COQ5_DROME
ID COQ5_DROME Reviewed; 301 AA.
AC Q9VYF8; Q8MR39;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03191};
DE EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_03191};
DE AltName: Full=Ubiquinone biosynthesis methyltransferase COQ5 {ECO:0000255|HAMAP-Rule:MF_03191};
DE Flags: Precursor;
GN Name=Coq5 {ECO:0000255|HAMAP-Rule:MF_03191}; ORFNames=CG2453;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Methyltransferase required for the conversion of 2-
CC polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-
CC 6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-
CC adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-
CC 1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03191};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex.
CC {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03191}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03191}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_03191}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM52653.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF48239.1; -; Genomic_DNA.
DR EMBL; AY122141; AAM52653.1; ALT_INIT; mRNA.
DR RefSeq; NP_001285193.1; NM_001298264.1.
DR RefSeq; NP_001285194.1; NM_001298265.1.
DR RefSeq; NP_572865.1; NM_132637.2.
DR AlphaFoldDB; Q9VYF8; -.
DR SMR; Q9VYF8; -.
DR BioGRID; 58657; 1.
DR IntAct; Q9VYF8; 5.
DR STRING; 7227.FBpp0073568; -.
DR PaxDb; Q9VYF8; -.
DR DNASU; 32272; -.
DR EnsemblMetazoa; FBtr0073737; FBpp0073568; FBgn0030460.
DR EnsemblMetazoa; FBtr0346124; FBpp0311953; FBgn0030460.
DR EnsemblMetazoa; FBtr0346125; FBpp0311954; FBgn0030460.
DR GeneID; 32272; -.
DR KEGG; dme:Dmel_CG2453; -.
DR UCSC; CG2453-RA; d. melanogaster.
DR CTD; 84274; -.
DR FlyBase; FBgn0030460; Coq5.
DR VEuPathDB; VectorBase:FBgn0030460; -.
DR eggNOG; KOG1540; Eukaryota.
DR HOGENOM; CLU_037990_0_1_1; -.
DR InParanoid; Q9VYF8; -.
DR OMA; VRNFENL; -.
DR OrthoDB; 1125002at2759; -.
DR PhylomeDB; Q9VYF8; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 32272; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32272; -.
DR PRO; PR:Q9VYF8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030460; Expressed in mouthpart and 21 other tissues.
DR ExpressionAtlas; Q9VYF8; baseline and differential.
DR Genevisible; Q9VYF8; DM.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043334; F:2-hexaprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR Pfam; PF01209; Ubie_methyltran; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1.
DR PROSITE; PS51608; SAM_MT_UBIE; 1.
DR PROSITE; PS01183; UBIE_1; 1.
DR PROSITE; PS01184; UBIE_2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT CHAIN 17..301
FT /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase,
FT mitochondrial"
FT /id="PRO_0000228635"
FT REGION 20..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT BINDING 173..174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
SQ SEQUENCE 301 AA; 34338 MW; B9B46C175C2211CB CRC64;
MQTTRSTRLL SLARRFVHTR TASQSAQNSK GMASGAESIS GKEKTTHFGF QTVRESEKEQ
KVHEVFEQVA NSYDVMNDAM SLGIHRVWKD VFVERLGPTH GMRLLDMAGG TGDITFRYLR
YLNNQPNPQQ RPSHVTVSDI NQHMLNVGEE RAKRLGLTTD QLSNCTVAWQ CADAEKLPFP
DASFTAYTIA FGIRNCTHVD KVLSEAYRVL QPGGRFMCLE FSHLTNETMQ WLYDQYSFQV
IPPMGQLLAG QWQAYQYLVE SIRRFPKQEQ FKQMIEQAGF DQVSYENLTF GVVSIHSGFK
L
