ID Q4WMS8_ASPFU Unreviewed; 313 AA. AC Q4WMS8; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 02-SEP-2026, entry version 117. DE RecName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03191}; DE EC=2.1.1.201 {ECO:0000256|HAMAP-Rule:MF_03191}; DE AltName: Full=Ubiquinone biosynthesis methyltransferase COQ5 {ECO:0000256|HAMAP-Rule:MF_03191}; GN Name=COQ5 {ECO:0000256|HAMAP-Rule:MF_03191}; GN ORFNames=AFUA_6G08850 {ECO:0000313|EMBL:EAL88736.1}; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Fumigati. OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88736.1, ECO:0000313|Proteomes:UP000002530}; RN [1] {ECO:0000313|EMBL:EAL88736.1, ECO:0000313|Proteomes:UP000002530} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293 RC {ECO:0000313|Proteomes:UP000002530}; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M., RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A., RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H., RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P., RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S., RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H., RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B., RA Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(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:0000256|HAMAP-Rule:MF_03191}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2-methoxy-6-(all-trans-polyprenyl)benzene-1,4-diol + S- CC adenosyl-L-methionine = a 5-methoxy-2-methyl-3-(all-trans- CC polyprenyl)benzene-1,4-diol + S-adenosyl-L-homocysteine + H(+); 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:0000256|HAMAP-Rule:MF_03191, ECO:0000256|PROSITE- CC ProRule:PRU00940}; CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_03191}. CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000256|HAMAP- CC Rule:MF_03191}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP- CC Rule:MF_03191}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_03191}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03191}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. MenG/UbiE family. {ECO:0000256|HAMAP-Rule:MF_03191, CC ECO:0000256|PROSITE-ProRule:PRU00940}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03191}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EAL88736.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000006; EAL88736.1; -; Genomic_DNA. DR RefSeq; XP_750774.1; XM_745681.1. DR AlphaFoldDB; Q4WMS8; -. DR FunCoup; Q4WMS8; 476. DR STRING; 330879.Q4WMS8; -. DR GeneID; 3508061; -. DR KEGG; afm:AFUA_6G08850; -. DR VEuPathDB; FungiDB:Afu6g08850; -. DR eggNOG; KOG1540; Eukaryota. DR HOGENOM; CLU_037990_0_1_1; -. DR InParanoid; Q4WMS8; -. DR OMA; MNDVMSM; -. DR OrthoDB; 6329284at2759; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000002530; Unassembled WGS sequence. DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi. DR GO; GO:0008425; F:2-methoxy-6-polyprenyl-1,4-benzoquinol methyltransferase activity; IBA:GO_Central. DR GO; GO:0009060; P:aerobic respiration; IEA:EnsemblFungi. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central. DR CDD; cd02440; AdoMet_MTases; 1. DR FunFam; 3.40.50.150:FF:000133; 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR01934; MenG_MenH_UbiE; 1. DR PANTHER; PTHR43591:SF24; 2-METHOXY-6-POLYPRENYL-1,4-BENZOQUINOL METHYLASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43591; METHYLTRANSFERASE; 1. DR Pfam; PF01209; Ubie_methyltran; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 {ECO:0000256|HAMAP-Rule:MF_03191}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_03191}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03191}; KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03191}; KW Reference proteome {ECO:0000313|Proteomes:UP000002530}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_03191}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03191}; Ubiquinone {ECO:0000313|EMBL:EAL88736.1}; KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03191, KW ECO:0000256|PROSITE-ProRule:PRU00940}. FT BINDING 123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191" FT BINDING 149 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191" FT BINDING 179..180 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03191" SQ SEQUENCE 313 AA; 35272 MW; E547589FBA91B2F2 CRC64; MSSRSLWKSL HYSAKRRVTI PQSQYRCFSC SLRVQDSKSN HEDQMTHFGF KNVPESQKES MVRTVFSSVA ASYDTMNDFM SLGIHRLWKD HFVRSLNPGS ALPSRDNDTT GKGWNILDIA GGTGDIAFRM LDHATNINND HQTRVTIADI NPDMLAEGKK RSISTPYYNT PRLSFMEANA QHMPNIPDNS VDLYTVVFGI RNFTDKQAAL EEAFRVLKPG GVFACMEFSK VDNSLFNAIY KQWSFSAIPL IGQIVAGDRD SYQYLVESIE KFPSQEEFRA MIQKAGFMIP GRGYENLTGG IAAIHKGIKP LTK //