Q9VHS7

PR
Gene name
Coq2
Protein name
4-hydroxybenzoate polyprenyltransferase, mitochondrial
Names
4-HB polyprenyltransferase, Coenzyme Q biosynthesis protein 2, Para-hydroxybenzoate--polyprenyltransferase, PHB:PPT, PHB:polyprenyltransferase
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG9613
EC number
2.5.1.39: Transferring alkyl or aryl groups, other than methyl groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

18-100 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9VHS7

Entry ID Method Resolution Chain Position Source
AF-Q9VHS7-F1 Predicted AlphaFoldDB

No variants for Q9VHS7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VHS7

No associated diseases with Q9VHS7

1 regional properties for Q9VHS7

Type Name Position InterPro Accession
conserved_site UbiA prenyltransferase conserved site 136 - 158 IPR030470

Functions

Description
EC Number 2.5.1.39 Transferring alkyl or aryl groups, other than methyl groups
Subcellular Localization
  • Mitochondrion inner membrane ; Multi-pass membrane protein ; Matrix side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
integral component of mitochondrial inner membrane The component of the mitochondrial inner membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.

4 GO annotations of molecular function

Name Definition
4-hydroxybenzoate decaprenyltransferase activity Catalysis of the reaction: all-trans-decaprenyl diphosphate + 4-hydroxybenzoate = 3-decaprenyl-4-hydroxybenzoate + diphosphate.
4-hydroxybenzoate nonaprenyltransferase activity Catalysis of the reaction: p-hydroxybenzoate + solanesyl pyrophosphate = nonaprenyl-4-hydroxybenzoate + diphosphate.
4-hydroxybenzoate octaprenyltransferase activity Catalysis of the reaction: farnesylfarnesylgeranyl diphosphate + p-hydroxybenzoate = 3-octaprenyl-4-hydroxybenzoate + diphosphate.
transferase activity, transferring alkyl or aryl (other than methyl) groups Catalysis of the transfer of an alkyl or aryl (but not methyl) group from one compound (donor) to another (acceptor).

6 GO annotations of biological process

Name Definition
defense response to fungus Reactions triggered in response to the presence of a fungus that act to protect the cell or organism.
defense response to Gram-negative bacterium Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.
defense response to Gram-positive bacterium Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.
determination of adult lifespan The pathways that regulate the duration of the adult phase of the life-cycle of an animal.
isoprenoid biosynthetic process The chemical reactions and pathways resulting in the formation of an isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues.
ubiquinone biosynthetic process The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8I7J4 coq-2 4-hydroxybenzoate polyprenyltransferase, mitochondrial Caenorhabditis elegans PR
10 20 30 40 50 60
MYALRHLRLQ SARHFRSSYA AAATTKHMLP RQPARVLIGD WSTWDKSRLQ DVCSRSSSTA
70 80 90 100 110 120
TEPVKQQTPL QELVSAAKPY AQLMRIDRPI GTYLLFWPCA WSIALSADAG CWPDLTMLGL
130 140 150 160 170 180
FGTGALIMRG AGCTINDLWD KDIDAKVERT RLRPLASGQI SQFDAIVFLS AQLSLGLLVL
190 200 210 220 230 240
VQLNWQSILL GASSLGLVIT YPLMKRVTYW PQLVLGMAFN WGALLGWCAT QGSVNLAACL
250 260 270 280 290 300
PLYLSGVCWT IVYDTIYAHQ DKLDDLQIGV KSTALRFGEN TKVWLSGFTA AMLTGLSAAG
310 320 330 340 350 360
WACDQTVPYY AAVGVVGAHL VQQIYSLNID NPSDCAKKFI SNHQVGLILF LGIVLGTLLK
370 380 390
SDESKKQRQS SLTTSTASSY VPALPQKPEV LS