UBIH_ECOLI
ID UBIH_ECOLI Reviewed; 392 AA.
AC P25534; Q2M9T4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=2-octaprenyl-6-methoxyphenol hydroxylase;
DE EC=1.14.13.-;
GN Name=ubiH; Synonyms=visB; OrderedLocusNames=b2907, JW2875;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=1339425; DOI=10.1128/jb.174.22.7352-7359.1992;
RA Nakahigashi K., Miyamoto K., Nishimura K., Inokuchi H.;
RT "Isolation and characterization of a light-sensitive mutant of Escherichia
RT coli K-12 with a mutation in a gene that is required for the biosynthesis
RT of ubiquinone.";
RL J. Bacteriol. 174:7352-7359(1992).
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 FUNCTION IN UBIQUINONE BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=4572721; DOI=10.1128/jb.114.1.42-52.1973;
RA Young I.G., Stroobant P., Macdonald C.G., Gibson F.;
RT "Pathway for ubiquinone biosynthesis in Escherichia coli K-12: gene-enzyme
RT relationships and intermediates.";
RL J. Bacteriol. 114:42-52(1973).
RN [5]
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: Is likely an oxygenase that introduces the hydroxyl group at
CC carbon four of 2-octaprenyl-6-methoxyphenol resulting in the formation
CC of 2-octaprenyl-6-methoxy-1,4-benzoquinol.
CC {ECO:0000269|PubMed:4572721}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
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 P25534; P67910: hldD; NbExp=2; IntAct=EBI-559377, EBI-543760;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30686758}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are photosensitive and
CC are not able to grow with a nonfermentable source of carbon. They also
CC fail to produce ubiquinone, and accumulate 2-octaprenylphenol and 2-
CC octaprenyl-6-methoxyphenol. {ECO:0000269|PubMed:1339425,
CC ECO:0000269|PubMed:4572721}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000305}.
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DR EMBL; D90281; BAA14326.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69075.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75945.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76972.1; -; Genomic_DNA.
DR PIR; C65075; C65075.
DR RefSeq; NP_417383.1; NC_000913.3.
DR RefSeq; WP_000111195.1; NZ_LN832404.1.
DR AlphaFoldDB; P25534; -.
DR SMR; P25534; -.
DR BioGRID; 4262345; 372.
DR BioGRID; 851710; 7.
DR DIP; DIP-11071N; -.
DR IntAct; P25534; 13.
DR STRING; 511145.b2907; -.
DR jPOST; P25534; -.
DR PaxDb; P25534; -.
DR PRIDE; P25534; -.
DR EnsemblBacteria; AAC75945; AAC75945; b2907.
DR EnsemblBacteria; BAE76972; BAE76972; BAE76972.
DR GeneID; 947388; -.
DR KEGG; ecj:JW2875; -.
DR KEGG; eco:b2907; -.
DR PATRIC; fig|1411691.4.peg.3825; -.
DR EchoBASE; EB1300; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_1_6; -.
DR InParanoid; P25534; -.
DR OMA; KRWFARQ; -.
DR PhylomeDB; P25534; -.
DR BioCyc; EcoCyc:OCTAPRENYL-METHOXYPHENOL-OH-MON; -.
DR BioCyc; MetaCyc:OCTAPRENYL-METHOXYPHENOL-OH-MON; -.
DR BRENDA; 1.14.99.B5; 2026.
DR UniPathway; UPA00232; -.
DR PRO; PR:P25534; -.
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:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; IMP:EcoCyc.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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:0009416; P:response to light stimulus; IMP:EcoliWiki.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoliWiki.
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; IPR011295; UbiH.
DR InterPro; IPR010971; UbiH/COQ6.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01988; Ubi-OHases; 1.
DR TIGRFAMs; TIGR01984; UbiH; 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..392
FT /note="2-octaprenyl-6-methoxyphenol hydroxylase"
FT /id="PRO_0000207579"
FT CONFLICT 382
FT /note="L -> V (in Ref. 1; BAA14326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42288 MW; 3CCE10DAA00A7FC5 CRC64;
MSVIIVGGGM AGATLALAIS RLSHGALPVH LIEATAPESH AHPGFDGRAI ALAAGTCQQL
ARIGVWQSLA DCATAITTVH VSDRGHAGFV TLAAEDYQLA ALGQVVELHN VGQRLFALLR
KAPGVTLHCP DRVANVARTQ SHVEVTLESG ETLTGRVLVA ADGTHSALAT ACGVDWQQEP
YEQLAVIANV ATSVAHEGRA FERFTQHGPL AMLPMSDGRC SLVWCHPLER REEVLSWSDE
KFCRELQSAF GWRLGKITHA GKRSAYPLAL THAARSITHR TVLVGNAAQT LHPIAGQGFN
LGMRDVMSLA ETLTQAQERG EDMGDYGVLC RYQQRRQSDR EATIGVTDSL VHLFANRWAP
LVVGRNIGLM TMELFTPARD VLAQRTLGWV AR
