ID M1CWB7_SOLTU Unreviewed; 431 AA.
AC M1CWB7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=COQ6 {ECO:0000256|HAMAP-Rule:MF_03193};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400076194, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400076194}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400076194};
RG EnsemblPlants;
RL Submitted (JUN-2015) 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 AlphaFoldDB; M1CWB7; -.
DR STRING; 4113.M1CWB7; -.
DR PaxDb; 4113-PGSC0003DMT400076194; -.
DR EnsemblPlants; PGSC0003DMT400076193; PGSC0003DMT400076193; PGSC0003DMG400029626.
DR EnsemblPlants; PGSC0003DMT400076194; PGSC0003DMT400076194; PGSC0003DMG400029626.
DR Gramene; PGSC0003DMT400076193; PGSC0003DMT400076193; PGSC0003DMG400029626.
DR Gramene; PGSC0003DMT400076194; PGSC0003DMT400076194; PGSC0003DMG400029626.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; M1CWB7; -.
DR OMA; VKQMQVW; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1CWB7; baseline.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
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: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: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:0016120; P:carotene biosynthetic process; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR GO; GO:0016123; P:xanthophyll biosynthetic process; IBA:GO_Central.
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; 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:UP000011115};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03193}.
FT DOMAIN 122..249
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 298..374
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 431 AA; 47200 MW; F186368D5D8F055B CRC64;
MPLTKQLSVA IIDSNPALMN NFHIKKEDPP DPRVSTVTPA TISFFKDMGA WEFVQQHRHA
YFDKMQVWDY TGLGYTRYNA RDVDADVLGC VVENKVLHKS LLSCIQNTDF QKTIHSSRLS
SITFPAMSSV TSSSGTSSSA SGSSAKLELD NGNSMYAKLV VGADGSKSSV RELARIQTTG
WKYSQSAIIC TVEHAVENFC AWQRFLPNGP IALLPIGEKF SNIVWSMDPK EAVDRNSMSE
EDFVKAVNLA LDHGYGPHPR SKSFEGGNVF SWLKADSTSS THEGFEVPPK VTKLASHRMA
FPLSLMHANS YASKRLVLIG DAAHTVHPLA GQGVNMGFAD ALCLSKVIAE GVAVGSDIGE
ITLLQRYESE RKAANITMMA ILDGFQKAYS IDFMPINVLR ALAFNGAQYI SPLKRKIISY
ASGNKLLPLF T
//
