NADC_YEAST
ID NADC_YEAST Reviewed; 295 AA.
AC P43619; D6VTT0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19;
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE Short=QAPRTase;
GN Name=BNA6; Synonyms=QPT1; OrderedLocusNames=YFR047C;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686379;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<149::aid-yea893>3.0.co;2-g;
RA Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.;
RT "Analysis of a 36.2 kb DNA sequence including the right telomere of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:149-167(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [3]
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 [4]
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=12062417; DOI=10.1016/s0014-5793(02)02585-1;
RA Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M.,
RA Rytka J., Herbert C.J.;
RT "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae.";
RL FEBS Lett. 517:97-102(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-295 IN COMPLEX WITH SUBSTRATE,
RP AND SUBUNIT.
RX PubMed=18321072; DOI=10.1021/bi7020475;
RA di Luccio E., Wilson D.K.;
RT "Comprehensive X-ray structural studies of the quinolinate phosphoribosyl
RT transferase (BNA6) from Saccharomyces cerevisiae.";
RL Biochemistry 47:4039-4050(2008).
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-
CC phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate;
CC Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58017; EC=2.4.2.19;
CC Evidence={ECO:0000269|PubMed:12062417};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000269|PubMed:12062417}.
CC -!- SUBUNIT: Hexamer formed by 3 homodimers. {ECO:0000269|PubMed:18321072}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; D50617; BAA09286.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12490.1; -; Genomic_DNA.
DR PIR; S56302; S56302.
DR RefSeq; NP_602317.3; NM_001180012.3.
DR PDB; 3C2E; X-ray; 1.90 A; A=2-295.
DR PDB; 3C2F; X-ray; 2.35 A; A=2-295.
DR PDB; 3C2O; X-ray; 2.30 A; A=2-295.
DR PDB; 3C2R; X-ray; 2.40 A; A/B=1-295.
DR PDB; 3C2V; X-ray; 2.29 A; A=2-295.
DR PDBsum; 3C2E; -.
DR PDBsum; 3C2F; -.
DR PDBsum; 3C2O; -.
DR PDBsum; 3C2R; -.
DR PDBsum; 3C2V; -.
DR AlphaFoldDB; P43619; -.
DR SMR; P43619; -.
DR BioGRID; 31205; 45.
DR DIP; DIP-1569N; -.
DR IntAct; P43619; 3.
DR MINT; P43619; -.
DR STRING; 4932.YFR047C; -.
DR iPTMnet; P43619; -.
DR MaxQB; P43619; -.
DR PaxDb; P43619; -.
DR PRIDE; P43619; -.
DR TopDownProteomics; P43619; -.
DR EnsemblFungi; YFR047C_mRNA; YFR047C; YFR047C.
DR GeneID; 850608; -.
DR KEGG; sce:YFR047C; -.
DR SGD; S000001943; BNA6.
DR VEuPathDB; FungiDB:YFR047C; -.
DR eggNOG; KOG3008; Eukaryota.
DR GeneTree; ENSGT00390000002761; -.
DR HOGENOM; CLU_039622_1_0_1; -.
DR InParanoid; P43619; -.
DR OMA; DMIMLKD; -.
DR BioCyc; MetaCyc:YFR047C-MON; -.
DR BioCyc; YEAST:YFR047C-MON; -.
DR BRENDA; 2.4.2.19; 984.
DR Reactome; R-SCE-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00331.
DR EvolutionaryTrace; P43619; -.
DR PRO; PR:P43619; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43619; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IMP:SGD.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IGI:SGD.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
DR CDD; cd01572; QPRTase; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.90.1170.20; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004393; NadC.
DR InterPro; IPR027277; NadC/ModD.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR PANTHER; PTHR32179; PTHR32179; 1.
DR Pfam; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR PIRSF; PIRSF006250; NadC_ModD; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR00078; nadC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosyltransferase; Nucleus;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..295
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000155956"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18321072"
FT BINDING 142..144
FT /ligand="substrate"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18321072"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18321072"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18321072"
FT BINDING 256..258
FT /ligand="substrate"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 99..132
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3C2E"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:3C2V"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:3C2E"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3C2O"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:3C2E"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3C2E"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3C2E"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:3C2V"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:3C2E"
SQ SEQUENCE 295 AA; 32365 MW; 0680BB5DDC095050 CRC64;
MPVYEHLLPV NGAWRQDVTN WLSEDVPSFD FGGYVVGSDL KEANLYCKQD GMLCGVPFAQ
EVFNQCELQV EWLFKEGSFL EPSKNDSGKI VVAKITGPAK NILLAERTAL NILSRSSGIA
TASHKIISLA RSTGYKGTIA GTRKTTPGLR RLEKYSMLVG GCDTHRYDLS SMVMLKDNHI
WATGSITNAV KNARAVCGFA VKIEVECLSE DEATEAIEAG ADVIMLDNFK GDGLKMCAQS
LKNKWNGKKH FLLECSGGLN LDNLEEYLCD DIDIYSTSSI HQGTPVIDFS LKLAH
