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Entry: A0A078LP78_9PSED
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ID   A0A078LP78_9PSED        Unreviewed;       232 AA.
AC   A0A078LP78;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-MAY-2019, entry version 26.
DE   RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472};
DE   AltName: Full=2-polyprenyl-6-hydroxyphenol methylase {ECO:0000256|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.222 {ECO:0000256|HAMAP-Rule:MF_00472};
DE   AltName: Full=3-demethylubiquinone 3-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472};
DE            EC=2.1.1.64 {ECO:0000256|HAMAP-Rule:MF_00472};
GN   Name=ubiG_1 {ECO:0000313|EMBL:CDZ93140.1};
GN   Synonyms=ubiG {ECO:0000256|HAMAP-Rule:MF_00472,
GN   ECO:0000313|EMBL:RRV18209.1};
GN   ORFNames=BN1079_00420 {ECO:0000313|EMBL:CDZ93140.1}, EGJ00_02470
GN   {ECO:0000313|EMBL:RRV18209.1};
OS   Pseudomonas saudiphocaensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ93140.1, ECO:0000313|Proteomes:UP000053902};
RN   [1] {ECO:0000313|EMBL:CDZ93140.1, ECO:0000313|Proteomes:UP000053902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20_BN {ECO:0000313|EMBL:CDZ93140.1,
RC   ECO:0000313|Proteomes:UP000053902};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RRV18209.1, ECO:0000313|Proteomes:UP000271179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS_399 {ECO:0000313|EMBL:RRV18209.1,
RC   ECO:0000313|Proteomes:UP000271179};
RA   D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S.,
RA   Gul D., Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT   "Transmission dynamics of multidrug resistant bacteria on intensive
RT   care unit surfaces.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation
CC       steps in the ubiquinone biosynthetic pathway. {ECO:0000256|HAMAP-
CC       Rule:MF_00472, ECO:0000256|SAAS:SAAS00561163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-
CC         L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+)
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31411, Rhea:RHEA-
CC         COMP:9550, Rhea:RHEA-COMP:9551, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:62729,
CC         ChEBI:CHEBI:62731; EC=2.1.1.222; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00472, ECO:0000256|SAAS:SAAS01122591};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a
CC         ubiquinol + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:44380, Rhea:RHEA-COMP:9566, Rhea:RHEA-COMP:10914,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17976, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:84422; EC=2.1.1.64;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00472,
CC         ECO:0000256|SAAS:SAAS01122587};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00472, ECO:0000256|SAAS:SAAS00063519}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       UbiG/COQ3 family. {ECO:0000256|HAMAP-Rule:MF_00472,
CC       ECO:0000256|SAAS:SAAS01087951}.
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DR   EMBL; CCSF01000001; CDZ93140.1; -; Genomic_DNA.
DR   EMBL; RHQU01000001; RRV18209.1; -; Genomic_DNA.
DR   RefSeq; WP_037021963.1; NZ_RHQU01000001.1.
DR   STRING; 1499686.BN1079_00420; -.
DR   EnsemblBacteria; CDZ93140; CDZ93140; BN1079_00420.
DR   OrthoDB; 1515497at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000053902; Unassembled WGS sequence.
DR   Proteomes; UP000271179; Unassembled WGS sequence.
DR   GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00472; UbiG; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR010233; UbiG_MeTrfase.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR01983; UbiG; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000053902,
KW   ECO:0000313|Proteomes:UP000271179};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00448101, ECO:0000313|EMBL:CDZ93140.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053902};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00448117};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00448111, ECO:0000313|EMBL:CDZ93140.1};
KW   Ubiquinone {ECO:0000313|EMBL:CDZ93140.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00063552}.
FT   BINDING      36     36       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING      55     55       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00472}.
FT   BINDING      76     76       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING     120    120       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00472}.
SQ   SEQUENCE   232 AA;  25887 MW;  75507B84F32838F4 CRC64;
     MSNVDHAEIA KFEALAHRWW DRESEFKPLH DINPLRVNWI DERASLAGKK VLDVGCGGGI
     LSEAMAQRGA TVTGIDMGEA PLSVARLHLL ESGLEVDYRQ ITAEALALEC PEQFDVVTCL
     EMLEHVPDPA SIIRACYKMV KPGGQVFFST INRNPKAYAL AIIGAEYVLK MLPRGTHDYR
     KFIRPSELGA WSRDAGLAVR DIVGLTYNPL TKDYKLSQDV DVNYMLQTLR EA
//
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