COQ6_DICDI
ID COQ6_DICDI Reviewed; 495 AA.
AC Q54EN1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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};
GN Name=coq6 {ECO:0000255|HAMAP-Rule:MF_03193}; ORFNames=DDB_G0291440;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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.
CC {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}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03193}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000255|HAMAP-
CC Rule:MF_03193}.
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DR EMBL; AAFI02000177; EAL61704.1; -; Genomic_DNA.
DR RefSeq; XP_635209.1; XM_630117.1.
DR AlphaFoldDB; Q54EN1; -.
DR SMR; Q54EN1; -.
DR STRING; 44689.DDB0231594; -.
DR PaxDb; Q54EN1; -.
DR PRIDE; Q54EN1; -.
DR EnsemblProtists; EAL61704; EAL61704; DDB_G0291440.
DR GeneID; 8628154; -.
DR KEGG; ddi:DDB_G0291440; -.
DR dictyBase; DDB_G0291440; coq6.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; Q54EN1; -.
DR OMA; SDVACII; -.
DR PhylomeDB; Q54EN1; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q54EN1; -.
DR Proteomes; UP000002195; Chromosome 6.
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: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: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; IPR010971; UbiH/COQ6.
DR InterPro; IPR000689; UbQ_mOase_COQ6.
DR Pfam; PF01494; FAD_binding_3; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01988; Ubi-OHases; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Reference proteome; Ubiquinone biosynthesis.
FT CHAIN 1..495
FT /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT mitochondrial"
FT /id="PRO_0000328200"
SQ SEQUENCE 495 AA; 55086 MW; BB7A599E401D24C5 CRC64;
MLRLINKTIN KNDLIKINNS KRFCSTTTNS TINKDNIYDI IIIGGGLVGS TMACSIGNNN
TTKHLKVALI ESSKIQTVEQ SISNAIPEIR TISFNNQTIE LFKSINVWDT IKSTKRVNPF
NQVRVWDTSG FEGIHFQDND IIDDGNNTTA MGYIIENNIV TSSLLSKVKQ FENIELFEQL
SVKSMNDYNE ETIRTTSILP SVTLSNDQQL HAKLIIGADG GNSILKKQLQ VPSIGRVYNQ
KAVVCTLKLG IKQDNNNNSS NNNNNNNNTL FQRFLPTGPI ALLPLANGYA NIIWSTNLMH
AQYLLELDDE SFLEQVKDSF LKSPSTSNSS FFEIASNLFN LNPKGLSGNE IYLPPIEGLV
SKRASFPLRI DHTFNYTLPR VCFIGDASHL VHPMAGQGVN LGMADVKTLS SIIEQSVQSG
YDIGDAMMLK RFEEIRKPEN LKMLLSIDTL FNLFTNNSIF VTGLRNFGMS LLNNISPLKN
LIIGVSKGES ILKFK
