COQ2_DROPS
ID COQ2_DROPS Reviewed; 397 AA.
AC Q298G6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Coenzyme Q biosynthesis protein 2;
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}; ORFNames=GA21912;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL27989.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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 -!- 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};
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:0000255|HAMAP-Rule:MF_03189}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL27989.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000070; EAL27989.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001358846.1; XM_001358809.3.
DR RefSeq; XP_015037401.1; XM_015181915.1.
DR AlphaFoldDB; Q298G6; -.
DR SMR; Q298G6; -.
DR STRING; 7237.FBpp0281971; -.
DR PRIDE; Q298G6; -.
DR EnsemblMetazoa; FBtr0283533; FBpp0281971; FBgn0081897.
DR EnsemblMetazoa; FBtr0370374; FBpp0332769; FBgn0081897.
DR GeneID; 4801812; -.
DR KEGG; dpo:Dpse_GA21912; -.
DR eggNOG; KOG1381; Eukaryota.
DR HOGENOM; CLU_034879_3_1_1; -.
DR InParanoid; Q298G6; -.
DR OMA; MVVYPYG; -.
DR PhylomeDB; Q298G6; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0081897; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblMetazoa.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006383; P:transcription by RNA polymerase III; ISS:UniProtKB.
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 3: Inferred from homology;
KW Isoprene biosynthesis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT CHAIN 15..397
FT /note="4-hydroxybenzoate polyprenyltransferase,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT /id="PRO_0000307703"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03189"
SQ SEQUENCE 397 AA; 43326 MW; A6DD94CF25AF0580 CRC64;
MFAVRHLLKS RKHFPYAYAA ATTTKSTLPM PAVPARVLIG LHTDSDCRNK RLPQIQELSF
RKMSSLPTSK KPGSLLEELY AATKPYAQLM RIDRPIGTYL LFWPCAWSIA LSADAGCWPD
LTMLGLFGTG ALIMRGAGCT INDLWDKDID AKVERTRTRP LASGQISQFD AIVFLSAQLS
LGLLVLVQLN WQSILLGASS LGLVITYPLM KRVTYWPQLV LGMAFNWGAL LGWCATQGSV
NLAACLPLYL SGVCWTIVYD TIYAHQDKLD DLQIGVKSTA LRFGENTKVW LSGFTAAMLT
GLSTAGWACD QTLPYYAAVG VVGAHLVQQI YSLNIDNPTD CAKKFLSNHQ VGLILFLGIV
LGTLLKANDT KNQPQPALTS SAASSYASLT QKPEVLS
