COQ2_YEAST
ID COQ2_YEAST Reviewed; 372 AA.
AC P32378; D6W1L7; Q6B1I3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000305};
DE Short=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000305|PubMed:1740455};
DE AltName: Full=4-hydroxybenzoate hexaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189};
DE AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000303|PubMed:1740455};
DE Short=PHB:PPT {ECO:0000255|HAMAP-Rule:MF_03189};
DE Short=PHB:polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000303|PubMed:1740455};
DE Flags: Precursor;
GN Name=COQ2 {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000303|PubMed:1740455};
GN OrderedLocusNames=YNR041C {ECO:0000312|SGD:S000005324}; ORFNames=N3419;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND PATHWAY.
RX PubMed=1740455; DOI=10.1016/s0021-9258(19)50638-x;
RA Ashby M.N., Kutsunai S.Y., Ackerman S., Tzagoloff A., Edwards P.A.;
RT "COQ2 is a candidate for the structural gene encoding para-
RT hydroxybenzoate:polyprenyltransferase.";
RL J. Biol. Chem. 267:4128-4136(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=24406904; DOI=10.1016/j.bbalip.2013.12.017;
RA He C.H., Xie L.X., Allan C.M., Tran U.C., Clarke C.F.;
RT "Coenzyme Q supplementation or over-expression of the yeast Coq8 putative
RT kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null
RT mutants.";
RL Biochim. Biophys. Acta 1841:630-644(2014).
CC -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with
CC an all-trans polyprenyl group. Mediates the second step in the final
CC reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the
CC condensation of the polyisoprenoid side chain with PHB, generating the
CC first membrane-bound Q intermediate. {ECO:0000255|HAMAP-Rule:MF_03189,
CC ECO:0000269|PubMed:1740455}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03189, ECO:0000305|PubMed:1740455};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03189,
CC ECO:0000269|PubMed:1740455};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000305|PubMed:1740455}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03189, ECO:0000269|PubMed:16823961,
CC ECO:0000269|PubMed:24406904}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-
CC Rule:MF_03189, ECO:0000269|PubMed:24406904}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000305}.
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DR EMBL; M81698; AAA34507.1; -; Genomic_DNA.
DR EMBL; Z71656; CAA96321.1; -; Genomic_DNA.
DR EMBL; AY693097; AAT93116.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10583.1; -; Genomic_DNA.
DR PIR; S20056; S20056.
DR RefSeq; NP_014439.3; NM_001183218.3.
DR AlphaFoldDB; P32378; -.
DR SMR; P32378; -.
DR BioGRID; 35867; 327.
DR DIP; DIP-4655N; -.
DR IntAct; P32378; 5.
DR MINT; P32378; -.
DR STRING; 4932.YNR041C; -.
DR iPTMnet; P32378; -.
DR MaxQB; P32378; -.
DR PaxDb; P32378; -.
DR PRIDE; P32378; -.
DR EnsemblFungi; YNR041C_mRNA; YNR041C; YNR041C.
DR GeneID; 855778; -.
DR KEGG; sce:YNR041C; -.
DR SGD; S000005324; COQ2.
DR VEuPathDB; FungiDB:YNR041C; -.
DR eggNOG; KOG1381; Eukaryota.
DR GeneTree; ENSGT00940000153771; -.
DR HOGENOM; CLU_034879_2_2_1; -.
DR InParanoid; P32378; -.
DR OMA; PTQCLWY; -.
DR BioCyc; MetaCyc:YNR041C-MON; -.
DR BioCyc; YEAST:YNR041C-MON; -.
DR BRENDA; 2.5.1.39; 984.
DR Reactome; R-SCE-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:P32378; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P32378; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IMP:SGD.
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; IMP:SGD.
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 1: Evidence at protein 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..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT CHAIN 43..372
FT /note="4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT /id="PRO_0000035921"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT CONFLICT 273
FT /note="A -> T (in Ref. 4; AAT93116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41001 MW; 4D9738CE248B4AD6 CRC64;
MFIWQRKSIL LGRSILGSGR VTVAGIIGSS RKRYTSSSSS SSSPSSKESA PVFTSKELEV
ARKERLDGLG PFVSRLPKKW IPYAELMRLE KPVGTWLLYL PCSWSILMGA MMQGATLSAT
AGMLGIFGVG ALVMRGAGCT INDFLDRKLD QRVIRSVERP IASGRVSPRR ALVFLGAQTL
VGMGVLSLLP AQCWWLGLAS LPIVFTYPLF KRFTYYPQAA LSACFNWGAL LGFPAMGVMS
WPTMIPLYLS SYLWCMTYDT IYAHQDKKFD IKAGIKSTAL AWGPRTKSIM KAMSASQIAL
LAVAGLNSGL LWGPGFIGGL GVFAYRLFSM IKKVDLDNPK NCWKYFNANI NTGLYFTYAL
AVDYILRLFG FL
