COQ7_PSEAE
ID COQ7_PSEAE Reviewed; 215 AA.
AC Q9I5R6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=3-demethoxyubiquinol 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_01658};
DE Short=DMQ hydroxylase {ECO:0000255|HAMAP-Rule:MF_01658, ECO:0000303|PubMed:11435415};
DE EC=1.14.99.60 {ECO:0000255|HAMAP-Rule:MF_01658, ECO:0000269|PubMed:11435415};
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, ECO:0000303|PubMed:11435415};
GN OrderedLocusNames=PA0655;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION IN UBIQUINONE BIOSYNTHESIS, CATALYTIC ACTIVITY, MEMBER OF THE
RP DI-IRON CARBOXYLATE PROTEIN FAMILY, COFACTOR, PATHWAY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11435415; DOI=10.1074/jbc.c100346200;
RA Stenmark P., Gruenler J., Mattsson J., Sindelar P.J., Nordlund P.,
RA Berthold D.A.;
RT "A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1),
RT a membrane-bound hydroxylase involved in ubiquinone biosynthesis.";
RL J. Biol. Chem. 276:33297-33300(2001).
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, ECO:0000269|PubMed:11435415}.
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 ECO:0000269|PubMed:11435415};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01658,
CC ECO:0000305|PubMed:11435415};
CC Note=Binds 2 iron ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01658,
CC ECO:0000305|PubMed:11435415};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01658, ECO:0000269|PubMed:11435415}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01658,
CC ECO:0000305|PubMed:11435415}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01658, ECO:0000305|PubMed:11435415}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000255|HAMAP-
CC Rule:MF_01658, ECO:0000305}.
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DR EMBL; AE004091; AAG04044.1; -; Genomic_DNA.
DR PIR; E83564; E83564.
DR RefSeq; NP_249346.1; NC_002516.2.
DR RefSeq; WP_003085224.1; NZ_QZGE01000010.1.
DR AlphaFoldDB; Q9I5R6; -.
DR SMR; Q9I5R6; -.
DR STRING; 287.DR97_3608; -.
DR PaxDb; Q9I5R6; -.
DR PRIDE; Q9I5R6; -.
DR DNASU; 880759; -.
DR EnsemblBacteria; AAG04044; AAG04044; PA0655.
DR GeneID; 880759; -.
DR KEGG; pae:PA0655; -.
DR PATRIC; fig|208964.12.peg.686; -.
DR PseudoCAP; PA0655; -.
DR HOGENOM; CLU_088601_0_0_6; -.
DR InParanoid; Q9I5R6; -.
DR OMA; NPLWYGG; -.
DR PhylomeDB; Q9I5R6; -.
DR BioCyc; MetaCyc:MON-13881; -.
DR BioCyc; PAER208964:G1FZ6-660-MON; -.
DR BRENDA; 1.14.99.60; 5087.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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:0004497; F:monooxygenase activity; IGI:UniProtKB.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IGI:UniProtKB.
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 1: Evidence at protein level;
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_0000338707"
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 ECO:0000305|PubMed:11435415"
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 ECO:0000305|PubMed:11435415"
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 ECO:0000305|PubMed:11435415"
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 ECO:0000305|PubMed:11435415"
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 ECO:0000305|PubMed:11435415"
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 ECO:0000305|PubMed:11435415"
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 ECO:0000305|PubMed:11435415"
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,
FT ECO:0000305|PubMed:11435415"
SQ SEQUENCE 215 AA; 23644 MW; F2D53B0130F645B3 CRC64;
MSADRHYSPI DRFLLQADSA LRTLLPFSGQ PARPSPAIVE PDGELSEEDT RHIAGLMRIN
HTGEVCAQAL YQGQSLTAKL PEVREAMEEA AEEEIDHLAW CEQRIRQLGS RPSVLNPIFY
GLSFGVGAAA GLVSDRVSLG FVAATEDQVC KHLDEHLAQI PQEDRKSRAI LEQMRIDEEQ
HSSNALAAGG LRFPAPVKLG MSLLAKVMTK STYRI
