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Database: UniProt
Entry: A0A183TL64_SCHSO
LinkDB: A0A183TL64_SCHSO
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ID   A0A183TL64_SCHSO        Unreviewed;       282 AA.
AC   A0A183TL64;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-JUL-2019, entry version 14.
DE   RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03190};
DE   AltName: Full=3-demethylubiquinol 3-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190};
DE            EC=2.1.1.64 {ECO:0000256|HAMAP-Rule:MF_03190};
DE   AltName: Full=Polyprenyldihydroxybenzoate methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190};
DE            EC=2.1.1.114 {ECO:0000256|HAMAP-Rule:MF_03190};
GN   ORFNames=SSLN_LOCUS17212 {ECO:0000313|EMBL:VDM03598.1};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda;
OC   Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001786501-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0001786501-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SSLN_0001786501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDM03598.1, ECO:0000313|Proteomes:UP000275846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NST_G2 {ECO:0000313|EMBL:VDM03598.1,
RC   ECO:0000313|Proteomes:UP000275846};
RG   Pathogen Informatics;
RL   Submitted (NOV-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_03190}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-
CC         adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-
CC         polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:44452, Rhea:RHEA-COMP:10930, Rhea:RHEA-
CC         COMP:10931, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:64694, ChEBI:CHEBI:84443;
CC         EC=2.1.1.114; Evidence={ECO:0000256|HAMAP-Rule:MF_03190};
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_03190};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_03190}.
CC   -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex.
CC       {ECO:0000256|HAMAP-Rule:MF_03190}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03190}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000256|HAMAP-
CC       Rule:MF_03190}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. UbiG/COQ3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_03190}.
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DR   EMBL; UYSU01042146; VDM03598.1; -; Genomic_DNA.
DR   WBParaSite; SSLN_0001786501-mRNA-1; SSLN_0001786501-mRNA-1; SSLN_0001786501.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000050788; Genome assembly.
DR   Proteomes; UP000275846; Unassembled WGS sequence.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR   GO; GO:1990886; F:3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004395; F:hexaprenyldihydroxybenzoate 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:UP000050788,
KW   ECO:0000313|Proteomes:UP000275846};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275846};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   BINDING      33     33       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   BINDING      61     61       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03190}.
FT   BINDING      82     82       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   BINDING     135    135       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03190}.
SQ   SEQUENCE   282 AA;  31477 MW;  620B7DE25AE89142 CRC64;
     MDSEEVATFQ KIAQKWWDPD GPMGALHSMN SLRITMITEA LKSSSSTEHF PLYGKRILDV
     GCGGGILSEP LALLGASVWG IDLIPEGIEV AKRHASTQAT HRWSATPFGA PEYSCCSVAD
     VASENPGQFD ALVASEVLEH VSDWENLIKD ASICLKPGGS FFVTTLNKTV PSYLLAILLA
     ERLFGLVPLG THSWNKFINP DRLRLAAIRC KSLCWPEFQF IHYTLMAWTL LLDLSIKYYF
     PFVDNLQPRK LLGMSYNPLI DRWTWTPSLA VNYAFHAVKE IN
//
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