COQ7_PSEMY
ID COQ7_PSEMY Reviewed; 215 AA.
AC A4XZC2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=3-demethoxyubiquinol 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_01658};
DE Short=DMQ hydroxylase {ECO:0000255|HAMAP-Rule:MF_01658};
DE EC=1.14.99.60 {ECO:0000255|HAMAP-Rule:MF_01658};
DE AltName: Full=2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase {ECO:0000255|HAMAP-Rule:MF_01658};
GN Name=coq7 {ECO:0000255|HAMAP-Rule:MF_01658}; OrderedLocusNames=Pmen_3941;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01658}.
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_01658};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01658};
CC Note=Binds 2 iron ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01658};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01658}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01658};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01658}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_01658}.
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DR EMBL; CP000680; ABP86688.1; -; Genomic_DNA.
DR RefSeq; WP_004373481.1; NC_009439.1.
DR AlphaFoldDB; A4XZC2; -.
DR SMR; A4XZC2; -.
DR STRING; 399739.Pmen_3941; -.
DR EnsemblBacteria; ABP86688; ABP86688; Pmen_3941.
DR KEGG; pmy:Pmen_3941; -.
DR PATRIC; fig|399739.8.peg.3994; -.
DR eggNOG; COG2941; Bacteria.
DR HOGENOM; CLU_088601_0_0_6; -.
DR OMA; NPLWYGG; -.
DR OrthoDB; 1382712at2; -.
DR UniPathway; UPA00232; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008682; F:3-demethoxyubiquinol 3-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cell membrane; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Ubiquinone biosynthesis.
FT CHAIN 1..215
FT /note="3-demethoxyubiquinol 3-hydroxylase"
FT /id="PRO_0000338713"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 146
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
SQ SEQUENCE 215 AA; 23508 MW; 714B60D625D66BDC CRC64;
MASERQYSPV DRLLLQADAA LRTLLPFSGA SSRPSPAIVQ AETDLNPEES RHIAGLMRIN
HTGEVCAQAL YQGQALTAKL PEVRSAMEHA ADEEIDHLAW CEQRIRELGS HPSVLNPLFY
GLSFGVGAVA GLVSDRVSLG FVAATEDQVC KHLDEHLEQI PEHDAKSRAI LEQMRIDEEQ
HANSALAAGG VRFPAPVKFG MTLLSKVMTK STYRI
