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COQ7_PSEPK
ID   COQ7_PSEPK              Reviewed;         215 AA.
AC   Q88QR1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=PP_0427;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66057.1; -; Genomic_DNA.
DR   RefSeq; NP_742593.1; NC_002947.4.
DR   RefSeq; WP_010951761.1; NC_002947.4.
DR   AlphaFoldDB; Q88QR1; -.
DR   SMR; Q88QR1; -.
DR   STRING; 160488.PP_0427; -.
DR   EnsemblBacteria; AAN66057; AAN66057; PP_0427.
DR   KEGG; ppu:PP_0427; -.
DR   PATRIC; fig|160488.4.peg.458; -.
DR   eggNOG; COG2941; Bacteria.
DR   HOGENOM; CLU_088601_0_0_6; -.
DR   OMA; NPLWYGG; -.
DR   PhylomeDB; Q88QR1; -.
DR   BioCyc; PPUT160488:G1G01-463-MON; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000556; 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_0000338716"
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;  24001 MW;  F57361FC3C66F7C9 CRC64;
     MATERHYSPL DRLLLQADTA MRTLLPFSGQ PTRPSPAIVQ PDADLDEQQA RHIAGLMRIN
     HTGEVCAQAL YQGQALTAKL PEVRKAMEHA AEEEVDHLAW CEQRIRQLNS HPSVLNPLFY
     GMSFGIGALA GLVSDKVSLG FVAATEHQVC KHLDEHLEQL PHEDEKSRAI LEQMRIDEEQ
     HAESALEAGG YRFPAPVRFG MSLLAKVMTK STYRI
 
 
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