Para-hydroxybenzoate--polyprenyltransferase, mitochondrial (P32378)

Identification
NamePara-hydroxybenzoate--polyprenyltransferase, mitochondrial
Synonyms
  • PHB:polyprenyltransferase
Gene NameCOQ2
Enzyme Class
Biological Properties
General FunctionInvolved in prenyltransferase activity
Specific FunctionCatalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB
Cellular LocationMitochondrion inner membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
hexaprenyl diphosphate + 4-Hydroxybenzoic acid → Pyrophosphate + 3-Hexaprenyl-4-hydroxybenzoic acid
Metabolites
YMDB IDNameView
YMDB00219PyrophosphateShow
YMDB004593-Hexaprenyl-4-hydroxybenzoic acidShow
YMDB004954-Hydroxybenzoic acidShow
YMDB00615nonaprenyl 4-hydroxybenzoateShow
YMDB00633hexaprenyl diphosphateShow
YMDB00636decaprenyl diphosphateShow
YMDB00832all-trans-nonaprenyl diphosphateShow
GO Classification
Component
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
transferase activity, transferring alkyl or aryl (other than methyl) groups
prenyltransferase activity
catalytic activity
transferase activity
Process
biosynthetic process
metabolic process
Gene Properties
Chromosome Locationchromosome 14
LocusYNR041C
Gene Sequence>1119 bp ATGTTTATTTGGCAGAGAAAGAGTATTTTACTAGGGAGGTCCATTCTGGGCAGCGGCCGA GTTACCGTTGCTGGAATCATTGGAAGCAGCAGAAAGAGATATACGTCTTCTTCCTCCTCC TCCTCCTCCCCTTCCTCGAAAGAATCAGCACCTGTGTTTACGTCGAAAGAGTTGGAAGTT GCAAGAAAGGAAAGATTGGATGGACTGGGACCGTTCGTGTCTCGGCTGCCTAAGAAATGG ATACCGTATGCGGAGCTGATGAGGCTAGAGAAACCCGTGGGCACGTGGCTGTTATATTTG CCCTGCAGTTGGTCTATACTTATGGGAGCCATGATGCAAGGTGCTACATTGAGCGCAACA GCTGGTATGTTGGGTATTTTCGGTGTAGGTGCATTGGTAATGAGAGGTGCTGGCTGCACC ATCAACGATTTTTTGGATAGAAAGTTGGATCAAAGAGTTATCAGGTCCGTCGAGAGGCCT ATCGCCTCTGGTAGAGTGAGCCCCCGTCGGGCGTTAGTATTCTTGGGGGCTCAAACTCTT GTTGGAATGGGCGTTCTATCTTTGCTTCCTGCGCAGTGTTGGTGGCTAGGCCTTGCATCG TTACCTATTGTGTTCACATACCCTTTGTTTAAGCGGTTTACGTACTATCCTCAAGCTGCA TTAAGTGCATGTTTCAATTGGGGAGCGTTACTTGGGTTTCCTGCCATGGGTGTAATGAGC TGGCCTACAATGATACCTTTGTACCTGAGCAGTTACTTGTGGTGTATGACTTACGATACT ATATACGCACACCAGGATAAAAAGTTTGACATCAAGACTGGAATCAAGTCTACCGCTTTG GCTTGGGGTCCACGCACAAAGTCTATCATGAAGGCCATGTCCGCGTCTCAAATCGCACTG TTAGCTGTCGCCGGCTTGAACAGTGGGTTGTTATGGGGGCCTGGGTTCATTGGTGGACTA GGAGTCTTCGCTTATAGACTCTTCAGCATGATAAAGAAAGTGGATCTTGACAATCCTAAA AACTGCTGGAAGTATTTTAATGCAAATATCAACACCGGACTTTACTTTACGTACGCCTTG GCAGTCGACTACATCTTGAGACTGTTTGGATTCTTGTAG
Protein Properties
Pfam Domain Function
Protein Residues372
Protein Molecular Weight41001.0
Protein Theoretical pI10.47
Signalling Regions
  • None
Transmembrane Regions
  • 92-112
  • 114-133
  • 170-191
  • 193-210
  • 229-249
  • 298-318
Protein Sequence>Para-hydroxybenzoate--polyprenyltransferase, mitochondrial MFIWQRKSILLGRSILGSGRVTVAGIIGSSRKRYTSSSSSSSSPSSKESAPVFTSKELEV ARKERLDGLGPFVSRLPKKWIPYAELMRLEKPVGTWLLYLPCSWSILMGAMMQGATLSAT AGMLGIFGVGALVMRGAGCTINDFLDRKLDQRVIRSVERPIASGRVSPRRALVFLGAQTL VGMGVLSLLPAQCWWLGLASLPIVFTYPLFKRFTYYPQAALSACFNWGALLGFPAMGVMS WPTMIPLYLSSYLWCMTYDTIYAHQDKKFDIKAGIKSTALAWGPRTKSIMKAMSASQIAL LAVAGLNSGLLWGPGFIGGLGVFAYRLFSMIKKVDLDNPKNCWKYFNANINTGLYFTYAL AVDYILRLFGFL
References
External Links
ResourceLink
Saccharomyces Genome Database COQ2
Uniprot IDP32378
Uniprot NameCOQ2_YEAST
GenBank Gene IDAY693097
Genebank Protein ID51013645
General Reference
  • Ashby, M. N., Kutsunai, S. Y., Ackerman, S., Tzagoloff, A., Edwards, P. A. (1992). "COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase." J Biol Chem 267:4128-4136.1740455
  • Philippsen, P., Kleine, K., Pohlmann, R., Dusterhoft, A., Hamberg, K., Hegemann, J. H., Obermaier, B., Urrestarazu, L. A., Aert, R., Albermann, K., Altmann, R., Andre, B., Baladron, V., Ballesta, J. P., Becam, A. M., Beinhauer, J., Boskovic, J., Buitrago, M. J., Bussereau, F., Coster, F., Crouzet, M., D'Angelo, M., Dal Pero, F., De Antoni, A., Del Rey, F., Doignon, F., Domdey, H., Dubois, E., Fiedler, T., Fleig, U., Floeth, M., Fritz, C., Gaillardin, C., Garcia-Cantalejo, J. M., Glansdorff, N. N., Goffeau, A., Gueldener, U., Herbert, C., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hinni, K., Iraqui Houssaini, I., Jacquet, M., Jimenez, A., Jonniaux, J. L., Karpfinger, L., Lanfranchi, G., Lepingle, A., Levesque, H., Lyck, R., Maftahi, M., Mallet, L., Maurer, K. C., Messenguy, F., Mewes, H. W., Mosti, D., Nasr, F., Nicaud, J. M., Niedenthal, R. K., Pandolfo, D., Pierard, A., Piravandi, E., Planta, R. J., Pohl, T. M., Purnelle, B., Rebischung, C., Remacha, M., Revuelta, J. L., Rinke, M., Saiz, J. E., Sartorello, F., Scherens, B., Sen-Gupta, M., Soler-Mira, A., Urbanus, J. H., Valle, G., Van Dyck, L., Verhasselt, P., Vierendeels, F., Vissers, S., Voet, M., Volckaert, G., Wach, A., Wambutt, R., Wedler, H., Zollner, A., Hani, J. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Nature 387:93-98.9169873
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956