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ID Q5LWU0_RUEPO Unreviewed; 257 AA.
AC Q5LWU0;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 08-MAY-2019, entry version 102.
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 ECO:0000313|EMBL:AAV93473.1};
GN OrderedLocusNames=SPO0145 {ECO:0000313|EMBL:AAV93473.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS (Silicibacter pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93473.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV93473.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT marine environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV93473.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
CC -!- FUNCTION: Methyltransferase required for the conversion of
CC demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion
CC of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-
CC polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
CC {ECO:0000256|HAMAP-Rule:MF_01813}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-demethylmenaquinol + S-adenosyl-L-methionine = a
CC menaquinol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42640, Rhea:RHEA-COMP:9539, Rhea:RHEA-COMP:9563,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18151, ChEBI:CHEBI:55437,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.163;
CC Evidence={ECO:0000256|HAMAP-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-
CC polyprenyl-1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-
CC COMP:10859, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:84166, ChEBI:CHEBI:84167;
CC EC=2.1.1.201; 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
CC methyltransferase superfamily. MenG/UbiE family.
CC {ECO:0000256|HAMAP-Rule:MF_01813, ECO:0000256|SAAS:SAAS00572359}.
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DR EMBL; CP000031; AAV93473.1; -; Genomic_DNA.
DR STRING; 246200.SPO0145; -.
DR EnsemblBacteria; AAV93473; AAV93473; SPO0145.
DR KEGG; sil:SPO0145; -.
DR eggNOG; ENOG4105DDZ; Bacteria.
DR eggNOG; COG2226; LUCA.
DR HOGENOM; HOG000249463; -.
DR KO; K03183; -.
DR OMA; VRNFENL; -.
DR UniPathway; UPA00079; UER00169.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001023; Chromosome.
DR GO; GO:0043333; F:2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity; IEA:UniProtKB-EC.
DR GO; GO:0102955; F:S-adenosylmethionine:2-demethylmenaquinol-7 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:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1.
DR InterPro; IPR029063; SAM-dependent_MTases.
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;
DR PRODOM; Q5LWU0.
DR SWISS-2DPAGE; Q5LWU0.
KW Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01813};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01813,
KW ECO:0000256|SAAS:SAAS00092033, ECO:0000313|EMBL:AAV93473.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01813,
KW ECO:0000256|SAAS:SAAS00463460};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01813,
KW ECO:0000256|SAAS:SAAS00463451, ECO:0000313|EMBL:AAV93473.1};
KW Ubiquinone {ECO:0000313|EMBL:AAV93473.1};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01813}.
FT REGION 129 130 S-adenosyl-L-methionine binding.
FT {ECO:0000256|HAMAP-Rule:MF_01813}.
FT BINDING 81 81 S-adenosyl-L-methionine.
FT {ECO:0000256|HAMAP-Rule:MF_01813}.
FT BINDING 101 101 S-adenosyl-L-methionine.
FT {ECO:0000256|HAMAP-Rule:MF_01813}.
FT BINDING 146 146 S-adenosyl-L-methionine.
FT {ECO:0000256|HAMAP-Rule:MF_01813}.
SQ SEQUENCE 257 AA; 28773 MW; 90B3AB97327AB5DD CRC64;
MRGTARPMSD RSDKTTHFGF ETVPEHEKAG RVQGVFGSVA SKYDVMNDVM SMGIHRVWKD
AMMDWLAPRP GQRLLDVAGG TGDISFRFLK RAGHGHATVL DLTEPMLVEG RKRAEAERMA
DSLDWVVGDA MALPFEDNTF DVYTISFGIR NVTRPQEALN EAYRVLRPGG RLMVLEFSQL
PNDGLQKLYD LYSFNVIPRM GQLIANDSAS YQYLVESIRN FPNQETFLGM VQAAGFGNAK
YRNLSMGIAA LHSGWKI
//
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