ID A0A834K3W4_VESGE Unreviewed; 906 AA. AC A0A834K3W4; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 14-DEC-2022, entry version 5. DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03190}; DE AltName: Full=3-demethylubiquinol 3-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190}; DE EC=2.1.1.64 {ECO:0000256|HAMAP-Rule:MF_03190}; DE AltName: Full=Polyprenyldihydroxybenzoate methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190}; DE EC=2.1.1.114 {ECO:0000256|HAMAP-Rule:MF_03190}; GN Name=coq3 {ECO:0000256|HAMAP-Rule:MF_03190}; GN ORFNames=HZH68_008153 {ECO:0000313|EMBL:KAF7399561.1}; OS Vespula germanica (German yellow jacket) (Paravespula germanica). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea; OC Vespidae; Vespinae; Vespula. OX NCBI_TaxID=30212 {ECO:0000313|EMBL:KAF7399561.1, ECO:0000313|Proteomes:UP000617340}; RN [1] {ECO:0000313|EMBL:KAF7399561.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Linc-1 {ECO:0000313|EMBL:KAF7399561.1}; RX PubMed=32859687; DOI=10.1534/g3.120.401579; RA Harrop T.W.R., Guhlin J., McLaughlin G.M., Permina E., Stockwell P., RA Gilligan J., Le Lec M.F., Gruber M.A.M., Quinn O., Lovegrove M., RA Duncan E.J., Remnant E.J., Van Eeckhoven J., Graham B., Knapp R.A., RA Langford K.W., Kronenberg Z., Press M.O., Eacker S.M., Wilson-Rankin E.E., RA Purcell J., Lester P.J., Dearden P.K.; RT "High-Quality Assemblies for Three Invasive Social Wasps from the RT Vespula Genus."; RL G3 (Bethesda) 10:3479-3488(2020). CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps CC in the ubiquinone biosynthetic pathway. {ECO:0000256|HAMAP- CC Rule:MF_03190}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L- CC methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44452, Rhea:RHEA- CC COMP:10930, Rhea:RHEA-COMP:10931, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64694, CC ChEBI:CHEBI:84443; EC=2.1.1.114; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03190}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA- CC COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03190}; CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_03190}. CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex. CC {ECO:0000256|HAMAP-Rule:MF_03190}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP- CC Rule:MF_03190}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_03190}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03190}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. UbiG/COQ3 family. {ECO:0000256|HAMAP-Rule:MF_03190}. 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:KAF7399561.1}. 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; JACSDZ010000007; KAF7399561.1; -; Genomic_DNA. DR AlphaFoldDB; A0A834K3W4; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000617340; Unassembled WGS sequence. DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule. DR GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro. DR GO; GO:0010420; F:3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0061542; F:3-demethylubiquinol-n 3-O-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. 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_00472; UbiG; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR003891; Initiation_fac_eIF4g_MI. DR InterPro; IPR003890; MIF4G-like_typ-3. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR010233; UbiG_MeTrfase. DR Pfam; PF02847; MA3; 1. DR Pfam; PF02854; MIF4G; 1. DR SMART; SM00544; MA3; 1. DR SMART; SM00543; MIF4G; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR TIGRFAMs; TIGR01983; UbiG; 1. DR PROSITE; PS51366; MI; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|HAMAP-Rule:MF_03190}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190}; KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03190}; KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03190}; KW Reference proteome {ECO:0000313|Proteomes:UP000617340}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03190}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03190}; KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03190}. FT DOMAIN 450..566 FT /note="MI" FT /evidence="ECO:0000259|PROSITE:PS51366" FT REGION 30..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 404..437 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 30..117 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 412..432 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 696 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190" FT BINDING 727 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190" FT BINDING 748 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190" FT BINDING 795 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03190" SQ SEQUENCE 906 AA; 103923 MW; DFDB897420DDA98C CRC64; MRFQRQVNSC FASYQYKFER FSRIIEKENM ERHSERRSER YSERYSDRHS ERRSEKRSER RSEKHSERYS DRRPDKHSDK HSDKHSDKHS DKHSDKHSEK RSEKHSEKRH TTETMTNNRK RTVDLLTAKT GGAYIPPAKL RMMQANITDK SGAAYQRIAW EALKKSIHGC INKVNVSNIG LITRELLREN IVRGRGLLAR SIIQAQAASP TFTPVYAALT AIINSKFPNI GELILKRLII QFKRGFRRND KPLCISSGTF VAHLLNQRVA HEILPLEILT LLVETPTDDS VEVAIAFLKE CGMKLTEVSR KGIEAIFEML RNILHEGQLD KRVQYMIEVM FQIRKDGFKD HQAVPQELDL VEEENQFTHL IQLDEAIDSQ DILNVFKFDS DYVTNEEKYK QLSKEILGSD DSDSEAGEDD EESSDEDSNA EIAEEKEGVI VDNTETNLTA LRRTIYLTIH SSLDFEECAH KLMKMQLKPG QEIELCHMFL DCCAEMRTYE KFFGLLAGRF CAINKIYVTP FEQIFQDSYH TIHRLDTNKL RNVSKFFAHL LFTDSISWEV LSCIKLNEED TTSSNRIFIK ILFQELSEYM GLSKLNQRVK DVTLQEAFSG LFPRDNPKNT RFAINFFTSI GLGGLTDDLR EHLKSSSETP KYVTNSIRPI GSSIDSKEIE FFGKLNNKWW DPNGHLALLH IMNHIRVQFV RDGLANTGII KDDTNLPLEG TKIVDIGCGG GIFSEPLARI GAEVTGIDNS LELIDVAKEH ASLDSTLSGK LNYIQTTIEE FEKENIEKYD AVIASEVLEH VADQRLFLKS CSSIIKPGGS LFITTINKTL PSWLGAIIAA EYILKLVPIG THDWDKFISP EEVQRFLEIC GLKTKLIHGM IFNPIKYEWS WSSNTSINYA LHAIKQ //