ID A0A087NIH5_9SPHN Unreviewed; 552 AA. AC A0A087NIH5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 02-OCT-2024, entry version 39. 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=IL54_4145 {ECO:0000313|EMBL:KFL48928.1}; OS Sphingobium sp. ba1. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL48928.1, ECO:0000313|Proteomes:UP000029094}; RN [1] {ECO:0000313|EMBL:KFL48928.1, ECO:0000313|Proteomes:UP000029094} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094}; RA Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M., RA Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.; RT "Draft genome sequence of a Kanamycin and Nickel resistant bacterium RT Sphingobium species."; RL Submitted (JUL-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|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:KFL48928.1}. 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; JPPQ01000006; KFL48928.1; -; Genomic_DNA. DR RefSeq; WP_037472166.1; NZ_JPPQ01000006.1. DR AlphaFoldDB; A0A087NIH5; -. DR PATRIC; fig|1522072.3.peg.316; -. DR eggNOG; COG0171; Bacteria. DR eggNOG; COG0388; Bacteria. DR OrthoDB; 9760188at2; -. DR UniPathway; UPA00253; UER00334. DR Proteomes; UP000029094; 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: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; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00552; nadE; 1. 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 PROSITE; PS50263; CN_HYDROLASE; 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}. FT DOMAIN 5..247 FT /note="CN hydrolase" FT /evidence="ECO:0000259|PROSITE:PS50263" FT ACT_SITE 43 FT /note="Proton acceptor; for glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT ACT_SITE 112 FT /note="For glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT ACT_SITE 148 FT /note="Nucleophile; for glutaminase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 118 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 174 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 180 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 290..297 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 373 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 397 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02090" FT BINDING 402 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 523 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 552 AA; 60558 MW; D96C6421E1DF396F CRC64; MTDKLVIALA QMTQSVGDLA ANADAMLEWR ARAMDADLIV YPELQLIGYP PEDLVLKPAL VERANQELDR LAQATGDGGP AMLVGTVVAA QGVLFNVVAL LEGGAVTAIR QKRELPNYGT FDEKRLFAPG PLPAPIDFKG VKIGVPICED IWFPFVTAHL KAQGADILIS PNGSPYEVDK DDRRTNGVAG TRVRETNLPL AYLNRVGGQD ELVFDGASFV MNADLSIAHQ LPDWDEALVL TIWEKQAGQW VCLPGDRHVL DDRPADIYNA MVLGLRDYVN RNRFPGVVLG LSGGIDSALS AAVAVDALGA DRVWCVMMPS RFTSQDSLDD AVACARLLGV RYDSIPIEPA VGAFDTMLGD VFAERQRDLT EENIQSRIRG LTLMALSNKF GHMLLTTGNK SEMSVGYATI YGDMAGGYSV LKDAYKTTVF DLCRWRNANV PTLGEDFGPA GPVMPERVIS KPPSAELRAD QRDDDSLPPY EVLDPILYGL VEEELSVEQL VARGFERETV ARIERLLYVA EYKRRQSPPG VKLGTRNFGR DRRYPITNAF RT //