ID E8QMP4_HELPR Unreviewed; 246 AA.
AC E8QMP4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:ADU83861.1};
GN Synonyms=menG {ECO:0000256|HAMAP-Rule:MF_01813};
GN OrderedLocusNames=HPLT_07380 {ECO:0000313|EMBL:ADU83861.1};
OS Helicobacter pylori (strain Lithuania75).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=907237 {ECO:0000313|EMBL:ADU83861.1, ECO:0000313|Proteomes:UP000007466};
RN [1] {ECO:0000313|Proteomes:UP000007466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lithuania75 {ECO:0000313|Proteomes:UP000007466};
RA Kersulyte D., Kupcinskas L., Chalkauskas H., Kiuduliene L., Janulaitis A.,
RA Berg D.E.;
RT "Genome sequence of Helicobacter pylori strain Lithuania75.";
RL Submitted (NOV-2010) 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; CP002334; ADU83861.1; -; Genomic_DNA.
DR RefSeq; WP_000711698.1; NC_017362.1.
DR AlphaFoldDB; E8QMP4; -.
DR KEGG; hph:HPLT_07380; -.
DR PATRIC; fig|907237.3.peg.1477; -.
DR HOGENOM; CLU_037990_0_0_7; -.
DR UniPathway; UPA00079; UER00169.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000007466; Chromosome.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
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:UniProtKB-UniPathway.
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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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}; Ubiquinone {ECO:0000313|EMBL:ADU83861.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688}.
FT COILED 96..123
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 65
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"
SQ SEQUENCE 246 AA; 27811 MW; 5D7E3C00ABD3E341 CRC64;
MKKEKHLKQE KIINMFDDIA SSYDQANRLM SFGLDVKWRE RACEHAFLFL ENKKALRLVD
VACGTGDMLV AWQKSALNCG IEFKECLGID PSNNMLELAI KKCEELENKI SFIQAQAKDL
KGVGNSSVDI LSIAYGLRNI VERQEALKEF FRVLKPRGVL VILEFLKKDN PTWLDKISGF
YTNKVLPLVG GAISKNYGAY SYLPQSIEGF LSLEGLKFEL KNAGFEILRT EDSIAQISTT
MLVRKS
//
