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COQ7_XANC8
ID   COQ7_XANC8              Reviewed;         217 AA.
AC   Q4UZF3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=XC_0489;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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; CP000050; AAY47570.1; -; Genomic_DNA.
DR   RefSeq; WP_011035727.1; NC_007086.1.
DR   AlphaFoldDB; Q4UZF3; -.
DR   SMR; Q4UZF3; -.
DR   EnsemblBacteria; AAY47570; AAY47570; XC_0489.
DR   GeneID; 58011787; -.
DR   KEGG; xcb:XC_0489; -.
DR   HOGENOM; CLU_088601_0_0_6; -.
DR   OMA; NPLWYGG; -.
DR   OrthoDB; 1382712at2; -.
DR   BioCyc; MetaCyc:MON-21242; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000420; 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; Ubiquinone biosynthesis.
FT   CHAIN           1..217
FT                   /note="3-demethoxyubiquinol 3-hydroxylase"
FT                   /id="PRO_0000338735"
FT   BINDING         66
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         96
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         96
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         99
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         180
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         180
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
SQ   SEQUENCE   217 AA;  23956 MW;  E28414B48AAB3DAC CRC64;
     MTQIPPSRLH SPLDRLLVEA QRALDTVFGN PPAERPNPAG DTPDAALAPA QRQHAAGLMR
     INHVGEVCAQ GLYFGQAAVA RDDHTRQHLL TAAQEETDHL AWCADRLREL ESRPSLFNPL
     WYAGSYALGA VAGLRGDDWS LGFVVETERQ VEAHLDEHLE TLPETDQRSR AILRVMKIDE
     ARHADHAEQA GARILPPPIP SAMALASKLM KTIAYRF
 
 
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