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Database: UniProt
Entry: A0A1I0E7X7_THASX
LinkDB: A0A1I0E7X7_THASX
Original site: A0A1I0E7X7_THASX 
ID   A0A1I0E7X7_THASX        Unreviewed;       260 AA.
AC   A0A1I0E7X7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE {ECO:0000256|HAMAP-Rule:MF_01813};
DE            EC=2.1.1.163 {ECO:0000256|HAMAP-Rule:MF_01813};
DE            EC=2.1.1.201 {ECO:0000256|HAMAP-Rule:MF_01813};
DE   AltName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase {ECO:0000256|HAMAP-Rule:MF_01813};
DE   AltName: Full=Demethylmenaquinone methyltransferase {ECO:0000256|HAMAP-Rule:MF_01813};
GN   Name=ubiE {ECO:0000256|HAMAP-Rule:MF_01813};
GN   ORFNames=SAMN05660429_01763 {ECO:0000313|EMBL:SET41168.1};
OS   Thalassotalea agarivorans (Thalassomonas agarivorans).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=349064 {ECO:0000313|EMBL:SET41168.1, ECO:0000313|Proteomes:UP000199308};
RN   [1] {ECO:0000313|EMBL:SET41168.1, ECO:0000313|Proteomes:UP000199308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19706 {ECO:0000313|EMBL:SET41168.1,
RC   ECO:0000313|Proteomes:UP000199308};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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: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   -!- 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:0000256|HAMAP-Rule:MF_01813};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-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; FOHK01000007; SET41168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0E7X7; -.
DR   STRING; 349064.SAMN05660429_01763; -.
DR   OrthoDB; 9808140at2; -.
DR   UniPathway; UPA00079; UER00169.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000199308; Unassembled WGS sequence.
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   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.
DR   PROSITE; PS01184; UBIE_2; 1.
PE   3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000199308};
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};
KW   Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW   Rule:MF_01813}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         104
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
FT   BINDING         132..133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01813"
SQ   SEQUENCE   260 AA;  28939 MW;  8EA9628BF5F6AC47 CRC64;
     MTSAKDQKPE QSASDSTTHF GFQTVDKGDK ASMVAGVFHS VAKQYDIMND LMSLGIHRLW
     KRFTIDASGV RPGNKVLDLA GGTGDLTAKF SKIVGQEGKV ILADINSSML NVGRDKLRDK
     GLVQNIEYVQ ANAEALPFED NSFDIVTIAF GLRNVTDKDK ALRSIYRVLK PGGRLLVLEF
     SKPEHEILNK VYDFYSFNIL PKMGEFVAKD SESYQYLAES IRMHPDQDTL KAMMDDAGFE
     QTTYHNLTGG IVALHKGFKF
//
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