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UBIE_BURMA
ID   UBIE_BURMA              Reviewed;         243 AA.
AC   Q62MP4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE {ECO:0000255|HAMAP-Rule:MF_01813};
DE            EC=2.1.1.163 {ECO:0000255|HAMAP-Rule:MF_01813};
DE            EC=2.1.1.201 {ECO:0000255|HAMAP-Rule:MF_01813};
DE   AltName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase {ECO:0000255|HAMAP-Rule:MF_01813};
DE   AltName: Full=Demethylmenaquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01813};
GN   Name=ubiE {ECO:0000255|HAMAP-Rule:MF_01813}; OrderedLocusNames=BMA0186;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
CC   -!- FUNCTION: Methyltransferase required for the conversion of
CC       demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of
CC       2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-
CC       methyl-6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|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:0000255|HAMAP-
CC         Rule:MF_01813};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S-
CC         adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl-
CC         1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01813};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis;
CC       menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01813}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01813}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. MenG/UbiE family. {ECO:0000255|HAMAP-Rule:MF_01813}.
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DR   EMBL; CP000010; AAU49007.1; -; Genomic_DNA.
DR   RefSeq; WP_004189973.1; NC_006348.1.
DR   RefSeq; YP_102024.1; NC_006348.1.
DR   AlphaFoldDB; Q62MP4; -.
DR   SMR; Q62MP4; -.
DR   STRING; 243160.BMA0186; -.
DR   EnsemblBacteria; AAU49007; AAU49007; BMA0186.
DR   GeneID; 56527152; -.
DR   KEGG; bma:BMA0186; -.
DR   PATRIC; fig|243160.12.peg.184; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_037990_0_0_4; -.
DR   OMA; VRNFENL; -.
DR   UniPathway; UPA00079; UER00169.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000006693; Chromosome 1.
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:0009060; P:aerobic respiration; IEA:UniProtKB-UniRule.
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   Gene3D; 3.40.50.150; -; 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   Pfam; PF01209; Ubie_methyltran; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1.
DR   PROSITE; PS51608; SAM_MT_UBIE; 1.
DR   PROSITE; PS01183; UBIE_1; 1.
PE   3: Inferred from homology;
KW   Menaquinone biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; Ubiquinone biosynthesis.
FT   CHAIN           1..243
FT                   /note="Ubiquinone/menaquinone biosynthesis C-
FT                   methyltransferase UbiE"
FT                   /id="PRO_0000193258"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT   BINDING         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT   BINDING         116..117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
SQ   SEQUENCE   243 AA;  26955 MW;  ACE84431CF68A06D CRC64;
     MSKTHFGFET VEENEKAKKV AGVFHSVASN YDLMNDLMSA GLHRAWKAFT IAQANVRPGG
     KVLDIAAGTG DLTKAFAKAA GPTGEVWHTD INESMLRVGR DRLLDKGVVT PSLLCDAEKL
     PFPDNYFDVV TVAFGLRNMT HKDSALAEMR RVAKPGGRVM VLEFSKVWEP LKKAYDVYSF
     KVLPWLGDKF AKDADSYRYL AESIRMHPDQ ETLKTMMEQA GLDAVKYYNL SGGVVALHVG
     TKY
 
 
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