ID   NADE_XYLFT              Reviewed;         545 AA.
AC   Q87D47;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_02090};
DE            EC=6.3.5.1 {ECO:0000255|HAMAP-Rule:MF_02090};
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_02090};
GN   Name=nadE {ECO:0000255|HAMAP-Rule:MF_02090}; OrderedLocusNames=PD_0839;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC       NAD. Uses L-glutamine as a nitrogen source. {ECO:0000255|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:0000255|HAMAP-Rule:MF_02090};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_02090}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_02090, ECO:0000305}.
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DR   EMBL; AE009442; AAO28707.1; -; Genomic_DNA.
DR   RefSeq; WP_004572843.1; NC_004556.1.
DR   AlphaFoldDB; Q87D47; -.
DR   SMR; Q87D47; -.
DR   EnsemblBacteria; AAO28707; AAO28707; PD_0839.
DR   GeneID; 58016383; -.
DR   KEGG; xft:PD_0839; -.
DR   HOGENOM; CLU_022313_2_0_6; -.
DR   OMA; VLMPSPY; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000002516; 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-EC.
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; 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; Ligase; NAD; Nucleotide-binding.
FT   CHAIN           1..545
FT                   /note="Glutamine-dependent NAD(+) synthetase"
FT                   /id="PRO_0000306414"
FT   DOMAIN          5..247
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          269..545
FT                   /note="Ligase"
FT   ACT_SITE        46
FT                   /note="Proton acceptor; for glutaminase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   ACT_SITE        113
FT                   /note="For glutaminase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   ACT_SITE        151
FT                   /note="Nucleophile; for glutaminase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         119
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         177
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         183
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         292..299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         375
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         399
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         404
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         516
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
SQ   SEQUENCE   545 AA;  59373 MW;  5F4E1CC3F34F0420 CRC64;
     MSEFLRIAMA QFDFPVGAVA QNAERIIALI EQARDEHGAD VVMFPELALS GYPPEDLLLR
     PGFLAHCQVA IERIAAATHG IVAVVGWPQS AGSVVYNVAS VLCDGQVEQT YRKRELPNYA
     VFDERRYFEV DPNGSRCVFK VKGVPVGVLI CEDLWFSEPL ADTVCGGAEL VLVPNASPYE
     RGKHAQRDAL LAERARETGA AIAYLNVVGG QDALVFDGAS VVVDGHGRVH PAAAAFSDQW
     LVVDYMRSER RFVPLQWVVE SEVSINALVW RAVVRGVQDY CRKNGFSKVW VGLSGGIDSA
     LVLAIAVDAL GADQVTAVRL PSRYTAELSN DLAAEQCHSL GVRLETVAIE PVFEGLLAAL
     GPLFAGMAPD ATEENLQSRS RGVILMALAN KFGGLLLTTG NKSEYAVGYA TIYGDMCGGY
     APLKDIYKSQ VFELAQWRNR VSDVLAIPPG VIHRPPSAEL RAQQTDQDSL PPYEVLDGIL
     SLYVDQEQSR EDIIAAGYAA GVVDYVLNLV RINEWKRHQA APGPKVSQRA FGRERRYPIS
     NAYRG