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Protein

Nicotinate-nucleotide pyrophosphorylase [carboxylating]

Gene

BNA6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the catabolism of quinolinic acid (QA).By similarity

Catalytic activityi

Beta-nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes nicotinate D-ribonucleotide from quinolinate.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinate-nucleotide pyrophosphorylase [carboxylating] (BNA6)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes nicotinate D-ribonucleotide from quinolinate, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071Substrate1 Publication
Binding sitei166 – 1661Substrate1 Publication
Binding sitei176 – 1761Substrate1 Publication
Binding sitei206 – 2061SubstrateBy similarity
Binding sitei227 – 2271Substrate1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: SGD

GO - Biological processi

  • 'de novo' NAD biosynthetic process from tryptophan Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8162.
YEAST:YFR047C-MONOMER.
BRENDAi2.4.2.19. 984.
ReactomeiR-SCE-196807. Nicotinate metabolism.
UniPathwayiUPA00253; UER00331.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC:2.4.2.19)
Alternative name(s):
Quinolinate phosphoribosyltransferase [decarboxylating]
Short name:
QAPRTase
Gene namesi
Name:BNA6
Synonyms:QPT1
Ordered Locus Names:YFR047C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFR047C.
SGDiS000001943. BNA6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Nicotinate-nucleotide pyrophosphorylase [carboxylating]PRO_0000155956Add
BLAST

Proteomic databases

MaxQBiP43619.
TopDownProteomicsiP43619.

PTM databases

iPTMnetiP43619.

Interactioni

Subunit structurei

Hexamer formed by 3 homodimers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-11793,EBI-11793

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31205. 22 interactions.
DIPiDIP-1569N.
IntActiP43619. 3 interactions.
MINTiMINT-394142.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Beta strandi10 – 123Combined sources
Helixi13 – 2513Combined sources
Helixi31 – 366Combined sources
Beta strandi40 – 478Combined sources
Beta strandi49 – 524Combined sources
Helixi56 – 6510Combined sources
Beta strandi69 – 746Combined sources
Helixi82 – 843Combined sources
Beta strandi85 – 884Combined sources
Beta strandi90 – 989Combined sources
Helixi99 – 13234Combined sources
Beta strandi137 – 1404Combined sources
Turni147 – 1493Combined sources
Helixi150 – 15910Combined sources
Turni169 – 1713Combined sources
Beta strandi172 – 1754Combined sources
Helixi177 – 1837Combined sources
Helixi186 – 19712Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi203 – 2064Combined sources
Beta strandi208 – 2103Combined sources
Helixi211 – 2199Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi273 – 2764Combined sources
Helixi278 – 2803Combined sources
Turni281 – 2833Combined sources
Beta strandi289 – 2935Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C2EX-ray1.90A2-295[»]
3C2FX-ray2.35A2-295[»]
3C2OX-ray2.30A2-295[»]
3C2RX-ray2.40A/B1-295[»]
3C2VX-ray2.29A2-295[»]
ProteinModelPortaliP43619.
SMRiP43619. Positions 2-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43619.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 1443Substrate binding
Regioni256 – 2583Substrate binding

Sequence similaritiesi

Belongs to the NadC/ModD family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000002761.
HOGENOMiHOG000224023.
InParanoidiP43619.
KOiK00767.
OMAiFEPVKHV.
OrthoDBiEOG7QNVX0.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.90.1170.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004393. NadC.
IPR027277. NadC/ModD.
IPR002638. Quinolinate_PRibosylTrfase_C.
IPR022412. Quinolinate_PRibosylTrfase_N.
[Graphical view]
PfamiPF01729. QRPTase_C. 1 hit.
PF02749. QRPTase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF006250. NadC_ModD. 1 hit.
SUPFAMiSSF51690. SSF51690. 1 hit.
TIGRFAMsiTIGR00078. nadC. 1 hit.

Sequencei

Sequence statusi: Complete.

P43619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVYEHLLPV NGAWRQDVTN WLSEDVPSFD FGGYVVGSDL KEANLYCKQD
60 70 80 90 100
GMLCGVPFAQ EVFNQCELQV EWLFKEGSFL EPSKNDSGKI VVAKITGPAK
110 120 130 140 150
NILLAERTAL NILSRSSGIA TASHKIISLA RSTGYKGTIA GTRKTTPGLR
160 170 180 190 200
RLEKYSMLVG GCDTHRYDLS SMVMLKDNHI WATGSITNAV KNARAVCGFA
210 220 230 240 250
VKIEVECLSE DEATEAIEAG ADVIMLDNFK GDGLKMCAQS LKNKWNGKKH
260 270 280 290
FLLECSGGLN LDNLEEYLCD DIDIYSTSSI HQGTPVIDFS LKLAH
Length:295
Mass (Da):32,365
Last modified:November 1, 1995 - v1
Checksum:i0680BB5DDC095050
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09286.1.
BK006940 Genomic DNA. Translation: DAA12490.1.
PIRiS56302.
RefSeqiNP_602317.3. NM_001180012.3.

Genome annotation databases

EnsemblFungiiBAA09286; BAA09286; BAA09286.
YFR047C; YFR047C; YFR047C.
GeneIDi850608.
KEGGisce:YFR047C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50617 Genomic DNA. Translation: BAA09286.1.
BK006940 Genomic DNA. Translation: DAA12490.1.
PIRiS56302.
RefSeqiNP_602317.3. NM_001180012.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C2EX-ray1.90A2-295[»]
3C2FX-ray2.35A2-295[»]
3C2OX-ray2.30A2-295[»]
3C2RX-ray2.40A/B1-295[»]
3C2VX-ray2.29A2-295[»]
ProteinModelPortaliP43619.
SMRiP43619. Positions 2-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31205. 22 interactions.
DIPiDIP-1569N.
IntActiP43619. 3 interactions.
MINTiMINT-394142.

PTM databases

iPTMnetiP43619.

Proteomic databases

MaxQBiP43619.
TopDownProteomicsiP43619.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09286; BAA09286; BAA09286.
YFR047C; YFR047C; YFR047C.
GeneIDi850608.
KEGGisce:YFR047C.

Organism-specific databases

EuPathDBiFungiDB:YFR047C.
SGDiS000001943. BNA6.

Phylogenomic databases

GeneTreeiENSGT00390000002761.
HOGENOMiHOG000224023.
InParanoidiP43619.
KOiK00767.
OMAiFEPVKHV.
OrthoDBiEOG7QNVX0.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00331.
BioCyciMetaCyc:MONOMER-8162.
YEAST:YFR047C-MONOMER.
BRENDAi2.4.2.19. 984.
ReactomeiR-SCE-196807. Nicotinate metabolism.

Miscellaneous databases

EvolutionaryTraceiP43619.
NextBioi966490.
PROiP43619.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.90.1170.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004393. NadC.
IPR027277. NadC/ModD.
IPR002638. Quinolinate_PRibosylTrfase_C.
IPR022412. Quinolinate_PRibosylTrfase_N.
[Graphical view]
PfamiPF01729. QRPTase_C. 1 hit.
PF02749. QRPTase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF006250. NadC_ModD. 1 hit.
SUPFAMiSSF51690. SSF51690. 1 hit.
TIGRFAMsiTIGR00078. nadC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
    Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
    Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae."
    Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M., Rytka J., Herbert C.J.
    FEBS Lett. 517:97-102(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, PATHWAY.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Comprehensive X-ray structural studies of the quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae."
    di Luccio E., Wilson D.K.
    Biochemistry 47:4039-4050(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-295 IN COMPLEX WITH SUBSTRATE, SUBUNIT.

Entry informationi

Entry nameiNADC_YEAST
AccessioniPrimary (citable) accession number: P43619
Secondary accession number(s): D6VTT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2660 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.