ID A0A1Q8X2D3_9ACTO Unreviewed; 241 AA. AC A0A1Q8X2D3; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 24-JAN-2024, entry version 22. DE RecName: Full=Demethylmenaquinone methyltransferase {ECO:0000256|HAMAP-Rule:MF_01813}; DE EC=2.1.1.163 {ECO:0000256|HAMAP-Rule:MF_01813}; GN Name=menG {ECO:0000256|HAMAP-Rule:MF_01813}; GN ORFNames=BKH18_08975 {ECO:0000313|EMBL:OLO74469.1}; OS Actinomyces oris. OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=544580 {ECO:0000313|EMBL:OLO74469.1, ECO:0000313|Proteomes:UP000186219}; RN [1] {ECO:0000313|EMBL:OLO74469.1, ECO:0000313|Proteomes:UP000186219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R23275 {ECO:0000313|EMBL:OLO74469.1, RC ECO:0000313|Proteomes:UP000186219}; RA Mughal S.R., Do T., Gilbert S.C., Witherden E.A., Didelot X., Beighton D.; RT "Genomic comparison of strains in the 'Actinomyces naeslundii' group."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Methyltransferase required for the conversion of CC demethylmenaquinol (DMKH2) to menaquinol (MKH2). {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_01813}; CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis; CC menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2. CC {ECO:0000256|HAMAP-Rule:MF_01813}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. MenG/UbiE family. {ECO:0000256|HAMAP-Rule:MF_01813}. 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:OLO74469.1}. 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; MSKU01000044; OLO74469.1; -; Genomic_DNA. DR RefSeq; WP_075375095.1; NZ_MSKU01000044.1. DR AlphaFoldDB; A0A1Q8X2D3; -. DR UniPathway; UPA00079; UER00169. DR Proteomes; UP000186219; Unassembled WGS sequence. DR GO; GO:0043770; F:demethylmenaquinone methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro. 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:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. 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 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. PE 3: Inferred from homology; KW Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP- KW Rule:MF_01813}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_01813}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_01813}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01813}. FT BINDING 66 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813" FT BINDING 84 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813" FT BINDING 106..107 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813" FT BINDING 123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813" SQ SEQUENCE 241 AA; 26024 MW; 0FE2AD2BB9738E12 CRC64; MSRSALRASL AKDPREVAGM FDAVARRYDL SNDVMSLFQV HMWRRVTRAA VAARPGTRVL DLAAGTGTSS VEYAADGAEV VACDFSTGMV AEGKRRHPEI AFVAGDATAL PFADGSFDVV TISYGLRNVQ DTARALSEMR RVTVPGGRIV IAEFSTPTWP AFRHLYRFYL GSALPAAARL VSSNTEAYDY LGESILAWPD QQKLAGLMQQ AGWRGVGYKN LSGGIVAVHR ATRPVPAQGE Q //