ID   NADE_MACFA              Reviewed;         706 AA.
AC   Q4R5Y2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 71.
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; ORFNames=QtsA-19858;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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; AB169410; BAE01493.1; -; mRNA.
DR   RefSeq; NP_001270170.1; NM_001283241.1.
DR   AlphaFoldDB; Q4R5Y2; -.
DR   SMR; Q4R5Y2; -.
DR   STRING; 9541.ENSMFAP00000042654; -.
DR   eggNOG; KOG2303; Eukaryota.
DR   OrthoDB; 3030505at2759; -.
DR   UniPathway; UPA00253; UER00334.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
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   CDD; cd07570; GAT_Gln-NAD-synth; 1.
DR   CDD; cd00553; NAD_synthase; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00552; nadE; 1.
DR   PANTHER; PTHR23090:SF9; GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE; 1.
DR   PANTHER; PTHR23090; NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PIRSF; PIRSF006630; NADS_GAT; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 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_0000237578"
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;  79071 MW;  1B3AF9BF3EF0523B CRC64;
     MGRKVTVATC ALNQWALDFE GNLQRILKSI EIAKNRGARY RLGPELEICG YGCWDHYYES
     DTLLHSFQVL AALLESPVTQ DIICDVGMPV MHRNVRYNCR VIFLSRKILL IRPKMALANE
     GNYRELRWFT PWSRSRHTEE YLLPRMIQDL TKQETAPFGD AVLATWDTCI GSEICEELWT
     PHSPHIDMGL DGVEIITNAS GSHHVLRKAN TRVDLVTMAT SKNGGIYLLA NQKGCDGDRL
     YYDGCAMIAM NGSVFAQGSQ FSLDDVEVLT ATLDLEDVRS YRAEISSRNL AASRASPYPR
     VKVDFALSCH EDLLAPVSEP IEWKYHSPEE EISLGPACWL WDFLRRSQQG GFLLPLSGGV
     DSAATACLVY SMCCQVCKSV RSGNQEVLAD VRTIVNQISY TPQDPRDLCG HILTTCYMAS
     KNSSQETCTR ARELAQQIGS HHISLNIDPA VKAVTGIFSL VTGKSPLFAA HGGSSRENLA
     LQNVQARIRM VLAYLFAQLS LWSRGIRGGL LVLGSANVDE SLLGYLTKYD CSSADINPIG
     GISKTDLRAF VQFCIERFQL TALQSIISAP VTAELEPLAD GQVSQTDEED MGMTYAELSV
     YGKLRKVAKM GPYSMFCKLL GMWRHVCTPR QVADKVKWFF TKHSMNRHKM TTLTPAYHAE
     NYSPEDNRFD LRPFLYNTSW PWQFRCIENQ VLQLERAAPQ SLDGVD
//