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Identification
HMDB Protein ID HMDBP03700
Secondary Accession Numbers
  • 9288
Name 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Synonyms
  1. COQ2 homolog
  2. PHB:polyprenyltransferase
  3. hCOQ2
  4. Para-hydroxybenzoate--polyprenyltransferase
Gene Name COQ2
Protein Type Enzyme
Biological Properties
General Function Involved in prenyltransferase activity
Specific Function Catalyzes 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.
Pathways
  • Ubiquinone and other terpenoid-quinone biosynthesis
  • ubiquinone biosynthesis
  • Ubiquinone Biosynthesis
Reactions
A polyprenyl diphosphate + 4-Hydroxybenzoic acid → Pyrophosphate + a 4-hydroxy-3-polyprenylbenzoate details
Geranyl-PP + 4-Hydroxybenzoic acid → 4-Hydroxy-3-polyprenylbenzoate + Pyrophosphate details
All-trans-hexaprenyl diphosphate + 4-Hydroxybenzoic acid → 3-Hexaprenyl-4-hydroxybenzoic acid + Pyrophosphate details
Solanesyl-PP + 4-Hydroxybenzoic acid → Pyrophosphate + Prenyl benzoate details
GO Classification
Biological Process
glycerol metabolic process
isoprenoid biosynthetic process
ubiquinone biosynthetic process
Cellular Component
mitochondrial membrane
integral to membrane
Component
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
prenyltransferase activity
Molecular Function
4-hydroxybenzoate decaprenyltransferase activity
4-hydroxybenzoate nonaprenyltransferase activity
Process
metabolic process
biosynthetic process
Cellular Location
  1. Mitochondrion membrane
  2. Multi-pass membrane protein (Probable)
Gene Properties
Chromosome Location 4
Locus 4q21.23
SNPs COQ2
Gene Sequence
>1116 bp
ATGCTGGGCTCGCGAGCCGCGGGGTTCGCGCGGGGCCTGCGGGCTTTGGCACTGGCGTGG
CTGCCGGGCTGGCGGGGCCGCTCCTTCGCCCTGGCGCGTGCGGCAGGCGCGCCCCACGGT
GGTGACTTGCAGCCCCCCGCCTGTCCCGAGCCGCGCGGGCGCCAGCTCAGTTTGTCCGCG
GCGGCGGTGGTGGACTCTGCGCCCCGCCCCCTGCAGCCGTACTTGCGCCTCATGCGGTTG
GACAAGCCCATTGGAACCTGGCTTCTGTATTTACCATGTACCTGGAGCATTGGTTTGGCA
GCTGAACCAGGTTGTTTTCCAGATTGGTACATGCTCTCCCTCTTTGGCACTGGAGCTATT
CTGATGCGTGGAGCAGGCTGTACTATTAATGACATGTGGGACCAGGACTATGATAAAAAG
GTTACAAGAACAGCCAATCGTCCAATAGCCGCTGGAGACATTTCAACTTTTCAGTCCTTT
GTTTTTCTTGGGGGACAGCTAACCCTGGCACTGGGTGTTCTTCTGTGTCTAAATTACTAC
AGTATAGCTCTGGGAGCAGGATCCTTACTTCTTGTCATCACCTACCCACTAATGAAAAGA
ATTTCATACTGGCCTCAACTAGCCTTGGGCTTGACATTTAATTGGGGAGCGTTACTTGGA
TGGTCTGCTATCAAGGGTTCCTGTGATCCATCTGTTTGCCTGCCTCTTTATTTTTCTGGA
GTTATGTGGACACTAATATATGACACTATTTATGCCCATCAGGACAAAAGAGATGATGTT
TTGATTGGTCTTAAGTCAACGGCTCTGCGGTTCGGAGAAAATACCAAGCCGTGGCTCAGC
GGCTTCAGTGTTGCAATGCTGGGGGCACTGAGCCTAGTGGGTGTGAACAGTGGACAGACT
GCTCCCTACTACGCTGCCCTGGGTGCTGTAGGAGCCCATCTGACTCACCAGATTTACACT
CTAGACATCCACAGACCTGAGGATTGTTGGAATAAATTTATCTCCAACCGAACACTGGGA
CTAATAGTTTTTTTAGGGATTGTCCTTGGGAATTTGTGGAAAGAAAAGAAGACAGACAAA
ACAAAGAAGGGTATAGAGAATAAAATAGAAAATTAA
Protein Properties
Number of Residues 371
Molecular Weight 45593.67
Theoretical pI 9.586
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Para-hydroxybenzoate--polyprenyltransferase, mitochondrial
MLGSRAAGFARGLRALALAWLPGWRGRSFALARAAGAPHGGDLQPPACPEPRGRQLSLSA
AAVVDSAPRPLQPYLRLMRLDKPIGTWLLYLPCTWSIGLAAEPGCFPDWYMLSLFGTGAI
LMRGAGCTINDMWDQDYDKKVTRTANRPIAAGDISTFQSFVFLGGQLTLALGVLLCLNYY
SIALGAGSLLLVITYPLMKRISYWPQLALGLTFNWGALLGWSAIKGSCDPSVCLPLYFSG
VMWTLIYDTIYAHQDKRDDVLIGLKSTALRFGENTKPWLSGFSVAMLGALSLVGVNSGQT
APYYAALGAVGAHLTHQIYTLDIHRPEDCWNKFISNRTLGLIVFLGIVLGNLWKEKKTDK
TKKGIENKIEN
GenBank ID Protein 14250676
UniProtKB/Swiss-Prot ID Q96H96
UniProtKB/Swiss-Prot Entry Name COQ2_HUMAN
PDB IDs Not Available
GenBank Gene ID BC008804
GeneCard ID COQ2
GenAtlas ID COQ2
HGNC ID HGNC:25223
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Forsgren M, Attersand A, Lake S, Grunler J, Swiezewska E, Dallner G, Climent I: Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ. Biochem J. 2004 Sep 1;382(Pt 2):519-26. [PubMed:15153069 ]
  3. Quinzii C, Naini A, Salviati L, Trevisson E, Navas P, Dimauro S, Hirano M: A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency. Am J Hum Genet. 2006 Feb;78(2):345-9. Epub 2005 Dec 22. [PubMed:16400613 ]