COQ7_DICDI
ID COQ7_DICDI Reviewed; 217 AA.
AC Q54VB3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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};
GN Name=coq7 {ECO:0000255|HAMAP-Rule:MF_03194}; ORFNames=DDB_G0280475;
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: 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.
CC {ECO:0000255|HAMAP-Rule:MF_03194}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03194}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03194}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03194}.
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_03194}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_03194}.
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DR EMBL; AAFI02000036; EAL67216.1; -; Genomic_DNA.
DR RefSeq; XP_641196.1; XM_636104.1.
DR AlphaFoldDB; Q54VB3; -.
DR SMR; Q54VB3; -.
DR STRING; 44689.DDB0266669; -.
DR PaxDb; Q54VB3; -.
DR EnsemblProtists; EAL67216; EAL67216; DDB_G0280475.
DR GeneID; 8622577; -.
DR KEGG; ddi:DDB_G0280475; -.
DR dictyBase; DDB_G0280475; coq7.
DR eggNOG; KOG4061; Eukaryota.
DR HOGENOM; CLU_071892_2_0_1; -.
DR InParanoid; Q54VB3; -.
DR OMA; HYNDQVR; -.
DR PhylomeDB; Q54VB3; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q54VB3; -.
DR Proteomes; UP000002195; Chromosome 3.
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; ISS:dictyBase.
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: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; ISS:dictyBase.
DR CDD; cd01042; DMQH; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR HAMAP; MF_01658; COQ7; 1.
DR InterPro; IPR012347; Ferritin-like.
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 2: Evidence at transcript level;
KW Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Reference proteome; Repeat;
KW Ubiquinone biosynthesis.
FT CHAIN 1..217
FT /note="5-demethoxyubiquinone hydroxylase, mitochondrial"
FT /id="PRO_0000330874"
FT REPEAT 49..130
FT /note="1"
FT REPEAT 131..217
FT /note="2"
FT REGION 49..217
FT /note="2 X approximate tandem repeats"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 91
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 91
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03194"
SQ SEQUENCE 217 AA; 24694 MW; 1793578297EFD2AA CRC64;
MNSLIKSTKF LKKTNIIRSY CTKTNNNNNT NITKNVLSEI EKEKLKRQII ERIIRVDHAG
EFGAARIYEG QLAVLANTKE GPLIREMADQ EKEHQAKFNQ LIYEKRVRPT ILSPIWNVAG
FGLGYVSALM GKEAAMAVTV AVETVISDHY NDQLRQLNDA GIDDKELKET IKKFRDDELE
HMHIGIEHDA ELAPLYKPFS ELVKVGTKTA IWLSTRV
