COQ7_PSEFS
ID COQ7_PSEFS Reviewed; 215 AA.
AC C3K303;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=PFLU_5554;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; AM181176; CAY52809.1; -; Genomic_DNA.
DR RefSeq; WP_015886151.1; NC_012660.1.
DR AlphaFoldDB; C3K303; -.
DR SMR; C3K303; -.
DR STRING; 294.SRM1_05211; -.
DR PRIDE; C3K303; -.
DR EnsemblBacteria; CAY52809; CAY52809; PFLU_5554.
DR GeneID; 57376223; -.
DR KEGG; pfs:PFLU_5554; -.
DR eggNOG; COG2941; Bacteria.
DR HOGENOM; CLU_088601_0_0_6; -.
DR OMA; NPLWYGG; -.
DR OrthoDB; 1382712at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000002332; Chromosome.
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; Reference proteome; Ubiquinone biosynthesis.
FT CHAIN 1..215
FT /note="3-demethoxyubiquinol 3-hydroxylase"
FT /id="PRO_1000215856"
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; 23881 MW; D855CF861DED5195 CRC64;
MTTQRHYSPI DRLLLQADMA MRTLLPFSGQ PYRPSPAIVQ PDAQMSETET RHVAGLMRIN
HTGEVCAQAL YQGQALTAKL PQVRAAMEHA AEEEIDHLAW CEQRIRQLGS HPSVLNPLFY
GLSFGIGAAA GLISDKVSLG FVAATEHQVC KHLDEHLEQL PAEDEKSRAI LEQMRIDEEH
HAESALDAGG FRFPAPVRFG MSLLAKVMTK STYRI
