Phosphopantetheine adenylyltransferase (P0A6I6)

Identification
Name:Phosphopantetheine adenylyltransferase
Synonyms:
  • Dephospho-CoA pyrophosphorylase
  • Pantetheine-phosphate adenylyltransferase
  • PPAT
Gene Name:coaD
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0Pantetheine 4'-phosphate ↔ 1.0Dephospho-CoA + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pantetheine 4'-phosphate ↔ 1.0Pyrophosphate + 1.0Dephospho-CoA
ReactionCard
SMPDB Reactions:
1.04'-phosphopantetheine+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Pyrophosphate+1.0Thumb
1.04'-phosphopantetheine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.04'-phosphopantetheine → 1.0Pyrophosphate + 1.0Dephospho-CoA
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0Pantetheine 4'-phosphate ↔ 1.0Dephospho-CoA + 1.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0pantotheine 4'-phosphate → 1.0Pyrophosphate + 1.03'-dephospho-CoA
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB231693'-dephospho-CoAMetaboCard
ECMDB242134'-phosphopantetheineMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01373Dephospho-CoAMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01416Pantetheine 4'-phosphateMetaboCard
ECMDB23216pantotheine 4'-phosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
adenylyltransferase activity
catalytic activity
nucleotidyltransferase activity
pantetheine-phosphate adenylyltransferase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
biosynthetic process
cellular metabolic process
coenzyme A biosynthetic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
Gene Properties
Blattner:b3634
Gene OrientationClockwise
Centisome Percentage:82.07
Left Sequence End3807848
Right Sequence End3808327
Gene Sequence:
>480 bp
ATGATCAGTCTGATTGCGGCGTTAGCGGTAGATCGCGTTATCGGCATGGAAAACGCCATG
CCGTGGAACCTGCCTGCCGATCTCGCCTGGTTTAAACGCAACACCTTAAATAAACCCGTG
ATTATGGGCCGCCATACCTGGGAATCAATCGGTCGTCCGTTGCCAGGACGCAAAAATATT
ATCCTCAGCAGTCAACCGGGTACGGACGATCGCGTAACGTGGGTGAAGTCGGTGGATGAA
GCCATCGCGGCGTGTGGTGACGTACCAGAAATCATGGTGATTGGCGGCGGTCGCGTTTAT
GAACAGTTCTTGCCAAAAGCGCAAAAACTGTATCTGACGCATATCGACGCAGAAGTGGAA
GGCGACACCCATTTCCCGGATTACGAGCCGGATGACTGGGAATCGGTATTCAGCGAATTC
CACGATGCTGATGCGCAGAACTCTCACAGCTATTGCTTTGAGATTCTGGAGCGGCGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:159
Protein Molecular Weight:17837
Protein Theoretical pI:7
PDB File:1GN8
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphopantetheine adenylyltransferase
MQKRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERVALAQQATA
HLGNVEVVGFSDLMANFARNQHATVLIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMP
SKEWSFISSSLVKEVARHQGDVTHFLPENVHQALMAKLA
References
External Links:
ResourceLink
Uniprot ID:P0A6I6
Uniprot Name:COAD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321929
PDB ID:1GN8
Ecogene ID:EG11190
Ecocyc:EG11190
ColiBase:b3634
Kegg Gene:b3634
EchoBASE ID:EB1176
CCDB:COAD_ECOLI
BacMap:16131505
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
  • Clementz, T., Raetz, C. R. (1991). "A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing." J Biol Chem 266:9687-9696. Pubmed: 2033061
  • Geerlof, A., Lewendon, A., Shaw, W. V. (1999). "Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli." J Biol Chem 274:27105-27111. Pubmed: 10480925
  • 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
  • Izard, T. (2002). "The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism." J Mol Biol 315:487-495. Pubmed: 11812124
  • Izard, T., Geerlof, A. (1999). "The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity." EMBO J 18:2021-2030. Pubmed: 10205156
  • Roncero, C., Casadaban, M. J. (1992). "Genetic analysis of the genes involved in synthesis of the lipopolysaccharide core in Escherichia coli K-12: three operons in the rfa locus." J Bacteriol 174:3250-3260. Pubmed: 1577693
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620