ID   NADE_SCHPO              Reviewed;         700 AA.
AC   O74940;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Putative glutamine-dependent NAD(+) synthetase;
DE            EC=6.3.5.1;
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
GN   ORFNames=SPCC553.02;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC       family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA19255.1; -; Genomic_DNA.
DR   PIR; T41401; T41401.
DR   RefSeq; NP_587771.1; NM_001022764.2.
DR   AlphaFoldDB; O74940; -.
DR   SMR; O74940; -.
DR   BioGRID; 276038; 2.
DR   STRING; 4896.SPCC553.02.1; -.
DR   iPTMnet; O74940; -.
DR   MaxQB; O74940; -.
DR   PaxDb; O74940; -.
DR   PRIDE; O74940; -.
DR   EnsemblFungi; SPCC553.02.1; SPCC553.02.1:pep; SPCC553.02.
DR   GeneID; 2539475; -.
DR   KEGG; spo:SPCC553.02; -.
DR   PomBase; SPCC553.02; -.
DR   VEuPathDB; FungiDB:SPCC553.02; -.
DR   eggNOG; KOG2303; Eukaryota.
DR   HOGENOM; CLU_011884_2_0_1; -.
DR   InParanoid; O74940; -.
DR   OMA; CEDHFYE; -.
DR   PhylomeDB; O74940; -.
DR   Reactome; R-SPO-196807; Nicotinate metabolism.
DR   UniPathway; UPA00253; UER00334.
DR   PRO; PR:O74940; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; ISO:PomBase.
DR   GO; GO:0009435; P:NAD biosynthetic process; ISO:PomBase.
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..700
FT                   /note="Putative glutamine-dependent NAD(+) synthetase"
FT                   /id="PRO_0000152247"
FT   DOMAIN          5..275
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          327..700
FT                   /note="Ligase"
FT   ACT_SITE        45
FT                   /note="Proton acceptor; for glutaminase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT   ACT_SITE        114
FT                   /note="For glutaminase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT   ACT_SITE        175
FT                   /note="Nucleophile; for glutaminase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT   ACT_SITE        359
FT                   /evidence="ECO:0000250"
FT   BINDING         357..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   700 AA;  79520 MW;  F915943317F62FED CRC64;
     MERYVTIASC QLNQWAMDFE GNRLRIIDSI KEAKRQNASL RVGPELEVTG YGCEDHFLES
     DTYYHSWEML CSIIHDPDCQ DILLDIGMPV MHKAMRHNCR ILALNGKILL IRPKIWLCDD
     GNFRESRWFT PWLRPRVVET HYLPTFVAKS LNQTTVPIGD AILQCNETVV GVETCEELFT
     PNSPHIDMAL DGVEIFINAS GSHHELRKLT TRVNLIQNAT EKCGGIYLYS NQRGCDGGRL
     YYDGSSMIFA NGKMLAQGHQ FSLKDVEVIS ATVDVDTVRS YRFQPSHGIQ GVTRPSYERI
     HVNFSLSSYQ QDYDIYRKPT DPIEVTIPLP EEEITFGPAC WLWDYLRRSH AAGFFLPLSG
     GLDSCSTAVL VYSMCRIVCK AMEEDDAQVL SDVRRIVGDP SYSSTDPKKL LNHLFYTAFM
     GSEHSSKETR SRAKELSSLI GSYHTDVNID TMTSAVVKLF ALVTGKTPQF RSNGGTNAEN
     LALQNIQARS RMLLGYLFAQ LLPWVRGYSG SLLVLGSSNV DECLRGYLTK YDCSSADINP
     IGGISKTDLK SFLRYAKEAL DLPILQEFLD ATPTAELEPT TESYVQSDEA DMGMTYAELS
     VFGRLRKISK CGPYSMFTQL MHQWGDRLSP SQVAEKVKRF FHYYGINRHK MTTLTPSYHA
     ETYGVDDNRY DLRQFLYPSW TWQNKKIDAL ASKFEQHQRK