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COQ6_SCHPO
ID   COQ6_SCHPO              Reviewed;         479 AA.
AC   Q9Y7Z9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 2.
DT   25-MAY-2022, entry version 138.
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=SPBC146.12;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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, composed of
CC       at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000255|HAMAP-
CC       Rule:MF_03193}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03193, ECO:0000269|PubMed:16823372}; Peripheral membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_03193}; Matrix side
CC       {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; CU329671; CAB46765.2; -; Genomic_DNA.
DR   PIR; T39426; T39426.
DR   RefSeq; NP_595401.2; NM_001021308.2.
DR   AlphaFoldDB; Q9Y7Z9; -.
DR   SMR; Q9Y7Z9; -.
DR   BioGRID; 276227; 2.
DR   STRING; 4896.SPBC146.12.1; -.
DR   MaxQB; Q9Y7Z9; -.
DR   PaxDb; Q9Y7Z9; -.
DR   EnsemblFungi; SPBC146.12.1; SPBC146.12.1:pep; SPBC146.12.
DR   GeneID; 2539672; -.
DR   KEGG; spo:SPBC146.12; -.
DR   PomBase; SPBC146.12; coq6.
DR   VEuPathDB; FungiDB:SPBC146.12; -.
DR   eggNOG; KOG3855; Eukaryota.
DR   HOGENOM; CLU_009665_8_0_1; -.
DR   InParanoid; Q9Y7Z9; -.
DR   OMA; SDVACII; -.
DR   UniPathway; UPA00232; -.
DR   PRO; PR:Q9Y7Z9; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR   GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; ISS:PomBase.
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: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; IMP:PomBase.
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; IPR018168; Ubi_Hdrlase_CS.
DR   InterPro; IPR010971; UbiH/COQ6.
DR   InterPro; IPR000689; UbQ_mOase_COQ6.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01989; COQ6; 1.
DR   TIGRFAMs; TIGR01988; Ubi-OHases; 1.
DR   PROSITE; PS01304; UBIH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Monooxygenase; Oxidoreductase; Reference proteome; Ubiquinone biosynthesis.
FT   CHAIN           1..479
FT                   /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT                   mitochondrial"
FT                   /id="PRO_0000207582"
SQ   SEQUENCE   479 AA;  53575 MW;  83E22D10046F8A66 CRC64;
     MSSLVLRGVS RVEMPTISPT LGIYTRKFAS QKILQRQFDV VIVGSGPVGL ALAAGLQSNP
     VTQSLKVGLL DIQDTMKLKD WKFETYSNRC SSLTNHTRMF FDKIGAWDFA RKDRIQPFQH
     ILASDGLTNS SIHLDQKPGS EPMAFMSENV NLQYALLNSI IDKMNNNIKK PNLEFLMPCT
     ITKLSKGENI YRTHIHTTTH GELTTKLLIG ADGRNSIVRK YANISMPGWN YLTHAVVGTL
     KIDPLKGPAV AFQRFLPTGP LAYLPLPDNN ATFVWSTRPH IASKLLRLPE ETFVKFLNAS
     FRLDYPDLSY LYQMDFSEPS KVNEQLDWRL QVKRNSNMQV PPVITEIVSG SRAAFPLRLA
     HVDEYVKEGI ALCGDAAHNT HPLAGQGLNT GIQDVESLIS ALSFAIKHGQ DIGSVFSLQP
     YFRDRYFKNH VYLGVVDKFH KLYAMENPVV TSVRTLGLSL FDRSASLKNF ILSTVANGI
 
 
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