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Protein

2-octaprenylphenol hydroxylase

Gene

ubiI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

FAD-dependent monooxygenase required for the aerobic hydroxylation of 2-octaprenylphenol to 2-octaprenyl-6-hydroxy-phenol, the first hydroxylation step in coenzyme Q (ubiquinone) biosynthesis.1 Publication

Cofactori

FAD1 Publication

Pathwayi: ubiquinone biosynthesis

This protein is involved in the pathway ubiquinone biosynthesis, which is part of Cofactor biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway ubiquinone biosynthesis and in Cofactor biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 524FADCurated
Nucleotide bindingi297 – 3037FADCurated

GO - Molecular functioni

GO - Biological processi

  • secondary metabolite biosynthetic process Source: GO_Central
  • ubiquinone biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Ubiquinone biosynthesis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:EG11333-MONOMER.
ECOL316407:JW2874-MONOMER.
MetaCyc:EG11333-MONOMER.
UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
2-octaprenylphenol hydroxylase (EC:1.14.13.-)
Gene namesi
Name:ubiI
Synonyms:visC
Ordered Locus Names:b2906, JW2874
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11333. visC.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene have a low level of coenzyme Q8 in aerobic conditions, and accumulate a compound derived from the Q biosynthetic pathway which was identified as 3-octaprenyl-4-hydroxyphenol. When grown anaerobically, they have a content of Q8 comparable with that in wild-type cells and do not accumulate 3-octaprenyl-4-hydroxyphenol. The levels of the isoprenoid naphthoquinones, demethylmenaquinone and menaquinone (MK8) are not affected in the deletion mutant under aerobic conditions.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi301 – 3033GVN → AVD: Leads to the same phenotype as the ubiI deletion mutant, indicating a strongly impaired catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4004002-octaprenylphenol hydroxylasePRO_0000207580Add
BLAST

Proteomic databases

PaxDbiP25535.
PRIDEiP25535.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi4262344. 9 interactions.
IntActiP25535. 3 interactions.
STRINGi511145.b2906.

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi13 – 2210Combined sources
Beta strandi29 – 324Combined sources
Beta strandi50 – 534Combined sources
Helixi55 – 639Combined sources
Helixi67 – 737Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 889Combined sources
Beta strandi91 – 966Combined sources
Helixi97 – 993Combined sources
Beta strandi102 – 1098Combined sources
Helixi110 – 12213Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi135 – 1406Combined sources
Beta strandi145 – 1495Combined sources
Beta strandi154 – 1629Combined sources
Helixi168 – 1736Combined sources
Beta strandi179 – 19618Combined sources
Beta strandi201 – 2077Combined sources
Beta strandi210 – 2167Combined sources
Beta strandi222 – 2298Combined sources
Helixi231 – 2399Combined sources
Helixi242 – 25211Combined sources
Turni253 – 2575Combined sources
Beta strandi258 – 2625Combined sources
Beta strandi267 – 2759Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi284 – 2863Combined sources
Helixi297 – 2993Combined sources
Helixi302 – 32120Combined sources
Helixi329 – 34719Combined sources
Helixi352 – 3565Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4K22X-ray2.00A/B1-365[»]
ProteinModelPortaliP25535.
SMRiP25535. Positions 1-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UbiH/COQ6 family.Curated

Phylogenomic databases

eggNOGiENOG4105EAK. Bacteria.
COG0654. LUCA.
HOGENOMiHOG000255771.
InParanoidiP25535.
KOiK18800.
OMAiDMRLGLC.
PhylomeDBiP25535.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR018168. Ubi_Hdrlase_CS.
IPR010971. UbiH/COQ6.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01988. Ubi-OHases. 1 hit.
PROSITEiPS01304. UBIH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25535-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSVDVAIVG GGMVGLAVAC GLQGSGLRVA VLEQRVQEPL AANAPPQLRV
60 70 80 90 100
SAINAASEKL LTRLGVWQDI LSRRASCYHG MEVWDKDSFG HISFDDQSMG
110 120 130 140 150
YSHLGHIVEN SVIHYALWNK AHQSSDITLL APAELQQVAW GENETFLTLK
160 170 180 190 200
DGSMLTARLV IGADGANSWL RNKADIPLTF WDYQHHALVA TIRTEEPHDA
210 220 230 240 250
VARQVFHGEG ILAFLPLSDP HLCSIVWSLS PEEAQRMQQA SEDEFNRALN
260 270 280 290 300
IAFDNRLGLC KVESARQVFP LTGRYARQFA SHRLALVGDA AHTIHPLAGQ
310 320 330 340 350
GVNLGFMDAA ELIAELKRLH RQGKDIGQYI YLRRYERSRK HSAALMLAGM
360 370 380 390 400
QGFRDLFSGT NPAKKLLRDI GLKLADTLPG VKPQLIRQAM GLNDLPEWLR
Length:400
Mass (Da):44,245
Last modified:August 29, 2003 - v2
Checksum:i5AECB27DC7FCED94
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261G → A in BAA14327 (PubMed:1339425).Curated
Sequence conflicti383 – 3831P → A in BAA14327 (PubMed:1339425).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90281 Genomic DNA. Translation: BAA14327.1.
U28377 Genomic DNA. Translation: AAA69074.1.
U00096 Genomic DNA. Translation: AAC75944.1.
AP009048 Genomic DNA. Translation: BAE76971.1.
PIRiB65075.
RefSeqiNP_417382.1. NC_000913.3.
WP_001192229.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75944; AAC75944; b2906.
BAE76971; BAE76971; BAE76971.
GeneIDi947389.
KEGGiecj:JW2874.
eco:b2906.
PATRICi32121226. VBIEscCol129921_3001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90281 Genomic DNA. Translation: BAA14327.1.
U28377 Genomic DNA. Translation: AAA69074.1.
U00096 Genomic DNA. Translation: AAC75944.1.
AP009048 Genomic DNA. Translation: BAE76971.1.
PIRiB65075.
RefSeqiNP_417382.1. NC_000913.3.
WP_001192229.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4K22X-ray2.00A/B1-365[»]
ProteinModelPortaliP25535.
SMRiP25535. Positions 1-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262344. 9 interactions.
IntActiP25535. 3 interactions.
STRINGi511145.b2906.

Proteomic databases

PaxDbiP25535.
PRIDEiP25535.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75944; AAC75944; b2906.
BAE76971; BAE76971; BAE76971.
GeneIDi947389.
KEGGiecj:JW2874.
eco:b2906.
PATRICi32121226. VBIEscCol129921_3001.

Organism-specific databases

EchoBASEiEB1309.
EcoGeneiEG11333. visC.

Phylogenomic databases

eggNOGiENOG4105EAK. Bacteria.
COG0654. LUCA.
HOGENOMiHOG000255771.
InParanoidiP25535.
KOiK18800.
OMAiDMRLGLC.
PhylomeDBiP25535.

Enzyme and pathway databases

UniPathwayiUPA00232.
BioCyciEcoCyc:EG11333-MONOMER.
ECOL316407:JW2874-MONOMER.
MetaCyc:EG11333-MONOMER.

Miscellaneous databases

PROiP25535.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR018168. Ubi_Hdrlase_CS.
IPR010971. UbiH/COQ6.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01988. Ubi-OHases. 1 hit.
PROSITEiPS01304. UBIH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBII_ECOLI
AccessioniPrimary (citable) accession number: P25535
Secondary accession number(s): Q2M9T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: August 29, 2003
Last modified: September 7, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Partially complements the C5-hydroxylation defect of S.cerevisiae cells lacking COQ6.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.