ID A0A0D4C0C8_9MICC Unreviewed; 237 AA.
AC A0A0D4C0C8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=UM93_10765 {ECO:0000313|EMBL:AJT41875.1};
OS Psychromicrobium lacuslunae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Psychromicrobium.
OX NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT41875.1, ECO:0000313|Proteomes:UP000061839};
RN [1] {ECO:0000313|EMBL:AJT41875.1, ECO:0000313|Proteomes:UP000061839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT41875.1,
RC ECO:0000313|Proteomes:UP000061839};
RX PubMed=25908143;
RA Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter sp.
RT Strain IHBB 11108 Using PacBio Single-Molecule Real-Time Sequencing
RT Technology.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP011005; AJT41875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D4C0C8; -.
DR STRING; 1618207.UM93_10765; -.
DR KEGG; ari:UM93_10765; -.
DR PATRIC; fig|1618207.4.peg.2182; -.
DR HOGENOM; CLU_037990_0_0_11; -.
DR OrthoDB; 9808140at2; -.
DR UniPathway; UPA00079; UER00169.
DR Proteomes; UP000061839; Chromosome.
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: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:UniProt.
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; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43591:SF106; METHYLTRANSFERASE-LIKE PROTEIN 27; 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; PS01184; UBIE_2; 1.
PE 3: Inferred from homology;
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01813};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01813}; Reference proteome {ECO:0000313|Proteomes:UP000061839};
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:AJT41875.1}.
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 102..103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ SEQUENCE 237 AA; 26041 MW; 881C6B6D81B8E5ED CRC64;
MSRASLEKRP DEVAAMFDDV APKYDLTNDL LSLGQTRRWR RIVVDTVDVR PGQRVLDVAA
GTGTSSEPYA DAGVDVVALD FSLGMLKVGK RRRPDIDFIA GDATALPFAD NTFDATTISF
GLRNVNEPKK AIAEMLRVTK PGGKLVIAEF SHPTFGPFRT VYTEYLMRAL PAIAKRSSSN
PTAYTYLAES IRAWPDQDHL AQWIAEAGWS KVSYRNLNGG TVALHRAYKA EAGTRSS
//