ID   NADE_BOVIN              Reviewed;         706 AA.
AC   Q3ZBF0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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.
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   -!- 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}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC       family. {ECO:0000305}.
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DR   EMBL; BC103388; AAI03389.1; -; mRNA.
DR   RefSeq; NP_001029615.1; NM_001034443.2.
DR   AlphaFoldDB; Q3ZBF0; -.
DR   SMR; Q3ZBF0; -.
DR   STRING; 9913.ENSBTAP00000021894; -.
DR   PaxDb; Q3ZBF0; -.
DR   PRIDE; Q3ZBF0; -.
DR   Ensembl; ENSBTAT00000077400; ENSBTAP00000074390; ENSBTAG00000016470.
DR   GeneID; 513400; -.
DR   KEGG; bta:513400; -.
DR   CTD; 55191; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016470; -.
DR   VGNC; VGNC:31865; NADSYN1.
DR   eggNOG; KOG2303; Eukaryota.
DR   GeneTree; ENSGT00390000010152; -.
DR   HOGENOM; CLU_011884_2_0_1; -.
DR   InParanoid; Q3ZBF0; -.
DR   OMA; CEDHFYE; -.
DR   OrthoDB; 283044at2759; -.
DR   TreeFam; TF351426; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000009136; Chromosome 29.
DR   Bgee; ENSBTAG00000016470; Expressed in urinary bladder and 104 other tissues.
DR   ExpressionAtlas; Q3ZBF0; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0034627; P:'de novo' NAD biosynthetic process; IEA:Ensembl.
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..706
FT                   /note="Glutamine-dependent NAD(+) synthetase"
FT                   /id="PRO_0000237576"
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   706 AA;  79400 MW;  AEAA2172BAD602E4 CRC64;
     MGRKVTVATC ALNQWALDFE GNLQRILKSI EIAKHRGARY RLGPELEICG YGCWDHYYES
     DTLLHSLQVL AALLESPVTQ DIICDVGMPV MHRNVRYNCR VIFLNRKILL IRPKMALANE
     GNYRELRWFT PWSRSRQTEE YFLPRMLQDL TKQETVPFGD AVLSTWDTCI GSEVCEELWT
     PHSPHVDMGL DGVEIFTNAS GSHHVLRKAH ARVDLVTMAT TKNGGIYLLA NQKGCDGDRL
     YYDGCALIAM NGSIFAQGSQ FSLDDVEVLT ATLDLEDIRS YRAEISSRNL AASRVSPYPR
     VKVDFALSCH EDLLEPVSEP IEWKYHSPAE EISLGPACWL WDFLRRSRQA GFFLPLSGGV
     DSAATACLVY SMCHQVCEAV KRGNLEVLAD VRTIVNQLSY TPQDPRELCG RVLTTCYMAS
     ENSSQETCDR ARELAQQIGS HHIGLHIDPV VKALVGLFSL VTGASPRFAV HGGSDRENLA
     LQNVQARVRM VIAYLFAQLS LWSRGAPGGL LVLGSANVDE SLLGYLTKYD CSSADINPIG
     GISKTDLRAF VQLCVERFQL PALQSILAAP ATAELEPLAH GRVSQTDEED MGMTYAELSV
     YGRLRKVAKT GPYSMFCKLL DMWRDTCSPR QVADKVKCFF SKYSMNRHKM TTLTPAYHAE
     SYSPDDNRFD LRPFLYNTRW PWQFRCIENQ VLQLEGRQRQ ELDGVD