ID   COQ5_LEIDO              Reviewed;         288 AA.
AC   P55905;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=MHOM/SD/00/1S-C12D;
RX   PubMed=8479459; DOI=10.1016/0166-6851(93)90057-5;
RA   Nakhasi H.L., Joshi M., Dwyer D.;
RT   "Cloning and characterization of differentially expressed genes from in
RT   vitro-grown 'amastigotes' of Leishmania donovani.";
RL   Mol. Biochem. Parasitol. 58:345-354(1993).
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   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       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; L06118; AAK14902.1; -; mRNA.
DR   PIR; B48583; B48583.
DR   RefSeq; XP_003865672.1; XM_003865624.1.
DR   AlphaFoldDB; P55905; -.
DR   SMR; P55905; -.
DR   GeneID; 13388558; -.
DR   KEGG; ldo:LDBPK_365590; -.
DR   VEuPathDB; TriTrypDB:LdBPK_365590.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_360063200; -.
DR   VEuPathDB; TriTrypDB:LDHU3_36.7420; -.
DR   OMA; VRNFENL; -.
DR   UniPathway; UPA00232; -.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
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   S-adenosyl-L-methionine; Transferase; Ubiquinone biosynthesis.
FT   CHAIN           1..288
FT                   /note="2-methoxy-6-polyprenyl-1,4-benzoquinol methylase,
FT                   mitochondrial"
FT                   /id="PRO_0000193363"
FT   REGION          260..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   BINDING         102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
FT   BINDING         146
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03191"
SQ   SEQUENCE   288 AA;  31975 MW;  0D17D477E37C5CEB CRC64;
     MLHYTRLGRN MGLGDAYVKK VFDSVATKYD MMNDVLSLGI HRIWKKHFVE DCVCPLPGSK
     FLDVAGGTGD IAFRITDSIR ARGQSFGIVP KTLDGTKVVV CDINAMMLKE GQKRAEREGY
     MDIDWVCASG EELPFEDGAF DSYTVSFGIR NFSDRPKALR EAFRVLKVGG ALHVLEFSRV
     TCPLLSVPYE LWSYGFMPQA GRMLADEESY RYLVDSIRAF PDQETFAQMI RDAGFGYVRY
     ENLTGGIACI HTGVKTTPTP ITPTTSSDIP AQNTSEATCE VKPEPNSA