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COQ7_ACIBC
ID   COQ7_ACIBC              Reviewed;         211 AA.
AC   B2HTV8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=ACICU_02334;
OS   Acinetobacter baumannii (strain ACICU).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=405416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACICU;
RX   PubMed=18411315; DOI=10.1128/aac.01643-07;
RA   Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA   Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT   "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT   Acinetobacter baumannii strain belonging to the European clone II group.";
RL   Antimicrob. Agents Chemother. 52:2616-2625(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; CP000863; ACC57646.1; -; Genomic_DNA.
DR   RefSeq; WP_001216787.1; NZ_CP031380.1.
DR   AlphaFoldDB; B2HTV8; -.
DR   SMR; B2HTV8; -.
DR   GeneID; 66396765; -.
DR   KEGG; abc:ACICU_02334; -.
DR   HOGENOM; CLU_088601_0_0_6; -.
DR   OMA; NPLWYGG; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000008839; 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_1000187041"
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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