ID E0W075_PEDHC Unreviewed; 458 AA.
AC E0W075;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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};
GN Name=8240379 {ECO:0000313|EnsemblMetazoa:PHUM546620-PA};
GN Synonyms=coq6 {ECO:0000256|HAMAP-Rule:MF_03193};
GN ORFNames=Phum_PHUM546620 {ECO:0000313|EMBL:EEB19031.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB19031.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB19031.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB19031.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB19031.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM546620-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM546620-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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.
CC {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}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family.
CC {ECO:0000256|ARBA:ARBA00005349, ECO:0000256|HAMAP-Rule:MF_03193}.
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DR EMBL; AAZO01006645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235857; EEB19031.1; -; Genomic_DNA.
DR RefSeq; XP_002431769.1; XM_002431724.1.
DR AlphaFoldDB; E0W075; -.
DR STRING; 121224.E0W075; -.
DR EnsemblMetazoa; PHUM546620-RA; PHUM546620-PA; PHUM546620.
DR GeneID; 8240379; -.
DR KEGG; phu:Phum_PHUM546620; -.
DR CTD; 8240379; -.
DR VEuPathDB; VectorBase:PHUM546620; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; E0W075; -.
DR OMA; VKQMQVW; -.
DR OrthoDB; 5473786at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000009046; Unassembled WGS sequence.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; IEA:InterPro.
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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:UniProtKB-UniRule.
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 FAD {ECO:0000256|HAMAP-Rule:MF_03193};
KW Flavoprotein {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}; Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW Ubiquinone {ECO:0000313|EMBL:EEB19031.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03193}.
FT DOMAIN 80..291
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 352..412
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 458 AA; 50877 MW; 90BC7E1D7E7CFB7B CRC64;
MGNKSILMFN KINRQPGKRF VKNLLDFSIR ENHYDIAIAG GGLVGTSMAC AVGKNSKLSE
SKVILFESAS QKSFKKKAKD DEYSNRVVSI NPGSKKFLEN IGAWKFISDL RYKTVKKLQV
WDACSDALIT FNDDLMKDVS YIVENDLILN ALEEVCSNLK NVTVKYESRI KKIVPPSDKN
KMVHLEMENG DEYTCNLLVG ADGFKSKTRE VIGGQYLSWN YDQKGIVATV KLSEPTENVV
AWQRFLPTGP IALLPLTNEL SSLVWSTETK KAEQLLGMNE ETFKDSLNDA FWKSYPKNEL
VSSATASLDK MLSSLTLKSF GSHQLPPSVS SIVPGSRAAF PLGFGHSIKY YRPGIVLVGD
AAHRIHPLAG QGVNLGFGDV ELLTNKLGDS VYNGNKIGCS RVLADYESER QREILPMLIT
TDFLQKLYST SFAPVVLVRS LGLQITNALH PLKVRFLQ
//
