COQ7_CHRVO
ID COQ7_CHRVO Reviewed; 206 AA.
AC Q7NSP9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=CV_3371;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016825; AAQ61035.1; -; Genomic_DNA.
DR RefSeq; WP_011136918.1; NC_005085.1.
DR AlphaFoldDB; Q7NSP9; -.
DR SMR; Q7NSP9; -.
DR STRING; 243365.CV_3371; -.
DR EnsemblBacteria; AAQ61035; AAQ61035; CV_3371.
DR KEGG; cvi:CV_3371; -.
DR eggNOG; COG2941; Bacteria.
DR HOGENOM; CLU_088601_0_0_4; -.
DR OMA; NPLWYGG; -.
DR OrthoDB; 1382712at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001424; 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..206
FT /note="3-demethoxyubiquinol 3-hydroxylase"
FT /id="PRO_0000338678"
FT BINDING 55
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
SQ SEQUENCE 206 AA; 22395 MW; EE75ADF4689F2515 CRC64;
MLDKLITELD KGLRTLCAPA HSGRAHPDQD IAEADLSAAE KKHALGLMRV NHCGEVCAQA
LYQGQALTAR DASAREALRQ AAQEEVEHLA WTERRIRELG GRPSLLNPLW YTGSLALGVA
AGVLGDKWNL GFLQETERQV GAHLDSHLSA LPPDDARSRA IVRQMRDDEL QHAEMAHELG
AAELPAPVKA AMKLSAKVMT GSSYRV
