UBII_ECOLI
ID UBII_ECOLI Reviewed; 400 AA.
AC P25535; Q2M9T5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=2-octaprenylphenol hydroxylase;
DE EC=1.14.13.240 {ECO:0000269|PubMed:23709220};
DE AltName: Full=2-polyprenylphenol 6-hydroxylase {ECO:0000305};
GN Name=ubiI {ECO:0000303|PubMed:23709220}; Synonyms=visC;
GN OrderedLocusNames=b2906, JW2874;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33694 / HB101;
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 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-365, FUNCTION AS A
RP 2-OCTAPRENYLPHENOL HYDROXYLASE, CATALYTIC ACTIVITY, ROLE IN UBIQUINONE
RP BIOSYNTHESIS, GENE NAME, COFACTOR, DISRUPTION PHENOTYPE, PATHWAY, SUBUNIT,
RP AND MUTAGENESIS OF 301-GLY--ASN-303.
RC STRAIN=K12;
RX PubMed=23709220; DOI=10.1074/jbc.m113.480368;
RA Hajj Chehade M., Loiseau L., Lombard M., Pecqueur L., Ismail A., Smadja M.,
RA Golinelli-Pimpaneau B., Mellot-Draznieks C., Hamelin O., Aussel L.,
RA Kieffer-Jaquinod S., Labessan N., Barras F., Fontecave M., Pierrel F.;
RT "ubiI, a new gene in Escherichia coli coenzyme Q biosynthesis, is involved
RT in aerobic C5-hydroxylation.";
RL J. Biol. Chem. 288:20085-20092(2013).
CC -!- FUNCTION: FAD-dependent monooxygenase required for the aerobic
CC hydroxylation of 2-octaprenylphenol to 2-octaprenyl-6-hydroxy-phenol,
CC the first hydroxylation step in coenzyme Q (ubiquinone) biosynthesis.
CC {ECO:0000269|PubMed:23709220}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-all-trans-octaprenylphenol + H(+) + NADPH + O2 = 3-(all-
CC trans-octaprenyl)benzene-1,2-diol + H2O + NADP(+);
CC Xref=Rhea:RHEA:27790, ChEBI:CHEBI:1233, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:40407,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.240;
CC Evidence={ECO:0000269|PubMed:23709220};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-all-trans-polyprenylphenol + H(+) + NADPH + O2 = a 3-(all-
CC trans-polyprenyl)benzene-1,2-diol + H2O + NADP(+);
CC Xref=Rhea:RHEA:55892, Rhea:RHEA-COMP:9516, Rhea:RHEA-COMP:9550,
CC ChEBI:CHEBI:1269, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:62729; EC=1.14.13.240;
CC Evidence={ECO:0000269|PubMed:23709220};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:23709220};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000269|PubMed:23709220}.
CC -!- SUBUNIT: Homotetramer (Probable). Component of the Ubi complex
CC metabolon, which regroups five ubiquinone biosynthesis proteins (UbiE,
CC UbiF, UbiG, UbiH and UbiI) and two accessory factors (UbiK and the
CC lipid-binding protein UbiJ) (PubMed:30686758).
CC {ECO:0000269|PubMed:30686758, ECO:0000305|PubMed:23709220}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30686758}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a low level of
CC coenzyme Q8 in aerobic conditions, and accumulate a compound derived
CC from the Q biosynthetic pathway which was identified as 3-octaprenyl-4-
CC hydroxyphenol. When grown anaerobically, they have a content of Q8
CC comparable with that in wild-type cells and do not accumulate 3-
CC octaprenyl-4-hydroxyphenol. The levels of the isoprenoid
CC naphthoquinones, demethylmenaquinone and menaquinone (MK8) are not
CC affected in the deletion mutant under aerobic conditions.
CC {ECO:0000269|PubMed:23709220}.
CC -!- MISCELLANEOUS: Partially complements the C5-hydroxylation defect of
CC S.cerevisiae cells lacking COQ6. {ECO:0000305|PubMed:23709220}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D90281; BAA14327.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69074.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75944.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76971.1; -; Genomic_DNA.
DR PIR; B65075; B65075.
DR RefSeq; NP_417382.1; NC_000913.3.
DR RefSeq; WP_001192229.1; NZ_LN832404.1.
DR PDB; 4K22; X-ray; 2.00 A; A/B=1-365.
DR PDBsum; 4K22; -.
DR AlphaFoldDB; P25535; -.
DR SMR; P25535; -.
DR BioGRID; 4262344; 10.
DR BioGRID; 851711; 1.
DR IntAct; P25535; 3.
DR STRING; 511145.b2906; -.
DR jPOST; P25535; -.
DR PaxDb; P25535; -.
DR PRIDE; P25535; -.
DR EnsemblBacteria; AAC75944; AAC75944; b2906.
DR EnsemblBacteria; BAE76971; BAE76971; BAE76971.
DR GeneID; 947389; -.
DR KEGG; ecj:JW2874; -.
DR KEGG; eco:b2906; -.
DR PATRIC; fig|511145.12.peg.3001; -.
DR EchoBASE; EB1309; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_3_6; -.
DR InParanoid; P25535; -.
DR OMA; SDVACII; -.
DR PhylomeDB; P25535; -.
DR BioCyc; EcoCyc:EG11333-MON; -.
DR BioCyc; MetaCyc:EG11333-MON; -.
DR BRENDA; 1.14.13.240; 2026.
DR UniPathway; UPA00232; -.
DR PHI-base; PHI:7028; -.
DR PRO; PR:P25535; -.
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:0019168; F:2-octaprenylphenol 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: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 3D-structure; Cytoplasm; FAD; Flavoprotein; Monooxygenase; Oxidoreductase;
KW Reference proteome; Ubiquinone biosynthesis.
FT CHAIN 1..400
FT /note="2-octaprenylphenol hydroxylase"
FT /id="PRO_0000207580"
FT BINDING 49..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305"
FT BINDING 297..303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305"
FT MUTAGEN 301..303
FT /note="GVN->AVD: Leads to the same phenotype as the ubiI
FT deletion mutant, indicating a strongly impaired catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:23709220"
FT CONFLICT 26
FT /note="G -> A (in Ref. 1; BAA14327)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="P -> A (in Ref. 1; BAA14327)"
FT /evidence="ECO:0000305"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 179..196
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:4K22"
FT TURN 253..257
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:4K22"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 302..321
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 329..347
FT /evidence="ECO:0007829|PDB:4K22"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:4K22"
SQ SEQUENCE 400 AA; 44245 MW; 5AECB27DC7FCED94 CRC64;
MQSVDVAIVG GGMVGLAVAC GLQGSGLRVA VLEQRVQEPL AANAPPQLRV SAINAASEKL
LTRLGVWQDI LSRRASCYHG MEVWDKDSFG HISFDDQSMG YSHLGHIVEN SVIHYALWNK
AHQSSDITLL APAELQQVAW GENETFLTLK DGSMLTARLV IGADGANSWL RNKADIPLTF
WDYQHHALVA TIRTEEPHDA VARQVFHGEG ILAFLPLSDP HLCSIVWSLS PEEAQRMQQA
SEDEFNRALN IAFDNRLGLC KVESARQVFP LTGRYARQFA SHRLALVGDA AHTIHPLAGQ
GVNLGFMDAA ELIAELKRLH RQGKDIGQYI YLRRYERSRK HSAALMLAGM QGFRDLFSGT
NPAKKLLRDI GLKLADTLPG VKPQLIRQAM GLNDLPEWLR
