ID C6J433_9BACL Unreviewed; 242 AA.
AC C6J433;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=POTG_03160 {ECO:0000313|EMBL:EES72320.1};
OS Paenibacillus sp. oral taxon 786 str. D14.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES72320.1, ECO:0000313|Proteomes:UP000003981};
RN [1] {ECO:0000313|EMBL:EES72320.1, ECO:0000313|Proteomes:UP000003981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D14 {ECO:0000313|EMBL:EES72320.1,
RC ECO:0000313|Proteomes:UP000003981};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C., White A.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Paenibacillus sp. D14.";
RL Submitted (MAR-2009) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01813}.
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DR EMBL; GG695983; EES72320.1; -; Genomic_DNA.
DR RefSeq; WP_009225878.1; NZ_GG695983.1.
DR AlphaFoldDB; C6J433; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_037990_0_0_9; -.
DR OrthoDB; 9808140at2; -.
DR UniPathway; UPA00079; UER00169.
DR Proteomes; UP000003981; 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 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 {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW Rule:MF_01813};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01813}; Reference proteome {ECO:0000313|Proteomes:UP000003981};
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}; Ubiquinone {ECO:0000313|EMBL:EES72320.1}.
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 110..111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ SEQUENCE 242 AA; 27726 MW; 1A182D670A22AB84 CRC64;
MSQTSSSETK EQFVHSVFES IAPKYDMMND LLSFRRHKAW RKFTMAKMNM SPGETALDLC
CGTCDWTISM AEASGGQIIG LDFSERMLEY GRLKVKERGL ESRITLVQGN AMELPFEDNR
FDYVTIGFGL RNVPDLRQVL REMRRVVKPG GKVVCLELSK PTWQPFKGLY YFYFQNVLPM
LGKLVAKRYE QYKWLPDSLV QFPGRAELAE IFRETGLTRV EAYPLTGGIA ALHIGTKETQ
HV
//