ID UBIE_BRUA2 Reviewed; 269 AA. AC Q2YJM4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 102. 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=BAB2_1026; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). 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; AM040265; CAJ13192.1; -; Genomic_DNA. DR RefSeq; WP_002965588.1; NZ_KN046823.1. DR AlphaFoldDB; Q2YJM4; -. DR SMR; Q2YJM4; -. DR STRING; 359391.BAB2_1026; -. DR GeneID; 58777123; -. DR KEGG; bmf:BAB2_1026; -. DR PATRIC; fig|359391.11.peg.714; -. DR HOGENOM; CLU_037990_0_0_5; -. DR PhylomeDB; Q2YJM4; -. DR UniPathway; UPA00079; UER00169. DR UniPathway; UPA00232; -. DR Proteomes; UP000002719; Chromosome II. 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; Reference proteome; KW S-adenosyl-L-methionine; Transferase; Ubiquinone biosynthesis. FT CHAIN 1..269 FT /note="Ubiquinone/menaquinone biosynthesis C- FT methyltransferase UbiE" FT /id="PRO_1000088274" FT BINDING 92 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813" FT BINDING 113 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813" FT BINDING 141..142 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01813" SQ SEQUENCE 269 AA; 29898 MW; 7A7D0AD3D80A7EC4 CRC64; MSQQNGNVNR VGAQDRVGAS GGMEHSFGFK AVDENEKQGL VNDVFHKVAK RYDIMNDLMS AGMHRVWKDA MVAWLAPSKR PGWTSLDVAG GTGDIAFRIV EASGRQAHVT ILDINGSMLG VGRERAIKKG LIDNLEFVEA NAEELPFEDN SFDAYTIAFG IRNVPHIDKA LSEAYRVLKP GGRFLCLEFS EVELPVLDKV YDEWSFRAIP RIGKMITGDA DSYSYLVESI RKFPKQQDFA AMIEKAGFER VSYRNFTGGI AALHSGWKL //