COQ2_BOVIN
ID COQ2_BOVIN Reviewed; 371 AA.
AC Q2KIQ4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_03189};
DE AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=PHB:PPT {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=PHB:polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE Flags: Precursor;
GN Name=COQ2 {ECO:0000255|HAMAP-Rule:MF_03189};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the second step in the final reaction sequence of
CC coenzyme Q (CoQ) biosynthesis. Catalyzes the prenylation of para-
CC hydroxybenzoate (PHB) with an all-trans polyprenyl donor (such as all-
CC trans-decaprenyl diphosphate). The length of the polyprenyl side chain
CC varies depending on the species, in humans, the side chain is comprised
CC of 10 isoprenyls (decaprenyl) producing CoQ10 (also known as
CC ubiquinone), whereas rodents predominantly generate CoQ9. However, this
CC specificity is not complete, human tissues have low amounts of CoQ9 and
CC rodent organs contain some CoQ10. Plays a central role in the
CC biosynthesis of CoQ10. CoQ10 is a vital molecule that transports
CC electrons from mitochondrial respiratory chain complexes. CoQs also
CC function as cofactors for uncoupling protein and play a role as
CC regulators of the extracellularly-induced ceramide-dependent apoptotic
CC pathway (By similarity). Regulates mitochondrial permeability
CC transition pore (mPTP) opening and ROS production (pivotal events in
CC cell death) in a tissue specific manner (By similarity).
CC {ECO:0000250|UniProtKB:Q499N4, ECO:0000250|UniProtKB:Q96H96}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-
CC hydroxy-3-all-trans-polyprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:44504, Rhea:RHEA-COMP:9514, Rhea:RHEA-COMP:9564,
CC ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58914,
CC ChEBI:CHEBI:78396; EC=2.5.1.39;
CC Evidence={ECO:0000250|UniProtKB:Q96H96};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44505;
CC Evidence={ECO:0000250|UniProtKB:Q96H96};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-decaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-decaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:44564, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:60721, ChEBI:CHEBI:84503; EC=2.5.1.39;
CC Evidence={ECO:0000250|UniProtKB:Q96H96};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44565;
CC Evidence={ECO:0000250|UniProtKB:Q96H96};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-nonaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-nonaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:17709, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58391, ChEBI:CHEBI:84502; EC=2.5.1.39;
CC Evidence={ECO:0000250|UniProtKB:Q96H96};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17710;
CC Evidence={ECO:0000250|UniProtKB:Q96H96};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03189};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000250|UniProtKB:Q96H96}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03189}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03189}.
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DR EMBL; BC112551; AAI12552.1; -; mRNA.
DR RefSeq; NP_001039358.1; NM_001045893.2.
DR AlphaFoldDB; Q2KIQ4; -.
DR SMR; Q2KIQ4; -.
DR STRING; 9913.ENSBTAP00000007549; -.
DR PaxDb; Q2KIQ4; -.
DR PRIDE; Q2KIQ4; -.
DR GeneID; 504633; -.
DR KEGG; bta:504633; -.
DR CTD; 27235; -.
DR eggNOG; KOG1381; Eukaryota.
DR InParanoid; Q2KIQ4; -.
DR OrthoDB; 1343847at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR006370; HB_polyprenyltransferase-like.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 2: Evidence at transcript level;
KW Isoprene biosynthesis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT CHAIN 46..371
FT /note="4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT /id="PRO_0000262866"
FT TOPO_DOM 46..83
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 105..108
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 130..171
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 193..200
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 222..231
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 253..277
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 299..300
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 322..332
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TOPO_DOM 354..371
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q96H96"
SQ SEQUENCE 371 AA; 40628 MW; 63617A2E114D06CE CRC64;
MLGSCGAGLV RGLRAETQAW LWGTRGRSLA LVHAARGLHA ANWQPSPGQG PRGRPLSLSA
AAVVNSAPRP LQPYLRLMRL DKPIGTWLLY LPCTWSIGLA ADPGCLPDWY MLSLFGTGAV
LMRGAGCTIN DMWDRDYDKK VTRTASRPIA AGDISTFRSF VFLGGQLTLA LGVLLCLNYY
SIALGAASLL LVTTYPLMKR ITYWPQLALG LTFNWGALLG WSAVKGSCDP SVCLPLYFSG
IMWTLIYDTI YAHQDKKDDA LIGLKSTALL FREDTKKWLS GFSVAMLGAL SLVGVNSGQT
MPYYTALAAV GAHLAHQIYT LDINRPEDCW EKFTSNRTIG LIIFLGIVLG NLCKAKETDK
TRKNIENRME N
