AVLHRGRVVL SFAKHHLPNY GVFDEFRYFV PGETLPVVRV HGVDVALAIC EDLWQDGGRV PAARAAGAGL LVAINASPYE VAKEDVRLDL VRKRAQEAGC TLAYLAMTGG QDELVYDGDS LVVDRNGEVL LRGPQFEEEC LLVDLELPPA AAEPPGGVVE DGLRIDRVTL SEDPLPPYEP AYPGGLAPAL DDAEVRYRAL VTGLRAYVRK NGFGSVLIGL SGGVDSALCA VLACDALGAE HVFALSMPSA YSSEHSRTDA EELAARTGLT LRTVPIAPMF DAYMGAVGLT GLAEENLQSR LRGTLLMAVS NQEGHIVLAP GNKSELAVGY STLYGDSVGA YGPIKDLYKT GVYQLARWRN RAAAERGETP PIPENTLVKP PSAELRPGQV DTDSLPDYDV LDRVLELYVD RDTGREGIIA AGFDPELVTR VLRLVDTAEY KRRQYPPGTK ISPKVFGKDR RLPLTNRWRE DGLPT //