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Database: UniProt
Entry: A0A0Q0HYL3_9GAMM
LinkDB: A0A0Q0HYL3_9GAMM
Original site: A0A0Q0HYL3_9GAMM 
ID   A0A0Q0HYL3_9GAMM        Unreviewed;       236 AA.
AC   A0A0Q0HYL3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-MAY-2019, entry version 19.
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_2 {ECO:0000313|EMBL:KPZ53455.1};
GN   Synonyms=ubiG {ECO:0000256|HAMAP-Rule:MF_00472};
GN   ORFNames=AN393_02812 {ECO:0000313|EMBL:KPZ53455.1};
OS   Pseudoalteromonas sp. P1-25.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1723758 {ECO:0000313|EMBL:KPZ53455.1, ECO:0000313|Proteomes:UP000050552};
RN   [1] {ECO:0000313|EMBL:KPZ53455.1, ECO:0000313|Proteomes:UP000050552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-25 {ECO:0000313|EMBL:KPZ53455.1,
RC   ECO:0000313|Proteomes:UP000050552};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPZ53455.1}.
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DR   EMBL; LKDW01000023; KPZ53455.1; -; Genomic_DNA.
DR   RefSeq; WP_055016061.1; NZ_LKDW01000023.1.
DR   EnsemblBacteria; KPZ53455; KPZ53455; AN393_02812.
DR   PATRIC; fig|1723758.3.peg.2869; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000050552; 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:UP000050552};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00448101, ECO:0000313|EMBL:KPZ53455.1};
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:KPZ53455.1};
KW   Ubiquinone {ECO:0000313|EMBL:KPZ53455.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00472,
KW   ECO:0000256|SAAS:SAAS00063552}.
FT   BINDING      39     39       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING      59     59       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00472}.
FT   BINDING      80     80       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00472}.
FT   BINDING     124    124       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00472}.
SQ   SEQUENCE   236 AA;  26088 MW;  F2AB95E2C215528D CRC64;
     MTEHQNVDNA EIAKFEAIAE RWWDQDGEFK PLHEINPLRL DFVANKSQGL FEKETLDVGC
     GGGILSESMA RMGANVTGID MGQEPLTVAK LHSLETGVNV DYIKVPAEEF ANQYPARFDV
     ITCMEMLEHV PDPASIIRAV AKLAKPGADV FFSTLNKTPK AYLFAIVGAE KLLKMVPEGT
     HDHNKFIKPA QLIAWAEQAG LKVRASAGLS YNPLSKQYSL NTDVSVNYIL HFEKLA
//
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