COQ7_SCHPO
ID COQ7_SCHPO Reviewed; 216 AA.
AC O74826;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=5-demethoxyubiquinone hydroxylase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03194};
DE Short=DMQ hydroxylase {ECO:0000255|HAMAP-Rule:MF_03194};
DE EC=1.14.99.60 {ECO:0000255|HAMAP-Rule:MF_03194};
DE AltName: Full=Ubiquinone biosynthesis monooxygenase COQ7 {ECO:0000255|HAMAP-Rule:MF_03194};
DE Flags: Precursor;
GN Name=coq7 {ECO:0000255|HAMAP-Rule:MF_03194}; ORFNames=SPBC337.15c;
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 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: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has
CC also a structural role in the COQ enzyme complex, stabilizing other COQ
CC polypeptides. {ECO:0000255|HAMAP-Rule:MF_03194}.
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 -!- 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 -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03194}.
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}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03194, ECO:0000269|PubMed:16823372}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_03194}; Matrix side
CC {ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_03194}.
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DR EMBL; CU329671; CAA21285.1; -; Genomic_DNA.
DR PIR; T40268; T40268.
DR RefSeq; NP_595416.1; NM_001021323.2.
DR AlphaFoldDB; O74826; -.
DR SMR; O74826; -.
DR BioGRID; 277539; 2.
DR STRING; 4896.SPBC337.15c.1; -.
DR MaxQB; O74826; -.
DR PaxDb; O74826; -.
DR EnsemblFungi; SPBC337.15c.1; SPBC337.15c.1:pep; SPBC337.15c.
DR GeneID; 2541024; -.
DR KEGG; spo:SPBC337.15c; -.
DR PomBase; SPBC337.15c; coq7.
DR VEuPathDB; FungiDB:SPBC337.15c; -.
DR eggNOG; KOG4061; Eukaryota.
DR HOGENOM; CLU_071892_2_0_1; -.
DR InParanoid; O74826; -.
DR OMA; NPLWYGG; -.
DR PhylomeDB; O74826; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:O74826; -.
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; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0008682; F:3-demethoxyubiquinol 3-hydroxylase activity; IMP:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:PomBase.
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 3: Inferred from homology;
KW Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Reference proteome; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT CHAIN 28..216
FT /note="5-demethoxyubiquinone hydroxylase, mitochondrial"
FT /id="PRO_0000315897"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 179
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
SQ SEQUENCE 216 AA; 24397 MW; 1493BD6358E9EBD0 CRC64;
MLSRRQLIPI ATKSVSPFLR SSITCRRISM GRKELSEKDS NILDSVIRVD QAGELGANQI
YKGQHFILQF TDPKVAPTIQ HMWDQEKYHL ATFDNYVLKN RVRPTFLRPF WDIAGFALGA
GTALLGTKAA MACTEAVETV IGGHYNDQLR ETAHLENKAP EFKEIRSHLA EFRDDELEHL
NTAVEGWNAK EAPAHALLTN AIQMGCKAAI WMCKRF
