NADE_YEAST
ID NADE_YEAST Reviewed; 714 AA.
AC P38795; D3DL24;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase;
DE EC=6.3.5.1;
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
GN Name=QNS1; OrderedLocusNames=YHR074W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {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; U10556; AAB68889.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06768.1; -; Genomic_DNA.
DR PIR; S46811; S46811.
DR RefSeq; NP_011941.1; NM_001179204.1.
DR AlphaFoldDB; P38795; -.
DR SMR; P38795; -.
DR BioGRID; 36508; 173.
DR DIP; DIP-5592N; -.
DR IntAct; P38795; 3.
DR MINT; P38795; -.
DR STRING; 4932.YHR074W; -.
DR iPTMnet; P38795; -.
DR MaxQB; P38795; -.
DR PaxDb; P38795; -.
DR PRIDE; P38795; -.
DR EnsemblFungi; YHR074W_mRNA; YHR074W; YHR074W.
DR GeneID; 856473; -.
DR KEGG; sce:YHR074W; -.
DR SGD; S000001116; QNS1.
DR VEuPathDB; FungiDB:YHR074W; -.
DR eggNOG; KOG2303; Eukaryota.
DR GeneTree; ENSGT00390000010152; -.
DR HOGENOM; CLU_011884_2_0_1; -.
DR InParanoid; P38795; -.
DR OMA; CEDHFYE; -.
DR BioCyc; YEAST:MON3O-845; -.
DR Reactome; R-SCE-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00334.
DR PRO; PR:P38795; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38795; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IDA:SGD.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IDA:SGD.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:SGD.
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 1: Evidence at protein level;
KW ATP-binding; Ligase; NAD; Nucleotide-binding; Reference proteome.
FT CHAIN 1..714
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000152248"
FT DOMAIN 5..275
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 329..714
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 361
FT /evidence="ECO:0000250"
FT BINDING 359..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 714 AA; 80686 MW; ED8C723550F9E8A9 CRC64;
MSHLITLATC NLNQWALDFE GNRDRILQSI KIAKERGARL RVGPELEITG YGCLDHFLEN
DVCLHSWEMY AQIIKNKETH GLILDIGMPV LHKNVRYNCR LLSLDGEILF IRPKIWLAND
GNYREMRFFT PWMKPGVVED FILPPEIQKV TGQRLVPFGD AVINSLDTCI GTETCEELFT
PQSPHIAMSL DGVEIMTNSS GSHHELRKLN KRLDLILNAT KRCGGVYLYA NQRGCDGDRL
YYDGCALIAI NGTIVAQGSQ FSLDDVEVVT ATVDLEEVRS YRAAVMSRGL QASLAEIKFK
RIDIPVELAL MTSRFDPTVC PTKVREPFYH SPEEEIALGP ACWMWDYLRR CNGTGFFLPL
SGGIDSCATA MIVHSMCRLV TDAAQNGNEQ VIKDVRKITR SGDDWIPDSP QDLASKIFHS
CFMGTENSSK ETRNRAKDLS NAIGSYHVDL KMDSLVSSVV SLFEVATGKK PIYKIFGGSQ
IENLALQNIQ ARLRMVLSYL FAQLLPWVRG IPNSGGLLVL GSANVDECLR GYLTKYDCSS
ADINPIGGIS KTDLKRFIAY ASKQYNMPIL NDFLNATPTA ELEPMTKDYV QSDEIDMGMT
YEELGVFGYL RKVEKCGPYS MFLKLLHQWS PKLTPRQISE KVKRFFFFYA INRHKQTVLT
PSYHAEQYSP EDNRFDLRPF LINPRFPWAS RKIDEVVEQC EAHKGSTLDI MSID
