ID   NADE_RAT                Reviewed;         725 AA.
AC   Q812E8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glutamine-dependent NAD(+) synthetase;
DE            EC=6.3.5.1 {ECO:0000250|UniProtKB:Q6IA69};
DE   AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
DE   AltName: Full=NAD(+) synthetase;
GN   Name=Nadsyn1; Synonyms=Qns1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Miura Y., Yamashita N., Suda Y.;
RT   "Rat NAD+ synthetase.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the final step of the nicotinamide adenine
CC       dinucleotide (NAD) de novo synthesis pathway, the ATP-dependent
CC       amidation of deamido-NAD using L-glutamine as a nitrogen source.
CC       {ECO:0000250|UniProtKB:Q6IA69}.
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:0000250|UniProtKB:Q6IA69};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24385;
CC         Evidence={ECO:0000250|UniProtKB:Q6IA69};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000250|UniProtKB:Q6IA69}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q6IA69}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC       family. {ECO:0000305}.
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DR   EMBL; AB090805; BAC57897.1; -; mRNA.
DR   RefSeq; NP_852145.1; NM_181480.1.
DR   AlphaFoldDB; Q812E8; -.
DR   SMR; Q812E8; -.
DR   BioGRID; 261873; 1.
DR   STRING; 10116.ENSRNOP00000028175; -.
DR   jPOST; Q812E8; -.
DR   PaxDb; Q812E8; -.
DR   GeneID; 353255; -.
DR   KEGG; rno:353255; -.
DR   UCSC; RGD:727801; rat.
DR   CTD; 55191; -.
DR   RGD; 727801; Nadsyn1.
DR   eggNOG; KOG2303; Eukaryota.
DR   InParanoid; Q812E8; -.
DR   OrthoDB; 283044at2759; -.
DR   PhylomeDB; Q812E8; -.
DR   Reactome; R-RNO-196807; Nicotinate metabolism.
DR   UniPathway; UPA00253; UER00334.
DR   PRO; PR:Q812E8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; ISS:UniProtKB.
DR   GO; GO:0034627; P:'de novo' NAD biosynthetic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   ATP-binding; Ligase; NAD; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..725
FT                   /note="Glutamine-dependent NAD(+) synthetase"
FT                   /id="PRO_0000237580"
FT   DOMAIN          5..275
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   REGION          325..706
FT                   /note="Ligase"
FT                   /evidence="ECO:0000250"
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        357
FT                   /evidence="ECO:0000250"
FT   BINDING         355..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   725 AA;  81511 MW;  4CA8EAFCE183871A CRC64;
     MGRKVTVATC ALNQWALDFE GNFQRILKSI QIAKGKGARY RLGPELEICG YGCWDHYHES
     DTLLHSLQVL AALLDAPATQ DIICDVGMPI MHRNVRYNCL VIFLNRKILL IRPKMALANE
     GNYRELRWFT PWARSRQTEE YVLPRMLQDL TKQETVPFGD VVLATQDTCI GSEICEELWT
     PCSPHVNMGL DGVEIITNAS GSHHVLRKAH TRVDLVTMAT SKNGGIYLLA NQKGCDGHLL
     YYDGCAMIAM NGSIFAQGTQ FSLDDVEVLT ATLDLEDVRS YRAKISSRNL EATRVNPYPR
     VTVDFALSVS EDLLEPVSEP VEWTYHRPEE EISLGPACWL WDFLRRNNQA GFFLPLSGGV
     DSAASACVVY SMCCLVCEAV KSGNQQVLTD VQNLVDESSY TPQDPRELCG RLLTTCYMAS
     ENSSQETHNR ATELAQQIGS YHISLNIDPA VKAILGIFSL VTGKFPRFSA HGGSSRENLA
     LQNVQARIRM VLAYLFAQLS LWSRGARGSL LVLGSANVDE SLLGYLTKYD CSSADINPIG
     GISKTDLRAF VQLCAERFQL PVLQAILSAP ATAELEPLAD GQVSQMDEED MGMTYTELSI
     FGRLRKVAKA GPYSMFCKLL NMWKDSCTPR QVAEKVKRFF SKYSINRHKM TTLTPAYHAE
     NYSPDDNRFD LRPFLYNTRW PWQFLCIDNQ VVQLERKTSQ TLEEQIQEHF KEPSPIWKQL
     LPKDP