ID A0A3B3DXZ2_ORYME Unreviewed; 510 AA.
AC A0A3B3DXZ2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03193};
DE EC=1.14.13.- {ECO:0000256|HAMAP-Rule:MF_03193};
DE AltName: Full=Coenzyme Q10 monooxygenase 6 {ECO:0000256|HAMAP-Rule:MF_03193};
GN Name=COQ6 {ECO:0000256|HAMAP-Rule:MF_03193};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000034988.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000034988.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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-
CC polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the
CC hydroxylation reaction may be funneled indirectly from NADPH via a
CC ferredoxin/ferredoxin reductase system to COQ6. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03193};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_03193};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|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 ADCK4
CC and COQ7. {ECO:0000256|HAMAP-Rule:MF_03193}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_03193}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03193}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03193}. Golgi
CC apparatus {ECO:0000256|HAMAP-Rule:MF_03193}. Cell projection
CC {ECO:0000256|HAMAP-Rule:MF_03193}. Note=Localizes to cell processes and
CC Golgi apparatus in podocytes. {ECO:0000256|HAMAP-Rule:MF_03193}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family.
CC {ECO:0000256|ARBA:ARBA00005349, ECO:0000256|HAMAP-Rule:MF_03193}.
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DR AlphaFoldDB; A0A3B3DXZ2; -.
DR STRING; 30732.ENSOMEP00000034988; -.
DR PaxDb; 30732-ENSOMEP00000034988; -.
DR Ensembl; ENSOMET00000029498.1; ENSOMEP00000034988.1; ENSOMEG00000021964.1.
DR GeneTree; ENSGT00390000015152; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000261560; Unplaced.
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: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: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; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 NCBIfam; TIGR01989; COQ6; 1.
DR NCBIfam; TIGR01988; Ubi-OHases; 1.
DR PANTHER; PTHR43876; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43876:SF7; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01304; UBIH; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|HAMAP-Rule:MF_03193};
KW FAD {ECO:0000256|HAMAP-Rule:MF_03193};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_03193};
KW Golgi apparatus {ECO:0000256|HAMAP-Rule:MF_03193};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03193};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03193};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|HAMAP-Rule:MF_03193};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_03193};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03193};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03193}.
FT DOMAIN 50..319
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 366..432
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 480..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 56104 MW; 37A0B3AF758949FD CRC64;
MHKITKAQLP LNGLARCFLT EKHLPAVNVV RKRLFCSQNG DDLGKNEVYD VIISGGGMVG
SAMACSLGMD PNLADKKILL LEAGNKKVMD NVPDTYSTRV SSISPGSATL LSGIGAWEHI
TKMRCKPYKR MQVWDGCSDA LITFDKEDLE NEMAYIVEND IVVVSIIRQL DTLSDNVQVK
YRSKVVKYTW PMPHHAADSV PWVRVTLANG ETLQTKLLIG ADGPNSMVRQ ELGIPTVKWN
YDQSAVVAVL HLSEPTENNV AWQRFLPTGP IAMLPLSDTH SSLVWSTSHR LAEELLELDE
ESFVDAINSA FWSSENHSEL IETAGSLFRS ALSAIMPSAG SPRQLPPSVA GIGPKSRVMF
PLGMGHASEY VRHRVALIGD AAHRVHPLAG QGANLGFGDV ACLTQLLSQA AFNGKDLGAI
QHLLEYETER QRQNLPMMAA IDLMKRLYST NVAPVVLLRT FGLQATNMLP TLKVSFPFGP
QPTWTSHPQH RPPVNPKTRP RHDPTLHPLL
//
