ID A0A150H8X9_9MICO Unreviewed; 235 AA.
AC A0A150H8X9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ubiE {ECO:0000313|EMBL:KXZ58552.1};
GN Synonyms=menG {ECO:0000256|HAMAP-Rule:MF_01813};
GN ORFNames=Bravens_01601 {ECO:0000313|EMBL:KXZ58552.1}, CYJ40_02365
GN {ECO:0000313|EMBL:PKY70920.1};
OS Brevibacterium ravenspurgense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=479117 {ECO:0000313|EMBL:KXZ58552.1, ECO:0000313|Proteomes:UP000243589};
RN [1] {ECO:0000313|EMBL:KXZ58552.1, ECO:0000313|Proteomes:UP000243589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG56047 {ECO:0000313|EMBL:KXZ58552.1,
RC ECO:0000313|Proteomes:UP000243589};
RA Bernier A.-M., Burdz T., Huynh C., Pachecho A.L., Wiebe D., Bonner C.,
RA Bernard K.;
RT "Use of Whole Genome Sequencing to ascertain that Brevibacterium
RT massiliense (Roux, Raoult 2009) is a later heterotypic synonym of
RT Brevibacterium ravenspurgense (Mages 2008).";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKY70920.1, ECO:0000313|Proteomes:UP000242755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0426 {ECO:0000313|EMBL:PKY70920.1,
RC ECO:0000313|Proteomes:UP000242755};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) 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}.
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:KXZ58552.1}.
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DR EMBL; LQQC01000010; KXZ58552.1; -; Genomic_DNA.
DR EMBL; PKGO01000002; PKY70920.1; -; Genomic_DNA.
DR RefSeq; WP_062022121.1; NZ_PKGO01000002.1.
DR AlphaFoldDB; A0A150H8X9; -.
DR STRING; 1176165.GCA_001584405_00243; -.
DR PATRIC; fig|479117.4.peg.1588; -.
DR UniPathway; UPA00079; UER00169.
DR Proteomes; UP000242755; Unassembled WGS sequence.
DR Proteomes; UP000243589; Unassembled WGS sequence.
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:UP000243589};
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:KXZ58552.1}.
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"
SQ SEQUENCE 235 AA; 26081 MW; 4BB68E85CF3E3E5E CRC64;
MNRAHLDKNK ADVASMFDAV AERYDITNDA MTFGISRWWR VEITRSVDPK PGELILDLAA
GTGSSSVPYA QRGATVIAGD ISEGMLAVGR RRHPEIQFQY ADATDLDFDD NTFDVVTITY
GFRNVQEPQK ALKEMLRVLK PGGRLVIAEF STPTFTPFAR FYKEYIMRAL PAVAKAVSSN
PEAYVYLAES IRAWPAQLPL AHMIRDAGFD QVKYRNLTGG IVAIHHALKP SGDAL
//