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COQ6_BOVIN
ID   COQ6_BOVIN              Reviewed;         469 AA.
AC   Q2KIL4; F1MQ68;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03193};
DE            EC=1.14.13.- {ECO:0000255|HAMAP-Rule:MF_03193};
DE   AltName: Full=Coenzyme Q10 monooxygenase 6 {ECO:0000255|HAMAP-Rule:MF_03193};
DE   Flags: Precursor;
GN   Name=COQ6 {ECO:0000255|HAMAP-Rule:MF_03193};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: FAD-dependent monooxygenase required for the C5-ring
CC       hydroxylation during ubiquinone biosynthesis. Catalyzes the
CC       hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-
CC       4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation
CC       reaction may be funneled indirectly from NADPH via a
CC       ferredoxin/ferredoxin reductase system to COQ6. {ECO:0000255|HAMAP-
CC       Rule:MF_03193}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2
CC         reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-
CC         hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:20361, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58373,
CC         ChEBI:CHEBI:84492; Evidence={ECO:0000255|HAMAP-Rule:MF_03193};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03193};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03193}.
CC   -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC       at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Interacts with COQ8B
CC       and COQ7. {ECO:0000255|HAMAP-Rule:MF_03193}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03193}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03193}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03193}. Golgi
CC       apparatus {ECO:0000255|HAMAP-Rule:MF_03193}. Cell projection
CC       {ECO:0000255|HAMAP-Rule:MF_03193}. Note=Localizes to cell processes and
CC       Golgi apparatus in podocytes. {ECO:0000255|HAMAP-Rule:MF_03193}.
CC   -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03193}.
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DR   EMBL; DAAA02029604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC112594; AAI12595.1; -; mRNA.
DR   RefSeq; NP_001039558.1; NM_001046093.2.
DR   AlphaFoldDB; Q2KIL4; -.
DR   SMR; Q2KIL4; -.
DR   STRING; 9913.ENSBTAP00000027093; -.
DR   PaxDb; Q2KIL4; -.
DR   PRIDE; Q2KIL4; -.
DR   Ensembl; ENSBTAT00000027093; ENSBTAP00000027093; ENSBTAG00000020331.
DR   GeneID; 511624; -.
DR   KEGG; bta:511624; -.
DR   CTD; 51004; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020331; -.
DR   VGNC; VGNC:27614; COQ6.
DR   eggNOG; KOG3855; Eukaryota.
DR   GeneTree; ENSGT00390000015152; -.
DR   HOGENOM; CLU_009665_8_0_1; -.
DR   InParanoid; Q2KIL4; -.
DR   OMA; SDVACII; -.
DR   OrthoDB; 655400at2759; -.
DR   TreeFam; TF105772; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000020331; Expressed in metanephros cortex and 106 other tissues.
DR   ExpressionAtlas; Q2KIL4; baseline and differential.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; IEA:InterPro.
DR   GO; GO:0106364; F:4-hydroxy-3-all-trans-hexaprenylbenzoate oxygenase activity; IEA:RHEA.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_03193; COQ6_monooxygenase; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018168; Ubi_Hdrlase_CS.
DR   InterPro; IPR010971; UbiH/COQ6.
DR   InterPro; IPR000689; UbQ_mOase_COQ6.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01989; COQ6; 1.
DR   TIGRFAMs; TIGR01988; Ubi-OHases; 1.
DR   PROSITE; PS01304; UBIH; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; FAD; Flavoprotein; Golgi apparatus; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transit peptide; Ubiquinone biosynthesis.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..469
FT                   /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT                   mitochondrial"
FT                   /id="PRO_0000328199"
FT   CONFLICT        457
FT                   /note="S -> Y (in Ref. 2; AAI12595)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   469 AA;  51072 MW;  02054598703A9862 CRC64;
     MAAQLARVRW GTVFAAAQKG PRVSCRRWAG ASADNVYDVV VSGGGLVGAA MACALGHDIH
     FCDKKILLLE AGPKKVLEKL PETYSNRVSS ISPGSATLLS SFGAWDHICN MRCRAFRRMQ
     VWDACSEALI MFDKDNLDDM GYIVENDVIM HALTKQLEAV SDQVTVLYKS KAVSYTWPYP
     FSMADSSPWV HITLGDGRTL QTKLLIGADG HNSGVRQAAG IRNVSWNYDQ SAVVATLHLS
     EATENNVAWQ RFLPSGPIAL LPLSDTLSSL VWSTSHEHAA ELVSMEEEEF VDAINSAFWS
     DVNHTDFIDS AGSMLQSAVA FLKPTRVSAR QLPPSVARVD AKSRVLFPLG LGHAAEYVRP
     RLALIGDAAH RVHPLAGQGV NMGFGDISSL LHHLSTAAFN GKDLGSMSHL TSYETDRQRH
     NTALLAATDL LKRLYSTRAT LVVLLRTWGL QATNAVSPLK EQIMAFASK
 
 
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