UBIF_ECOLI
ID UBIF_ECOLI Reviewed; 391 AA.
AC P75728; P77111;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=3-demethoxyubiquinol 3-hydroxylase {ECO:0000305};
DE EC=1.14.99.60 {ECO:0000269|PubMed:10802164};
DE AltName: Full=2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase;
GN Name=ubiF; Synonyms=yleB; OrderedLocusNames=b0662, JW0659;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-337.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=10802164; DOI=10.1111/j.1574-6968.2000.tb09097.x;
RA Kwon O., Kotsakis A., Meganathan R.;
RT "Ubiquinone (coenzyme Q) biosynthesis in Escherichia coli: identification
RT of the ubiF gene.";
RL FEMS Microbiol. Lett. 186:157-161(2000).
RN [6]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=30686758; DOI=10.1016/j.chembiol.2018.12.001;
RA Hajj Chehade M., Pelosi L., Fyfe C.D., Loiseau L., Rascalou B.,
RA Brugiere S., Kazemzadeh K., Vo C.D., Ciccone L., Aussel L., Coute Y.,
RA Fontecave M., Barras F., Lombard M., Pierrel F.;
RT "A soluble metabolon synthesizes the isoprenoid lipid ubiquinone.";
RL Cell Chem. Biol. 26:482-492(2019).
CC -!- FUNCTION: Catalyzes the hydroxylation of 2-octaprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
CC {ECO:0000269|PubMed:10802164}.
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:0000269|PubMed:10802164};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P53318};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000269|PubMed:10802164}.
CC -!- SUBUNIT: Component of the Ubi complex metabolon, which regroups five
CC ubiquinone biosynthesis proteins (UbiE, UbiF, UbiG, UbiH and UbiI) and
CC two accessory factors (UbiK and the lipid-binding protein UbiJ).
CC {ECO:0000269|PubMed:30686758}.
CC -!- INTERACTION:
CC P75728; P75680: insO1; NbExp=3; IntAct=EBI-562588, EBI-9152908;
CC P75728; P33230: rcbA; NbExp=2; IntAct=EBI-562588, EBI-562744;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30686758}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000305}.
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DR EMBL; U00096; AAC73763.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35316.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40864.1; -; Genomic_DNA.
DR PIR; D64801; D64801.
DR RefSeq; NP_415195.1; NC_000913.3.
DR RefSeq; WP_000184541.1; NZ_SSZK01000037.1.
DR AlphaFoldDB; P75728; -.
DR SMR; P75728; -.
DR BioGRID; 4261231; 299.
DR BioGRID; 849642; 6.
DR DIP; DIP-11069N; -.
DR IntAct; P75728; 12.
DR STRING; 511145.b0662; -.
DR jPOST; P75728; -.
DR PaxDb; P75728; -.
DR PRIDE; P75728; -.
DR DNASU; 945261; -.
DR EnsemblBacteria; AAC73763; AAC73763; b0662.
DR EnsemblBacteria; BAA35316; BAA35316; BAA35316.
DR GeneID; 945261; -.
DR KEGG; ecj:JW0659; -.
DR KEGG; eco:b0662; -.
DR PATRIC; fig|1411691.4.peg.1606; -.
DR EchoBASE; EB3422; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_3_6; -.
DR InParanoid; P75728; -.
DR OMA; PELGYMV; -.
DR PhylomeDB; P75728; -.
DR BioCyc; EcoCyc:OCTAPRENYL-METHYL-METHOXY-BENZOQ-OH-MON; -.
DR BioCyc; MetaCyc:OCTAPRENYL-METHYL-METHOXY-BENZOQ-OH-MON; -.
DR BRENDA; 1.14.99.60; 2026.
DR UniPathway; UPA00232; -.
DR PRO; PR:P75728; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; IDA:EcoCyc.
DR GO; GO:0008682; F:3-demethoxyubiquinol 3-hydroxylase activity; IMP:EcoliWiki.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; ISS:EcoCyc.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018168; Ubi_Hdrlase_CS.
DR InterPro; IPR010971; UbiH/COQ6.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01988; Ubi-OHases; 1.
DR PROSITE; PS01304; UBIH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Monooxygenase; Oxidoreductase;
KW Reference proteome; Ubiquinone biosynthesis.
FT CHAIN 1..391
FT /note="3-demethoxyubiquinol 3-hydroxylase"
FT /id="PRO_0000207587"
SQ SEQUENCE 391 AA; 42953 MW; 05325684AAB6D30A CRC64;
MTNQPTEIAI VGGGMVGGAL ALGLAQHGFA VTVIEHAEPA PFVADSQPDV RISAISAASV
SLLKGLGVWD AVQAMRCHPY RRLETWEWET AHVVFDAAEL KLPLLGYMVE NTVLQQALWQ
ALEAHPKVTL RVPGSLIALH RHDDLQELEL KGGEVIRAKL VIGADGANSQ VRQMAGIGVH
AWQYAQSCML ISVQCENDPG DSTWQQFTPD GPRAFLPLFD NWASLVWYDS PARIRQLQNM
NMAQLQAEIA KHFPSRLGYV TPLAAGAFPL TRRHALQYVQ PGLALVGDAA HTIHPLAGQG
VNLGYRDVDA LIDVLVNARS YGEAWASYPV LKRYQMRRMA DNFIMQSGMD LFYAGFSNNL
PPLRFMRNLG LMAAERAGVL KRQALKYALG L
