ID   NADE_SYNY3              Reviewed;         558 AA.
AC   P74292;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 135.
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=slr1691;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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}.
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; BA000022; BAA18386.1; -; Genomic_DNA.
DR   PIR; S75927; S75927.
DR   AlphaFoldDB; P74292; -.
DR   SMR; P74292; -.
DR   IntAct; P74292; 1.
DR   STRING; 1148.1653472; -.
DR   PaxDb; P74292; -.
DR   EnsemblBacteria; BAA18386; BAA18386; BAA18386.
DR   KEGG; syn:slr1691; -.
DR   eggNOG; COG0171; Bacteria.
DR   eggNOG; COG0388; Bacteria.
DR   InParanoid; P74292; -.
DR   OMA; VLMPSPY; -.
DR   PhylomeDB; P74292; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; NAD; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..558
FT                   /note="Glutamine-dependent NAD(+) synthetase"
FT                   /id="PRO_0000152244"
FT   DOMAIN          2..262
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          284..558
FT                   /note="Ligase"
FT   ACT_SITE        42
FT                   /note="Proton acceptor; for glutaminase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   ACT_SITE        117
FT                   /note="For glutaminase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   ACT_SITE        153
FT                   /note="Nucleophile; for glutaminase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         123
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         190
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         196
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         304..311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         387
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         416
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
FT   BINDING         526
FT                   /ligand="deamido-NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:58437"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02090"
SQ   SEQUENCE   558 AA;  61076 MW;  1F794E66DFBC6616 CRC64;
     MFTIALAQLN PTIGAIAENA EKIVTAALQA QARGADLLLT PELALCGYPP KDLLLNPSFV
     EQLEEELQWL AEKMPPSIAI LVGTVTPHHQ AERQGQKKLW NSAVLIEQGQ IKQWFHKCLL
     PTYDVFDEDR YFASAAKSEY FIYKNVKIGV TICEDLWNDE AFWGQKFYQV NPLMDLIDQG
     VNLVVNLSAS PYSCGKHYLR ESLISHSAKR FNVPLIYVNQ VGGNDDLIFD GGSFAVNSQG
     KIIGRSPLFQ EDLALLSYDL SSGELTGQKL ASLPMVDTEE LWQALVLGVG DYLHKCGFSK
     AILGLSGGID SSLVAAIAVE ALGKENVLGI LMPSPYSSDH SIQDALALAK NLGMNTQTIP
     IGPIMATYDQ ALVPLFQDAP FGLAEENLQS RIRGNLLMAI ANKFGHLLLS TGNKSELAVG
     YCTLYGDMNG GLAAIADVPK TQVFELCRWL NREQTIIPPS VLTKPPSAEL KPGQVDTDSL
     PPYDVLDGIL GRLVEKHQSP QEIINAGFER EVVLKICQLV QKSEFKRRQA APGLKVTDRA
     FGSGWRMPIA QAFHPQGS