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COQ7_ACIBS
ID   COQ7_ACIBS              Reviewed;         211 AA.
AC   B0VM45;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, 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=ABSDF1605;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAP00945.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VM45; -.
DR   SMR; B0VM45; -.
DR   EnsemblBacteria; CAP00945; CAP00945; ABSDF1605.
DR   KEGG; abm:ABSDF1605; -.
DR   HOGENOM; CLU_088601_0_0_6; -.
DR   OMA; NPLWYGG; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001741; 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..211
FT                   /note="3-demethoxyubiquinol 3-hydroxylase"
FT                   /id="PRO_1000187042"
FT   BINDING         60
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         90
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         90
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         93
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         142
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         174
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         174
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
FT   BINDING         177
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01658"
SQ   SEQUENCE   211 AA;  23556 MW;  2944B2C86D95A9E9 CRC64;
     MRHYTGIDQL INSFDQALRS LVPGATAAQR QNPAETVEAK LGVEDARHVA GLMRVNHSGE
     VCAQALYHGQ ALTAKLPNVR REMQQAAIEE QDHLAWCEDR LKELNSHTSL LNPIWYGLSY
     GMGALAGIAG DKYSLGFVAE TERQVSLHLQ DHLNQLPAQD ERSRKILEQM NEDELHHRHT
     ALEAGGVELP YAVKITMTAI SKLMTKTSYY L
 
 
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