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COQ5_DICDI
ID   COQ5_DICDI              Reviewed;         314 AA.
AC   Q54VN2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=DDB_G0280237;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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}.
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DR   EMBL; AAFI02000035; EAL67345.1; -; Genomic_DNA.
DR   RefSeq; XP_641323.1; XM_636231.1.
DR   AlphaFoldDB; Q54VN2; -.
DR   SMR; Q54VN2; -.
DR   STRING; 44689.DDB0231541; -.
DR   PaxDb; Q54VN2; -.
DR   EnsemblProtists; EAL67345; EAL67345; DDB_G0280237.
DR   GeneID; 8622456; -.
DR   KEGG; ddi:DDB_G0280237; -.
DR   dictyBase; DDB_G0280237; coq5.
DR   eggNOG; KOG1540; Eukaryota.
DR   HOGENOM; CLU_037990_0_1_1; -.
DR   InParanoid; Q54VN2; -.
DR   OMA; VRNFENL; -.
DR   PhylomeDB; Q54VN2; -.
DR   UniPathway; UPA00232; -.
DR   PRO; PR:Q54VN2; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0043334; F:2-hexaprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; ISS:dictyBase.
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:0009060; P:aerobic respiration; ISS:dictyBase.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006743; P:ubiquinone metabolic process; ISS:dictyBase.
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   3: Inferred from homology;
KW   Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide;
KW   Ubiquinone biosynthesis.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   CHAIN           20..314
FT                   /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase,
FT                   mitochondrial"
FT                   /id="PRO_0000328351"
FT   BINDING         109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   BINDING         186..187
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   BINDING         203
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
SQ   SEQUENCE   314 AA;  35300 MW;  2BD9E94DB5CA4964 CRC64;
     MLQSLNRSVR YLSTSIGSRL YCSNTNQTTK NNTNASGVND NQQTHFGFKT VNKEDKESMV
     KDVFDSVSSS YDLMNDVMSM GIHRLWKDEL INTLNPTPGS HLLDVAGGTG DISFRFLDKI
     KTSPNYFPNI NKSNNGGGEV LKSSSLPSSA TVFDINQSML NEGKKRGLNK GYTDQSDPSI
     DWVQGNSEQL PFKDNTFNCY TVSFGIRNCT NIDQVLREAY RVLKPGGRFL CLEFSQVPNP
     LLRFAYDQYS FNVIPIMGQL ISGDRDSYSY LVESIRKFPD QETFVQMIQD AGFKQVTYKN
     LTFGICSIHS GFKL
 
 
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