Quinolinate synthase A (P11458)

Identification
Name:Quinolinate synthase A
Synonyms:Not Available
Gene Name:nadA
Enzyme Class:
Biological Properties
General Function:Involved in quinolinate synthetase A activity
Specific Function:Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Nicotinate and nicotinamide metabolism ec00760
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 2.0Thumb+1.0Thumb+1.0Thumb
1.0Dihydroxyacetone phosphate + 1.0Iminoaspartic acid ↔ 2.0Water + 1.0Phosphate + 1.0Quinolinic acid
ReactionCard
1.0Thumb+2.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Quinolinic acid + 2.0Water + 1.0Phosphate ↔ 1.0Iminoaspartic acid + 1.0Dihydroxyacetone phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb+1.0Thumb
1.0Iminoaspartic acid + 1.0Dihydroxyacetone phosphate → 1.0Phosphate + 2.0Water + 1.0Quinolinic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 2.0Thumb+1.0Thumb+1.0Thumb
1.0Dihydroxyacetone phosphate + 1.0Iminoaspartic acid ↔ 2.0Water + 1.0Phosphate + 1.0Quinolinic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb+1.0Thumb
1.0Dihydroxyacetone phosphate + 1.0Iminoaspartic acid → 1.0Quinolinic acid + 2.0Water + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01473Dihydroxyacetone phosphateMetaboCard
ECMDB01131Iminoaspartic acidMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00232Quinolinic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
quinolinate synthetase A activity
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:b0750
Gene OrientationClockwise
Centisome Percentage:16.84
Left Sequence End781308
Right Sequence End782351
Gene Sequence:
>1044 bp
ATGCGTATTGAAGAAGATCTGAAGTTAGGTTTTAAAGACGTTCTCATCCGCCCTAAACGC
TCCACTCTTAAAAGCCGTTCCGATGTTGAACTGGAACGTCAATTCACCTTCAAACATTCA
GGTCAGAGCTGGTCCGGCGTGCCGATTATCGCCGCAAATATGGACACCGTAGGCACATTT
TCTATGGCCTCTGCGCTGGCTTCTTTTGATATTTTGACTGCTGTGCATAAACACTATTCT
GTCGAAGAGTGGCAAGCGTTTATCAACAATTCTTCCGCTGATGTGCTGAAACATGTGATG
GTTTCTACCGGTACGTCTGATGCGGATTTCGAAAAAACTAAACAGATTCTCGACCTGAAC
CCGGCATTAAACTTCGTTTGTATTGACGTGGCGAATGGTTATTCCGAACACTTCGTGCAG
TTCGTTGCGAAAGCGCGTGAAGCGTGGCCGACCAAAACCATTTGTGCTGGTAACGTAGTG
ACTGGTGAAATGTGTGAGGAGCTTATCCTCTCAGGTGCCGATATCGTTAAAGTTGGCATT
GGCCCAGGTTCTGTTTGTACAACTCGCGTCAAAACAGGCGTCGGTTATCCGCAACTTTCT
GCGGTAATCGAATGTGCCGATGCTGCGCACGGTCTGGGCGGAATGATCGTCAGCGATGGT
GGCTGCACCACGCCGGGCGATGTGGCGAAAGCCTTTGGCGGCGGTGCCGATTTCGTCATG
CTTGGCGGCATGCTGGCGGGCCACGAAGAGAGCGGCGGTCGCATCGTTGAGGAGAACGGC
GAGAAATTTATGCTGTTCTACGGCATGAGCTCCGAGTCTGCGATGAAACGTCACGTTGGC
GGCGTTGCGGAATATCGCGCAGCAGAAGGTAAAACCGTTAAGCTGCCGCTGCGAGGCCCG
GTTGAAAATACCGCGCGAGATATTTTGGGCGGCCTGCGTTCAGCTTGTACATACGTTGGG
GCTTCACGCCTGAAAGAGCTGACCAAGCGCACCACGTTTATTCGTGTGCAGGAACAAGAA
AACCGCATCTTCAACAACCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:347
Protein Molecular Weight:38240
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Quinolinate synthase A
MSVMFDPDTAIYPFPPKPTPLSIDEKAYYREKIKRLLKERNAVMVAHYYTDPEIQQLAEE
TGGCISDSLEMARFGAKHPASTLLVAGVRFMGETAKILSPEKTILMPTLQAECSLDLGCP
VEEFNAFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDHLDSLGEKIIWAPDKH
LGRYVQKQTGGDILCWQGACIVHDEFKTQALTRLQEEYPDAAILVHPESPQAIVDMADAV
GSTSQLIAAAKTLPHQRLIVATDRGIFYKMQQAVPDKELLEAPTAGEGATCRSCAHCPWM
AMNGLQAIAEALEQEGSNHEVHVDERLRERALVPLNRMLDFAATLRG
References
External Links:
ResourceLink
Uniprot ID:P11458
Uniprot Name:NADA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674329
Ecogene ID:EG10630
Ecocyc:EG10630
ColiBase:b0750
Kegg Gene:b0750
EchoBASE ID:EB0624
CCDB:NADA_ECOLI
BacMap:16128718
General Reference:
  • 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
  • Ceciliani, F., Caramori, T., Ronchi, S., Tedeschi, G., Mortarino, M., Galizzi, A. (2000). "Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase." Protein Expr Purif 18:64-70. Pubmed: 10648170
  • Cicchillo, R. M., Tu, L., Stromberg, J. A., Hoffart, L. M., Krebs, C., Booker, S. J. (2005). "Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster." J Am Chem Soc 127:7310-7311. Pubmed: 15898769
  • Flachmann, R., Kunz, N., Seifert, J., Gutlich, M., Wientjes, F. J., Laufer, A., Gassen, H. G. (1988). "Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB." Eur J Biochem 175:221-228. Pubmed: 2841129
  • 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
  • Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F., Fontecave, M. (2005). "Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis." FEBS Lett 579:3737-3743. Pubmed: 15967443
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Saunders, A. H., Booker, S. J. (2008). "Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation." Biochemistry 47:8467-8469. Pubmed: 18651751