ID A0A174SX17_9BACE Unreviewed; 245 AA.
AC A0A174SX17;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:CUQ00417.1};
GN Synonyms=menG {ECO:0000256|HAMAP-Rule:MF_01813};
GN ORFNames=DW794_08185 {ECO:0000313|EMBL:RHD49424.1}, ERS852494_02332
GN {ECO:0000313|EMBL:CUP47969.1}, ERS852558_01538
GN {ECO:0000313|EMBL:CUQ00417.1}, F2Y31_07910
GN {ECO:0000313|EMBL:KAA5500355.1}, NXW23_07530
GN {ECO:0000313|EMBL:UVQ98163.1};
OS Bacteroides caccae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=47678 {ECO:0000313|EMBL:CUQ00417.1, ECO:0000313|Proteomes:UP000095725};
RN [1] {ECO:0000313|Proteomes:UP000095657, ECO:0000313|Proteomes:UP000095725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUP47969.1,
RC ECO:0000313|Proteomes:UP000095657}, and 2789STDY5834946
RC {ECO:0000313|EMBL:CUQ00417.1, ECO:0000313|Proteomes:UP000095725};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RHD49424.1, ECO:0000313|Proteomes:UP000284689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM31-16AC {ECO:0000313|EMBL:RHD49424.1,
RC ECO:0000313|Proteomes:UP000284689};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAA5500355.1, ECO:0000313|Proteomes:UP000368418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A19 {ECO:0000313|EMBL:KAA5500355.1,
RC ECO:0000313|Proteomes:UP000368418};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
RN [4] {ECO:0000313|EMBL:UVQ98163.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BFG-474 {ECO:0000313|EMBL:UVQ98163.1};
RA Tisza M.J., Smith D., Dekker J.P.;
RT "Genome Sequencing of Bacteroides fragilis Group Isolates with Nanopore
RT Technology.";
RL Submitted (AUG-2022) 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; CZAI01000005; CUP47969.1; -; Genomic_DNA.
DR EMBL; CZBL01000005; CUQ00417.1; -; Genomic_DNA.
DR EMBL; VVYD01000005; KAA5500355.1; -; Genomic_DNA.
DR EMBL; QSJD01000010; RHD49424.1; -; Genomic_DNA.
DR EMBL; CP103166; UVQ98163.1; -; Genomic_DNA.
DR RefSeq; WP_055172104.1; NZ_VVYD01000005.1.
DR STRING; 47678.ERS852494_02332; -.
DR UniPathway; UPA00079; UER00169.
DR Proteomes; UP000095657; Unassembled WGS sequence.
DR Proteomes; UP000095725; Unassembled WGS sequence.
DR Proteomes; UP000284689; Unassembled WGS sequence.
DR Proteomes; UP000368418; Unassembled WGS sequence.
DR Proteomes; UP001060260; 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; PS01183; UBIE_1; 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:UP000095657};
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:CUQ00417.1}.
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT BINDING 118..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ SEQUENCE 245 AA; 27807 MW; B07727EFE7EC56F5 CRC64;
MDYPQQHIKP YNEEGKKTEQ VERMFDNIAH AYDKLNHTLS LGIDRSWRRK AIAWLRPFHP
QRMMDVATGT GDFAILACRK LQPAELIGTD ISEGMMNVGR EKVKKEGLSD KISFAREDCT
SLSFADNDFD AITVAFGIRN FEDLDKGLSE MCRVLKPGGH LVILELTTPD RFPMKQLFSI
YSKAVIPLLG KLLSKDNSAY RYLPDTIKVF PQGEIMKGVI SRAGFSEVNF RRLTFGICTL
YTATK
//
