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UBIE_SHEHH
ID   UBIE_SHEHH              Reviewed;         251 AA.
AC   B0TJ16;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Shal_3879;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000931; ABZ78419.1; -; Genomic_DNA.
DR   RefSeq; WP_012278936.1; NC_010334.1.
DR   AlphaFoldDB; B0TJ16; -.
DR   SMR; B0TJ16; -.
DR   STRING; 458817.Shal_3879; -.
DR   EnsemblBacteria; ABZ78419; ABZ78419; Shal_3879.
DR   KEGG; shl:Shal_3879; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_037990_0_0_6; -.
DR   OMA; VRNFENL; -.
DR   OrthoDB; 1431378at2; -.
DR   UniPathway; UPA00079; UER00169.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001317; 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: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.
DR   PROSITE; PS01184; UBIE_2; 1.
PE   3: Inferred from homology;
KW   Menaquinone biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; Ubiquinone biosynthesis.
FT   CHAIN           1..251
FT                   /note="Ubiquinone/menaquinone biosynthesis C-
FT                   methyltransferase UbiE"
FT                   /id="PRO_1000088296"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
FT   BINDING         123..124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01813"
SQ   SEQUENCE   251 AA;  27927 MW;  75A8670EC268357D CRC64;
     MSEDTSNSTH FGYKTIEAEK KADLVAGVFH SVAAKYDIMN DVMSFGIHRM WKRFTIESAG
     ARPGMKVLDL AGGTGDLTAK FSRIIGDTGQ VTLADINDSM LKVGREKLRD KGIVGNVNYV
     QANAEALPFP DNHFDIITIA FGLRNVTDKD AAIASMLRVL KPGGKLLVLE FSKPQHDIMR
     KVYDLYSFKV LPKMGSLITK DADSYEYLAE SIRMHPDQDT LKQMMEDAGF EQVNYTNMTD
     GIVALHKGYK F
 
 
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