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Entry: A4HN95_LEIBR
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ID   A4HN95_LEIBR            Unreviewed;       291 AA.
AC   A4HN95;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
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=LBRM_34_4230 {ECO:0000313|EMBL:CAM43640.1};
OS   Leishmania braziliensis.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Leishmaniinae; Leishmania; Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660 {ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM43640.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43640.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.-A., Carver T., Norbertczak H.,
RA   Chillingworth T., Hance Z., Jagels K., Moule S., Ormond D., Rutter S.,
RA   Sqaures R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B.,
RA   Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D.,
RA   Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O.,
RA   Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM43640.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM43640.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural
RT   change between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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; FR799009; CAM43640.1; -; Genomic_DNA.
DR   RefSeq; XP_001568525.1; XM_001568475.1.
DR   EnsemblProtists; CAM43640; CAM43640; LBRM_34_4230.
DR   GeneDB; LbrM.34.4230:pep; -.
DR   GeneID; 5419483; -.
DR   KEGG; lbz:LBRM_34_4230; -.
DR   EuPathDB; TriTrypDB:LbrM.34.4230; -.
DR   eggNOG; KOG1270; Eukaryota.
DR   eggNOG; COG2227; LUCA.
DR   InParanoid; A4HN95; -.
DR   KO; K00568; -.
DR   OMA; GTHDYAK; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000007258; Chromosome 35.
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:UP000007258};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03190,
KW   ECO:0000313|EMBL:CAM43640.1};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007258};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03190};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03190,
KW   ECO:0000313|EMBL:CAM43640.1};
KW   Ubiquinone {ECO:0000313|EMBL:CAM43640.1};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   BINDING      36     36       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   BINDING      77     77       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03190}.
FT   BINDING      98     98       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03190}.
FT   BINDING     155    155       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03190}.
SQ   SEQUENCE   291 AA;  31747 MW;  D16541315D52208D CRC64;
     MKGVAADEVA KFAALQKHWW DPTGPLRSLH LLNPIRVSYV NDIVRSYAKA GGSLTDASIG
     LLGSHGITPQ HQILDVGCGG GILAESLARI GGTVTGIDAC AESIEVAEKR RQEMAANFGA
     SSSPSNWSQR LSYRHVSLFD IVEQEKQQFD IVVASEVIEH VSDARAFLQA LCEATRPGGL
     LFLSTIDKSL TTAIVYIGVA EMLTGFVEPG THDWRKFIPP DDVTAFAQRF SVRKVDQHYI
     VTYPDFFQSA VSGDFQVNFC LSNSVNTGHY FWAGRKSPQT EEKRATMPPG G
//
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