COQ7_BOVIN
ID COQ7_BOVIN Reviewed; 217 AA.
AC Q2TBW2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=5-demethoxyubiquinone hydroxylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03194};
DE Short=DMQ hydroxylase {ECO:0000255|HAMAP-Rule:MF_03194};
DE EC=1.14.99.60 {ECO:0000255|HAMAP-Rule:MF_03194};
DE AltName: Full=Timing protein clk-1 homolog {ECO:0000255|HAMAP-Rule:MF_03194};
DE AltName: Full=Ubiquinone biosynthesis monooxygenase COQ7 {ECO:0000255|HAMAP-Rule:MF_03194};
DE Flags: Precursor;
GN Name=COQ7 {ECO:0000255|HAMAP-Rule:MF_03194};
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 MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has
CC also a structural role in the COQ enzyme complex, stabilizing other COQ
CC polypeptides. Involved in lifespan determination in a ubiquinone-
CC independent manner. Plays a role in modulating mitochondrial stress
CC responses, acting in the nucleus, perhaps via regulating gene
CC expression, independent of its characterized mitochondrial function in
CC ubiquinone biosynthesis (By similarity). {ECO:0000250|UniProtKB:Q99807,
CC ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol +
CC AH2 + O2 = A + a 3-demethylubiquinol + H2O; Xref=Rhea:RHEA:50908,
CC Rhea:RHEA-COMP:10859, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:84167, ChEBI:CHEBI:84422; EC=1.14.99.60;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03194};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03194};
CC Note=Binds 2 iron ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03194};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03194}.
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 COQ6. Interacts with COQ9. {ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03194}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03194}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_03194}.
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DR EMBL; BC109578; AAI09579.1; -; mRNA.
DR RefSeq; NP_001106712.1; NM_001113241.1.
DR AlphaFoldDB; Q2TBW2; -.
DR SMR; Q2TBW2; -.
DR STRING; 9913.ENSBTAP00000043418; -.
DR PaxDb; Q2TBW2; -.
DR GeneID; 504771; -.
DR KEGG; bta:504771; -.
DR CTD; 10229; -.
DR eggNOG; KOG4061; Eukaryota.
DR InParanoid; Q2TBW2; -.
DR OrthoDB; 1242061at2759; -.
DR TreeFam; TF314559; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008682; F:3-demethoxyubiquinol 3-hydroxylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UniProtKB-UniRule.
DR GO; GO:0008340; P:determination of adult lifespan; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR CDD; cd01042; DMQH; 1.
DR HAMAP; MF_01658; COQ7; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR011566; Ubq_synth_Coq7.
DR PANTHER; PTHR11237; PTHR11237; 1.
DR Pfam; PF03232; COQ7; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 2: Evidence at transcript level;
KW Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Reference proteome; Repeat; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT CHAIN 35..217
FT /note="5-demethoxyubiquinone hydroxylase, mitochondrial"
FT /id="PRO_0000252363"
FT REPEAT 48..129
FT /note="1"
FT REPEAT 130..217
FT /note="2"
FT REGION 48..217
FT /note="2 X approximate tandem repeats"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 93
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
SQ SEQUENCE 217 AA; 24361 MW; 722E4A141731D1CD CRC64;
MSCARALAAC CLWRLRTGAL QPLSAYGRRI SVRFCSSGMT LDNINREAVD RIIRVDHAGE
YGANRIYAGQ MAVLGRTSIG PVIQKMWDQE KDHLKKFNEL MVAFRVRPTV LMPFWNVVGF
ALGAGTALLG KEGAMACTVA VEESIAHHYN NQIRTLMEKE PEKYEELLQV IKKFRDEELE
HHDIGLEHDA ELAPAYVVLK SVIQAGCKVA IYLSERL
