ID A0A3A9ZCN3_9ACTN Unreviewed; 615 AA. AC A0A3A9ZCN3; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 28-JUN-2023, entry version 20. 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; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; 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 sediment."; RL Int. J. Syst. Evol. Microbiol. 64:819-826(2014). 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|ARBA:ARBA00005188, CC ECO:0000256|HAMAP-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|ARBA:ARBA00007145, ECO:0000256|HAMAP- CC Rule:MF_02090, 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A3A9ZCN3; -. DR EnsemblBacteria; RKN45935; RKN45935; D7294_05775. DR OrthoDB; 9760188at2; -. DR UniPathway; UPA00253; UER00334. DR Proteomes; UP000272474; Unassembled WGS sequence. 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:0000257; F:nitrilase activity; IEA:UniProt. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd07570; GAT_Gln-NAD-synth; 1. DR CDD; cd00553; NAD_synthase; 1. DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1. DR Gene3D; 3.40.50.620; HUPs; 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:SF9; GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE; 1. DR PANTHER; PTHR23090; NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR Pfam; PF02540; NAD_synthase; 1. DR PIRSF; PIRSF006630; NADS_GAT; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_02090}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}; KW NAD {ECO:0000256|HAMAP-Rule:MF_02090, ECO:0000256|PIRNR:PIRNR006630}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_02090}; Reference proteome {ECO:0000313|Proteomes:UP000272474}. FT DOMAIN 32..287 FT /note="CN hydrolase" FT /evidence="ECO:0000259|PROSITE:PS50263" FT REGION 504..531 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 72 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10139" FT ACT_SITE 72 FT /note="Proton acceptor; for glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT ACT_SITE 154 FT /note="For glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT ACT_SITE 190 FT /note="Nucleophile; for glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 160 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 217 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 223 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 359..366 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 436 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 465 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 581 FT /ligand="deamido-NAD(+)" FT /ligand_id="ChEBI:CHEBI:58437" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000256|HAMAP-Rule: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 //