ID UBIE_SHESR Reviewed; 251 AA. AC Q0HZP7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE {ECO:0000255|HAMAP-Rule:MF_01813}; DE EC=2.1.1.163 {ECO:0000255|HAMAP-Rule:MF_01813}; DE EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_01813}; DE AltName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase {ECO:0000255|HAMAP-Rule:MF_01813}; DE AltName: Full=Demethylmenaquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01813}; GN Name=ubiE {ECO:0000255|HAMAP-Rule:MF_01813}; GN OrderedLocusNames=Shewmr7_0405; OS Shewanella sp. (strain MR-7). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=60481; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-7; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Methyltransferase required for the conversion of CC demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of CC 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3- CC methyl-6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP- CC Rule:MF_01813}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2-demethylmenaquinol + S-adenosyl-L-methionine = a CC menaquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42640, CC Rhea:RHEA-COMP:9539, Rhea:RHEA-COMP:9563, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:18151, ChEBI:CHEBI:55437, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789; EC=2.1.1.163; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01813}; 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_01813}; CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis; CC menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_01813}. 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; CP000444; ABI41408.1; -; Genomic_DNA. DR AlphaFoldDB; Q0HZP7; -. DR SMR; Q0HZP7; -. DR KEGG; shm:Shewmr7_0405; -. DR HOGENOM; CLU_037990_0_0_6; -. DR UniPathway; UPA00079; UER00169. DR UniPathway; UPA00232; -. DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC. DR GO; GO:0043770; F:demethylmenaquinone methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0102094; F:S-adenosylmethionine:2-demethylmenaquinol methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0102955; F:S-adenosylmethionine:2-demethylmenaquinol-7 methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0102027; F:S-adenosylmethionine:2-demethylquinol-8 methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009060; P:aerobic respiration; IEA:UniProtKB-UniRule. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd02440; AdoMet_MTases; 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 Menaquinone biosynthesis; Methyltransferase; S-adenosyl-L-methionine; KW Transferase; Ubiquinone biosynthesis. FT CHAIN 1..251 FT /note="Ubiquinone/menaquinone biosynthesis C- FT methyltransferase UbiE" FT /id="PRO_1000056301" FT BINDING 74 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813" FT BINDING 95 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813" FT BINDING 123..124 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813" SQ SEQUENCE 251 AA; 28105 MW; E433C97ACB23BE56 CRC64; MSEGESKNTH FGYKTVEADK KADLVAGVFH SVAAKYDIMN DVMSFGIHRF WKRYTIEVSG ARPGMKVLDL AGGTGDLTAK FSHLVGEKGE VVLADINDSM LKVGRTKLRD RGIVGNVSYV QANAEALPFP DNHFDIITIA FGLRNVTDKD AALRSMNRVL KPGGKLLVLE FSKPQHELMR KVYDLYSFKV LPKMGEIITK DADSYEYLAE SIRMHPDQET LKQMMVDAGF EQVDYTNMTD GIVALHRGYK F //