Nicotinate-nucleotide pyrophosphorylase [carboxylating]

Details

Name
Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Synonyms
  • 2.4.2.19
  • QAPRTase
  • Quinolinate phosphoribosyltransferase [decarboxylating]
Gene Name
nadC
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051199|Nicotinate-nucleotide pyrophosphorylase [carboxylating]
MGLSDWELAAARAAIARGLDEDLRYGPDVTTLATVPASATTTASLVTREAGVVAGLDVAL
LTLNEVLGTNGYRVLDRVEDGARVPPGEALMTLEAQTRGLLTAERTMLNLVGHLSGIATA
TAAWVDAVRGTKAKIRDTRKTLPGLRALQKYAVRTGGGVNHRLGLGDAALIKDNHVAAAG
SVVDALRAVRNAAPDLPCEVEVDSLEQLDAVLPEKPELILLDNFAVWQTQTAVQRRDSRA
PTVMLESSGGLSLQTAATYAETGVDYLAVGALTHSVRVLDIGLDM
Number of residues
285
Molecular Weight
29950.79
Theoretical pI
Not Available
GO Classification
Functions
nicotinate-nucleotide diphosphorylase (carboxylating) activity
Processes
NAD biosynthetic process / quinolinate catabolic process
Components
cell wall / cytoplasm / plasma membrane
General Function
Involved in the catabolism of quinolinic acid (QA).
Specific Function
Nicotinate-nucleotide diphosphorylase (carboxylating) activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051200|Nicotinate-nucleotide pyrophosphorylase [carboxylating] (nadC)
ATGGGGTTATCCGACTGGGAGCTGGCTGCGGCTCGAGCAGCAATCGCGCGTGGGCTCGAC
GAGGACCTCCGGTACGGCCCGGATGTCACCACATTGGCGACGGTGCCTGCCAGTGCGACG
ACCACCGCATCGCTGGTGACCCGGGAGGCCGGTGTGGTTGCCGGATTGGATGTCGCGCTG
CTGACGCTGAACGAAGTCCTGGGCACCAACGGTTATCGGGTGCTCGACCGCGTCGAGGAC
GGCGCCCGGGTGCCGCCGGGAGAGGCACTTATGACGCTGGAAGCCCAAACGCGCGGATTG
TTGACCGCCGAGCGCACCATGTTGAACCTGGTCGGTCACCTGTCGGGAATCGCCACCGCG
ACGGCCGCGTGGGTCGATGCTGTGCGCGGGACCAAAGCGAAAATCCGCGATACCCGTAAG
ACGCTGCCCGGCCTGCGCGCGCTGCAAAAATACGCGGTGCGTACCGGTGGCGGCGTCAAC
CATCGGCTGGGGTTGGGTGATGCCGCGCTAATCAAGGACAACCACGTTGCCGCCGCCGGA
TCCGTGGTAGACGCGCTACGTGCGGTGCGAAATGCTGCACCCGATCTGCCGTGCGAGGTG
GAAGTGGACTCGCTTGAGCAGCTCGATGCCGTGCTGCCGGAAAAACCCGAGCTGATCCTG
CTGGACAATTTTGCGGTGTGGCAGACGCAGACCGCGGTGCAGCGTCGGGACTCGCGCGCG
CCCACCGTCATGCTGGAGTCATCCGGTGGGCTCAGCCTGCAGACGGCGGCGACCTACGCC
GAAACCGGGGTGGACTACCTGGCGGTCGGGGCGCTCACACACTCAGTGCGCGTGCTCGAC
ATCGGCTTGGATATGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WJJ7
UniProtKB Entry NameNADC_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  3. Sharma V, Grubmeyer C, Sacchettini JC: Crystal structure of quinolinic acid phosphoribosyltransferase from Mmycobacterium tuberculosis: a potential TB drug target. Structure. 1998 Dec 15;6(12):1587-99. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01796Quinolinic AcidexperimentalunknownDetails
DB02382NamnexperimentalunknownDetails
DB02746Phthalic AcidexperimentalunknownDetails
DB042945-Phosphoribosyl-1-(Beta-Methylene) PyrophosphateexperimentalunknownDetails