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Protein

Nicotinate-nucleotide pyrophosphorylase [carboxylating]

Gene

nadC

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Pathway:iNAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes nicotinate D-ribonucleotide from quinolinate.
Proteins known to be involved in this subpathway in this organism are:
  1. Nicotinate-nucleotide pyrophosphorylase [carboxylating] (nadC)
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 sitei105 – 1051Substrate1 Publication
Binding sitei162 – 1621Substrate1 Publication
Binding sitei172 – 1721Substrate1 Publication
Binding sitei201 – 2011Substrate1 Publication
Binding sitei222 – 2221Substrate1 Publication

GO - Molecular functioni

  • nicotinate-nucleotide diphosphorylase (carboxylating) activity Source: MTBBASE

GO - Biological processi

  • NAD biosynthetic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Enzyme and pathway databases

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:nadC
Ordered Locus Names:Rv1596
ORF Names:MTCY336.08c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1596.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Nicotinate-nucleotide pyrophosphorylase [carboxylating]PRO_0000155946Add
BLAST

Interactioni

Subunit structurei

Homodimer. Hexamer formed by 3 homodimers.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv1596.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2319Combined sources
Helixi29 – 346Combined sources
Beta strandi40 – 4910Combined sources
Helixi56 – 6712Combined sources
Beta strandi71 – 777Combined sources
Beta strandi89 – 968Combined sources
Helixi97 – 12731Combined sources
Turni128 – 1303Combined sources
Beta strandi134 – 1363Combined sources
Turni143 – 1453Combined sources
Helixi146 – 15510Combined sources
Beta strandi164 – 1718Combined sources
Helixi173 – 1797Combined sources
Helixi182 – 19211Combined sources
Beta strandi198 – 2047Combined sources
Helixi205 – 2117Combined sources
Helixi212 – 2143Combined sources
Beta strandi217 – 2237Combined sources
Helixi226 – 23914Combined sources
Beta strandi244 – 2507Combined sources
Turni253 – 2553Combined sources
Helixi256 – 2616Combined sources
Beta strandi265 – 2684Combined sources
Helixi270 – 2723Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi281 – 2844Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QPNX-ray2.60A/B/C/D/E/F2-285[»]
1QPOX-ray2.40A/B/C/D/E/F2-285[»]
1QPQX-ray2.45A/B/C/D/E/F2-285[»]
1QPRX-ray2.45A/B/C/D/E/F2-285[»]
ProteinModelPortaliP9WJJ7.
SMRiP9WJJ7. Positions 2-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 1403Substrate binding
Regioni248 – 2503Substrate binding
Regioni269 – 2713Substrate binding

Sequence similaritiesi

Belongs to the NadC/ModD family.Curated

Phylogenomic databases

KOiK00767.
OMAiCGGCHNH.
PhylomeDBiP9WJJ7.

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.

P9WJJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLSDWELAA ARAAIARGLD EDLRYGPDVT TLATVPASAT TTASLVTREA
60 70 80 90 100
GVVAGLDVAL LTLNEVLGTN GYRVLDRVED GARVPPGEAL MTLEAQTRGL
110 120 130 140 150
LTAERTMLNL VGHLSGIATA TAAWVDAVRG TKAKIRDTRK TLPGLRALQK
160 170 180 190 200
YAVRTGGGVN HRLGLGDAAL IKDNHVAAAG SVVDALRAVR NAAPDLPCEV
210 220 230 240 250
EVDSLEQLDA VLPEKPELIL LDNFAVWQTQ TAVQRRDSRA PTVMLESSGG
260 270 280
LSLQTAATYA ETGVDYLAVG ALTHSVRVLD IGLDM
Length:285
Mass (Da):29,951
Last modified:April 16, 2014 - v1
Checksum:i45DE3335EC1C522F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44360.1.
PIRiF70543.
RefSeqiNP_216112.1. NC_000962.3.
WP_003898939.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44360; CCP44360; Rv1596.
GeneIDi886281.
KEGGimtu:Rv1596.
mtv:RVBD_1596.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44360.1.
PIRiF70543.
RefSeqiNP_216112.1. NC_000962.3.
WP_003898939.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QPNX-ray2.60A/B/C/D/E/F2-285[»]
1QPOX-ray2.40A/B/C/D/E/F2-285[»]
1QPQX-ray2.45A/B/C/D/E/F2-285[»]
1QPRX-ray2.45A/B/C/D/E/F2-285[»]
ProteinModelPortaliP9WJJ7.
SMRiP9WJJ7. Positions 2-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1596.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44360; CCP44360; Rv1596.
GeneIDi886281.
KEGGimtu:Rv1596.
mtv:RVBD_1596.

Organism-specific databases

TubercuListiRv1596.

Phylogenomic databases

KOiK00767.
OMAiCGGCHNH.
PhylomeDBiP9WJJ7.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00331.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  3. "Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential tb drug target."
    Sharma V., Grubmeyer C., Sacchettini J.C.
    Structure 6:1587-1599(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiNADC_MYCTU
AccessioniPrimary (citable) accession number: P9WJJ7
Secondary accession number(s): L0T8R5, O06594
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: July 22, 2015
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.