COQ6_YEAST
ID COQ6_YEAST Reviewed; 479 AA.
AC P53318; D6VV35; Q05674; Q05675;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000305|PubMed:12721307};
DE EC=1.14.13.- {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000305|PubMed:21944752};
DE AltName: Full=Ubiquinone C4-deaminase {ECO:0000303|PubMed:26260787};
DE EC=3.5.-.- {ECO:0000269|PubMed:26260787};
DE Flags: Precursor;
GN Name=COQ6 {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000303|PubMed:12721307};
GN OrderedLocusNames=YGR255C {ECO:0000312|SGD:S000003487}; ORFNames=G9165;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, COFACTOR, AND
RP PATHWAY.
RX PubMed=12721307; DOI=10.1074/jbc.m303234200;
RA Gin P., Hsu A.Y., Rothman S.C., Jonassen T., Lee P.T., Tzagoloff A.,
RA Clarke C.F.;
RT "The Saccharomyces cerevisiae COQ6 gene encodes a mitochondrial flavin-
RT dependent monooxygenase required for coenzyme Q biosynthesis.";
RL J. Biol. Chem. 278:25308-25316(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9133741;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<369::aid-yea81>3.0.co;2-v;
RA Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.;
RT "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII
RT reveals the presence of three new open reading frames and of a tRNAThr
RT gene.";
RL Yeast 13:369-372(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Miosga T.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION IN COQ ENZYME COMPLEX, AND INTERACTION WITH COQ9.
RX PubMed=17391640; DOI=10.1016/j.abb.2007.02.016;
RA Hsieh E.J., Gin P., Gulmezian M., Tran U.C., Saiki R., Marbois B.N.,
RA Clarke C.F.;
RT "Saccharomyces cerevisiae Coq9 polypeptide is a subunit of the
RT mitochondrial coenzyme Q biosynthetic complex.";
RL Arch. Biochem. Biophys. 463:19-26(2007).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-202; GLY-386 AND
RP ASN-388.
RX PubMed=21944752; DOI=10.1016/j.chembiol.2011.07.008;
RA Ozeir M., Muhlenhoff U., Webert H., Lill R., Fontecave M., Pierrel F.;
RT "Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation
RT reaction and substrate analogs rescue Coq6 deficiency.";
RL Chem. Biol. 18:1134-1142(2011).
RN [10]
RP SUBUNIT.
RX PubMed=24406904; DOI=10.1016/j.bbalip.2013.12.017;
RA He C.H., Xie L.X., Allan C.M., Tran U.C., Clarke C.F.;
RT "Coenzyme Q supplementation or over-expression of the yeast Coq8 putative
RT kinase stabilizes multi-subunit Coq polypeptide complexes in yeast coq null
RT mutants.";
RL Biochim. Biophys. Acta 1841:630-644(2014).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26260787; DOI=10.1074/jbc.m115.675744;
RA Ozeir M., Pelosi L., Ismail A., Mellot-Draznieks C., Fontecave M.,
RA Pierrel F.;
RT "Coq6 is responsible for the C4-deamination reaction in coenzyme Q
RT biosynthesis in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 290:24140-24151(2015).
RN [12]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF GLY-248 AND LEU-382.
RX PubMed=26808124; DOI=10.1371/journal.pcbi.1004690;
RA Ismail A., Leroux V., Smadja M., Gonzalez L., Lombard M., Pierrel F.,
RA Mellot-Draznieks C., Fontecave M.;
RT "Coenzyme Q biosynthesis: evidence for a substrate access channel in the
RT FAD-dependent monooxygenase Coq6.";
RL PLoS Comput. Biol. 12:E1004690-E1004690(2016).
CC -!- FUNCTION: FAD-dependent monooxygenase required for the C5-ring
CC hydroxylation during ubiquinone biosynthesis. Catalyzes the
CC hydroxylation of 3-hexaprenyl-4-hydroxybenzoic acid (HHB) to 3-
CC hexaprenyl-4,5-dihydroxybenzoic acid (DHHB). The electrons required for
CC the hydroxylation reaction may be funneled indirectly from NADPH via
CC ferredoxin (YAH1) and ferredoxin reductase (ARH1) to COQ6
CC (PubMed:21944752). Can also convert 3-hexaprenyl-4-aminobenzoic acid
CC (HAB), a COQ2-prenylated pABA, to DHHB in a two step process. HAB is
CC first hydroxylated at C5 to yield 3-hexaprenyl-4-amino-5-hydroxybenzoic
CC acid (HHAB) which is further deaminated at C4 by COQ6 to produce DHHB
CC (PubMed:26260787). {ECO:0000255|HAMAP-Rule:MF_03193,
CC ECO:0000269|PubMed:21944752, ECO:0000269|PubMed:26260787}.
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 ECO:0000269|PubMed:21944752};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2
CC reduced [2Fe-2S]-[ferredoxin] = 4-amino-5-hydroxy-3-all-trans-
CC hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:58392, 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:142618,
CC ChEBI:CHEBI:142619; Evidence={ECO:0000255|HAMAP-Rule:MF_03193,
CC ECO:0000269|PubMed:26260787};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxy-3-all-trans-hexaprenylbenzoate + 5 H(+) + O2
CC + 4 reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-
CC hexaprenylbenzoate + H2O + NH4(+) + 4 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:58396, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58373, ChEBI:CHEBI:142619; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03193, ECO:0000269|PubMed:26260787};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03193,
CC ECO:0000269|PubMed:26808124};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000305|PubMed:12721307,
CC ECO:0000305|PubMed:21944752}.
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, ECO:0000269|PubMed:17391640,
CC ECO:0000269|PubMed:24406904}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03193, ECO:0000269|PubMed:12721307,
CC ECO:0000269|PubMed:14576278}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000269|PubMed:12721307}; Matrix
CC side {ECO:0000255|HAMAP-Rule:MF_03193, ECO:0000269|PubMed:12721307}.
CC -!- MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000255|HAMAP-
CC Rule:MF_03193, ECO:0000305}.
CC -!- CAUTION: Based on current literature, utilization of para-aminobenzoic
CC acid (pABA) involving C4-deamination seems not to occur in bacteria,
CC plants and mammals where only C5 hydroxylation of HHB has been shown,
CC even if human COQ6 is able to perform the deamination reaction in the
CC absence of COQ9. {ECO:0000305|PubMed:26260787}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56704.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF003698; AAB61341.1; -; Genomic_DNA.
DR EMBL; X99228; CAA67617.1; -; Genomic_DNA.
DR EMBL; Z73040; CAA97284.1; -; Genomic_DNA.
DR EMBL; X80690; CAA56704.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X80690; CAA56705.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08346.1; -; Genomic_DNA.
DR PIR; S64587; S64587.
DR RefSeq; NP_011771.1; NM_001181384.1.
DR AlphaFoldDB; P53318; -.
DR SMR; P53318; -.
DR BioGRID; 33506; 134.
DR ComplexPortal; CPX-1155; CoQ biosynthetic complex.
DR IntAct; P53318; 8.
DR MINT; P53318; -.
DR STRING; 4932.YGR255C; -.
DR MaxQB; P53318; -.
DR PaxDb; P53318; -.
DR PRIDE; P53318; -.
DR TopDownProteomics; P53318; -.
DR EnsemblFungi; YGR255C_mRNA; YGR255C; YGR255C.
DR GeneID; 853170; -.
DR KEGG; sce:YGR255C; -.
DR SGD; S000003487; COQ6.
DR VEuPathDB; FungiDB:YGR255C; -.
DR eggNOG; KOG3855; Eukaryota.
DR GeneTree; ENSGT00390000015152; -.
DR HOGENOM; CLU_009665_8_0_1; -.
DR InParanoid; P53318; -.
DR OMA; SDVACII; -.
DR BioCyc; MetaCyc:YGR255C-MON; -.
DR BioCyc; YEAST:YGR255C-MON; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:P53318; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53318; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; ISA:SGD.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IMP:SGD.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:SGD.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03193"
FT CHAIN 18..479
FT /note="Ubiquinone biosynthesis monooxygenase COQ6,
FT mitochondrial"
FT /id="PRO_0000207581"
FT MUTAGEN 202
FT /note="G->A: Accumulates ubiquinone biosynthesis
FT intermediates lacking the C5-ring hydroxyl."
FT /evidence="ECO:0000269|PubMed:21944752"
FT MUTAGEN 248
FT /note="G->R: Abolishes catalytic activity; when associated
FT with E-382."
FT /evidence="ECO:0000269|PubMed:26808124"
FT MUTAGEN 382
FT /note="L->E: Abolishes catalytic activity; when associated
FT with R-248."
FT /evidence="ECO:0000269|PubMed:26808124"
FT MUTAGEN 386
FT /note="G->A: Accumulates ubiquinone biosynthesis
FT intermediates lacking the C5-ring hydroxyl; when associated
FT with D-388."
FT /evidence="ECO:0000269|PubMed:21944752"
FT MUTAGEN 388
FT /note="N->D: Accumulates ubiquinone biosynthesis
FT intermediates lacking the C5-ring hydroxyl; when associated
FT with A-386."
FT /evidence="ECO:0000269|PubMed:21944752"
FT CONFLICT 60
FT /note="V -> I (in Ref. 5; CAA56704)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="K -> R (in Ref. 5; CAA56704)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="K -> E (in Ref. 5; CAA56705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 53527 MW; B6D4286545CCE695 CRC64;
MFFSKVMLTR RILVRGLATA KSSAPKLTDV LIVGGGPAGL TLAASIKNSP QLKDLKTTLV
DMVDLKDKLS DFYNSPPDYF TNRIVSVTPR SIHFLENNAG ATLMHDRIQS YDGLYVTDGC
SKATLDLARD SMLCMIEIIN IQASLYNRIS QYDSKKDSID IIDNTKVVNI KHSDPNDPLS
WPLVTLSNGE VYKTRLLVGA DGFNSPTRRF SQIPSRGWMY NAYGVVASMK LEYPPFKLRG
WQRFLPTGPI AHLPMPENNA TLVWSSSERL SRLLLSLPPE SFTALINAAF VLEDADMNYY
YRTLEDGSMD TDKLIEDIKF RTEEIYATLK DESDIDEIYP PRVVSIIDKT RARFPLKLTH
ADRYCTDRVA LVGDAAHTTH PLAGQGLNMG QTDVHGLVYA LEKAMERGLD IGSSLSLEPF
WAERYPSNNV LLGMADKLFK LYHTNFPPVV ALRTFGLNLT NKIGPVKNMI IDTLGGNEK
