(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWU0_RUEPO

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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
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
//

If you have problems or comments...

PBIL Back to PBIL home page