Identification
Name:Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Synonyms:
  • Quinolinate phosphoribosyltransferase [decarboxylating]
  • QAPRTase
Gene Name:nadC
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Involved in the catabolism of quinolinic acid (QA)
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
2.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Pyrophosphate+1.0nicotinate beta-D-ribonucleotide+1.0Thumb
1.0Quinolinic acid + 1.0Hydrogen ion + 1.0Phosphoribosyl pyrophosphate → 1.0Carbon dioxide + 1.0Pyrophosphate + 1.0nicotinate beta-D-ribonucleotide + 1.0Nicotinamide ribotide
ReactionCard
EcoCyc Reactions:
2.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00229Nicotinamide ribotideMetaboCard
ECMDB00280Phosphoribosyl pyrophosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00232Quinolinic acidMetaboCard
GO Classification:
Function
catalytic activity
nicotinate-nucleotide diphosphorylase (carboxylating) activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
Process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
NAD biosynthetic process
nicotinamide nucleotide biosynthetic process
pyridine nucleotide biosynthetic process
Gene Properties
Blattner:b0109
Gene OrientationCounterclockwise
Centisome Percentage:2.54
Left Sequence End117752
Right Sequence End118645
Gene Sequence:
>894 bp
ATGCCGCCTCGCCGCTATAACCCTGACACCCGACGTGACGAGCTGCTGGAACGCATTAAT
CTCGATATCCCCGGCGCGGTGGCCCAGGCGCTGCGGGAAGATTTAGGCGGAACAGTCGAT
GCCAACAATGATATTACGGCAAAACTTTTACCGGAAAATTCTCGCTCTCATGCCACGGTG
ATCACCCGCGAGAATGGCGTCTTTTGCGGCAAACGCTGGGTTGAAGAGGTGTTTATTCAA
CTGGCAGGCGACGATGTCACCATAATCTGGCATGTGGATGACGGCGATGTCATCAATGCC
AATCAATCCTTGTTCGAACTTGAAGGCCCATCCCGCGTGCTGTTAACGGGCGAACGCACT
GCGCTTAATTTTGTGCAAACCCTTTCAGGAGTTGCCAGTAAGGTACGCCACTATGTCGAA
TTGCTGGAAGGCACCAACACGCAGTTGTTGGATACGCGCAAAACCTTACCCGGCCTGCGT
TCAGCTCTGAAATACGCGGTACTTTGCGGCGGCGGAGCGAATCACCGTCTGGGGCTTTCT
GATGCCTTCCTGATCAAAGAAAACCATATTATTGCCTCCGGCTCAGTGCGCCAGGCGGTC
GAAAAAGCGTCCTGGCTGCACCCGGATGCGCCAGTAGAAGTCGAAGTAGAGAATCTGGAA
GAACTTGATGAAGCCCTGAAAGCAGGAGCCGATATCATCATGCTGGATAACTTCGAAACA
GAACAGATGCGCGAAGCCGTCAAACGCACCAACGGCAAGGCGCTACTGGAAGTGTCTGGC
AACGTCACTGACAAAACACTGCGTGAATTTGCCGAAACGGGCGTGGACTTTATCTCCGTC
GGTGCGCTAACTAAACACGTACAAGCACTCGACCTTTCAATGCGTTTTCGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:297
Protein Molecular Weight:32762
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Nicotinate-nucleotide pyrophosphorylase [carboxylating]
MPPRRYNPDTRRDELLERINLDIPGAVAQALREDLGGTVDANNDITAKLLPENSRSHATV
ITRENGVFCGKRWVEEVFIQLAGDDVTIIWHVDDGDVINANQSLFELEGPSRVLLTGERT
ALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLS
DAFLIKENHIIASGSVRQAVEKASWLHPDAPVEVEVENLEELDEALKAGADIIMLDNFET
EQMREAVKRTNGKALLEVSGNVTDKTLREFAETGVDFISVGALTKHVQALDLSMRFR
References
External Links:
ResourceLink
Uniprot ID:P30011
Uniprot Name:NADC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674333
Ecogene ID:EG11546
Ecocyc:EG11546
ColiBase:b0109
Kegg Gene:b0109
EchoBASE ID:EB1508
CCDB:NADC_ECOLI
BacMap:16128102
General Reference:
  • Bhatia, R., Calvo, K. C. (1996). "The sequencing expression, purification, and steady-state kinetic analysis of quinolinate phosphoribosyl transferase from Escherichia coli." Arch Biochem Biophys 325:270-278. Pubmed: 8561507
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Honore, N., Nicolas, M. H., Cole, S. T. (1989). "Regulation of enterobacterial cephalosporinase production: the role of a membrane-bound sensory transducer." Mol Microbiol 3:1121-1130. Pubmed: 2607970
  • Hughes, K. T., Dessen, A., Gray, J. P., Grubmeyer, C. (1993). "The Salmonella typhimurium nadC gene: sequence determination by use of Mud-P22 and purification of quinolinate phosphoribosyltransferase." J Bacteriol 175:479-486. Pubmed: 8419294
  • Lindquist, S., Galleni, M., Lindberg, F., Normark, S. (1989). "Signalling proteins in enterobacterial AmpC beta-lactamase regulation." Mol Microbiol 3:1091-1102. Pubmed: 2691840
  • Whitchurch, C. B., Mattick, J. S. (1994). "Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria." Gene 150:9-15. Pubmed: 7959070