COQ7_YEAST
ID COQ7_YEAST Reviewed; 233 AA.
AC P41735; D6W2I3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=5-demethoxyubiquinone hydroxylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03194, ECO:0000305|PubMed:16624818};
DE Short=DMQ hydroxylase {ECO:0000255|HAMAP-Rule:MF_03194};
DE EC=1.14.99.60 {ECO:0000255|HAMAP-Rule:MF_03194, ECO:0000269|PubMed:19002377, ECO:0000269|PubMed:23940037, ECO:0000305|PubMed:16624818};
DE AltName: Full=Catabolite repression protein 5 {ECO:0000303|PubMed:8557031};
DE AltName: Full=Ubiquinone biosynthesis monooxygenase COQ7 {ECO:0000255|HAMAP-Rule:MF_03194, ECO:0000305|PubMed:8621692};
DE Flags: Precursor;
GN Name=CAT5 {ECO:0000303|PubMed:8557031};
GN Synonyms=COQ7 {ECO:0000255|HAMAP-Rule:MF_03194,
GN ECO:0000303|PubMed:8621692};
GN OrderedLocusNames=YOR125C {ECO:0000312|SGD:S000005651};
GN ORFNames=O3284, YOR3284C;
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].
RX PubMed=8557031; DOI=10.1002/j.1460-2075.1995.tb00302.x;
RA Proft M., Koetter P., Hedges D., Bojunga N., Entian K.-D.;
RT "CAT5, a new gene necessary for derepression of gluconeogenic enzymes in
RT Saccharomyces cerevisiae.";
RL EMBO J. 14:6116-6126(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PATHWAY.
RX PubMed=8621692; DOI=10.1074/jbc.271.6.2995;
RA Marbois B.N., Clarke C.F.;
RT "The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for
RT ubiquinone biosynthesis.";
RL J. Biol. Chem. 271:2995-3004(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9452453; DOI=10.1074/jbc.273.6.3351;
RA Jonassen T., Proft M., Randez-Gil F., Schultz J.R., Marbois B.N.,
RA Entian K.-D., Clarke C.F.;
RT "Yeast Clk-1 homologue (Coq7/Cat5) is a mitochondrial protein in coenzyme Q
RT synthesis.";
RL J. Biol. Chem. 273:3351-3357(1998).
RN [8]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
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 [10]
RP FUNCTION, AND MUTAGENESIS OF GLU-194.
RX PubMed=16624818; DOI=10.1074/jbc.m513267200;
RA Tran U.C., Marbois B.N., Gin P., Gulmezian M., Jonassen T., Clarke C.F.;
RT "Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial
RT targeting of the Escherichia coli UbiF polypeptide: two functions of yeast
RT Coq7 polypeptide in coenzyme Q biosynthesis.";
RL J. Biol. Chem. 281:16401-16409(2006).
RN [11]
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 [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19002377; DOI=10.1007/s00018-008-8547-7;
RA Padilla S., Tran U.C., Jimenez-Hidalgo M., Lopez-Martin J.M.,
RA Martin-Montalvo A., Clarke C.F., Navas P., Santos-Ocana C.;
RT "Hydroxylation of demethoxy-Q6 constitutes a control point in yeast
RT coenzyme Q6 biosynthesis.";
RL Cell. Mol. Life Sci. 66:173-186(2009).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT
RP SER-20; SER-28 AND THR-32, DEPHOSPHORYLATION, METAL-BINDING SITES, AND
RP MUTAGENESIS OF SER-20; SER-28 AND THR-32.
RX PubMed=23940037; DOI=10.1074/jbc.m113.474494;
RA Martin-Montalvo A., Gonzalez-Mariscal I., Pomares-Viciana T.,
RA Padilla-Lopez S., Ballesteros M., Vazquez-Fonseca L., Gandolfo P.,
RA Brautigan D.L., Navas P., Santos-Ocana C.;
RT "The phosphatase Ptc7 induces coenzyme Q biosynthesis by activating the
RT hydroxylase Coq7 in yeast.";
RL J. Biol. Chem. 288:28126-28137(2013).
RN [14]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Catalyzes the hydroxylation of 2-hexaprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis
CC (PubMed:16624818, PubMed:8621692, PubMed:9452453, PubMed:23940037). Has
CC also a structural role in the COQ enzyme complex, stabilizing COQ3 and
CC COQ4 polypeptides (PubMed:16624818). {ECO:0000255|HAMAP-Rule:MF_03194,
CC ECO:0000269|PubMed:16624818, ECO:0000269|PubMed:23940037,
CC ECO:0000269|PubMed:8621692, ECO:0000269|PubMed:9452453}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol +
CC AH2 + O2 = A + a 3-demethylubiquinol + H2O; Xref=Rhea:RHEA:50908,
CC Rhea:RHEA-COMP:10859, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:84167, ChEBI:CHEBI:84422; EC=1.14.99.60;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03194,
CC ECO:0000269|PubMed:19002377, ECO:0000269|PubMed:23940037};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03194};
CC Note=Binds 2 iron ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03194};
CC -!- ACTIVITY REGULATION: Dephosphorylation by PTC7 leads to activation.
CC {ECO:0000269|PubMed:23940037}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03194, ECO:0000305|PubMed:8621692}.
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_03194, ECO:0000269|PubMed:17391640,
CC ECO:0000269|PubMed:24406904}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03194, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:24406904, ECO:0000269|PubMed:9452453}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03194,
CC ECO:0000269|PubMed:24406904}; Matrix side {ECO:0000255|HAMAP-
CC Rule:MF_03194, ECO:0000269|PubMed:24406904}.
CC -!- PTM: Phosphorylated (PubMed:23940037). Dephosphorylated by PTC7;
CC dephosphorylation is essential for enzyme activation (PubMed:23940037).
CC {ECO:0000269|PubMed:23940037}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_03194, ECO:0000305}.
CC -!- CAUTION: Was originally thought to be involved in carbon catabolite
CC repression (PubMed:8557031). It has later been demonstrated that the
CC catabolite-regulation defect in COQ7 mutants was a secondary effect of
CC the respiration deficiency in ubiquinone-deficient mutants and could be
CC rescued by the addition of exogenous ubiquinone (PubMed:9452453).
CC {ECO:0000305|PubMed:8557031, ECO:0000305|PubMed:9452453}.
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DR EMBL; X82930; CAA58105.1; -; Genomic_DNA.
DR EMBL; S81938; AAB36435.1; -; mRNA.
DR EMBL; X90518; CAA62119.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64044.1; -; Genomic_DNA.
DR EMBL; Z75033; CAA99324.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10899.1; -; Genomic_DNA.
DR PIR; S49912; S49912.
DR RefSeq; NP_014768.2; NM_001183544.1.
DR AlphaFoldDB; P41735; -.
DR SMR; P41735; -.
DR BioGRID; 34520; 397.
DR ComplexPortal; CPX-1155; CoQ biosynthetic complex.
DR DIP; DIP-6435N; -.
DR IntAct; P41735; 14.
DR MINT; P41735; -.
DR STRING; 4932.YOR125C; -.
DR iPTMnet; P41735; -.
DR MaxQB; P41735; -.
DR PaxDb; P41735; -.
DR PRIDE; P41735; -.
DR EnsemblFungi; YOR125C_mRNA; YOR125C; YOR125C.
DR GeneID; 854292; -.
DR KEGG; sce:YOR125C; -.
DR SGD; S000005651; CAT5.
DR VEuPathDB; FungiDB:YOR125C; -.
DR eggNOG; KOG4061; Eukaryota.
DR GeneTree; ENSGT00390000014520; -.
DR HOGENOM; CLU_071892_0_0_1; -.
DR InParanoid; P41735; -.
DR OMA; HYNDQVR; -.
DR BioCyc; MetaCyc:MON3O-164; -.
DR BioCyc; YEAST:MON3O-164; -.
DR BRENDA; 1.14.99.60; 984.
DR UniPathway; UPA00232; -.
DR PRO; PR:P41735; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P41735; 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:0008682; F:3-demethoxyubiquinol 3-hydroxylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; ISS:SGD.
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:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:SGD.
DR CDD; cd01042; DMQH; 1.
DR HAMAP; MF_01658; COQ7; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR011566; Ubq_synth_Coq7.
DR PANTHER; PTHR11237; PTHR11237; 1.
DR Pfam; PF03232; COQ7; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT CHAIN 16..233
FT /note="5-demethoxyubiquinone hydroxylase, mitochondrial"
FT /id="PRO_0000089330"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 95
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 95
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23940037"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23940037"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23940037"
FT MUTAGEN 20
FT /note="S->A: Loss of phosphorylation and increased levels
FT of COQ6; when associated with S-28 and T-32."
FT /evidence="ECO:0000269|PubMed:23940037"
FT MUTAGEN 28
FT /note="S->A: Loss of phosphorylation and increased levels
FT of COQ6; when associated with S-20 and T-32."
FT /evidence="ECO:0000269|PubMed:23940037"
FT MUTAGEN 32
FT /note="T->A: Loss of phosphorylation and increased levels
FT of COQ6; when associated with S-20 and S-28."
FT /evidence="ECO:0000269|PubMed:23940037"
FT MUTAGEN 194
FT /note="E->K: Lacks ubiquinone and accumulates the
FT intermediate DMQH2, causing respiratory deficiency."
FT /evidence="ECO:0000269|PubMed:16624818"
SQ SEQUENCE 233 AA; 26060 MW; 2686F44C5F17EFE5 CRC64;
MLSRVSVFKP ASRGFSVLSS LKITEHTSAK HTEKPEHAPK CQNLSDAQAA FLDRVIRVDQ
AGELGADYIY AGQYFVLAHR YPHLKPVLKH IWDQEIHHHN TFNNLQLKRR VRPSLLTPLW
KAGAFAMGAG TALISPEAAM ACTEAVETVI GGHYNGQLRN LANQFNLERT DGTKGPSEEI
KSLTSTIQQF RDDELEHLDT AIKHDSYMAV PYTVITEGIK TICRVAIWSA ERI
