Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-octaprenylphenol hydroxylase

Gene

ubiI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Miscellaneous

Partially complements the C5-hydroxylation defect of S.cerevisiae cells lacking COQ6.1 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi49 – 52FADCurated4
Nucleotide bindingi297 – 303FADCurated7

GO - Molecular functioni

GO - Biological processi

  • ubiquinone biosynthetic process Source: EcoCyc

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processUbiquinone biosynthesis
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:EG11333-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi301 – 303GVN → AVD: Leads to the same phenotype as the ubiI deletion mutant, indicating a strongly impaired catalytic activity. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002075801 – 4002-octaprenylphenol hydroxylaseAdd BLAST400

Proteomic databases

PaxDbiP25535
PRIDEiP25535

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi4262344, 10 interactors
IntActiP25535, 3 interactors
STRINGi316385.ECDH10B_3080

Structurei

Secondary structure

1400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Helixi13 – 22Combined sources10
Beta strandi29 – 32Combined sources4
Beta strandi50 – 53Combined sources4
Helixi55 – 63Combined sources9
Helixi67 – 73Combined sources7
Beta strandi76 – 78Combined sources3
Beta strandi80 – 88Combined sources9
Beta strandi91 – 96Combined sources6
Helixi97 – 99Combined sources3
Beta strandi102 – 109Combined sources8
Helixi110 – 122Combined sources13
Beta strandi127 – 132Combined sources6
Beta strandi135 – 140Combined sources6
Beta strandi145 – 149Combined sources5
Beta strandi154 – 162Combined sources9
Helixi168 – 173Combined sources6
Beta strandi179 – 196Combined sources18
Beta strandi201 – 207Combined sources7
Beta strandi210 – 216Combined sources7
Beta strandi222 – 229Combined sources8
Helixi231 – 239Combined sources9
Helixi242 – 252Combined sources11
Turni253 – 257Combined sources5
Beta strandi258 – 262Combined sources5
Beta strandi267 – 275Combined sources9
Beta strandi279 – 281Combined sources3
Beta strandi284 – 286Combined sources3
Helixi297 – 299Combined sources3
Helixi302 – 321Combined sources20
Helixi329 – 347Combined sources19
Helixi352 – 356Combined sources5

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the UbiH/COQ6 family.Curated

Phylogenomic databases

eggNOGiENOG4105EAK Bacteria
COG0654 LUCA
HOGENOMiHOG000255771
InParanoidiP25535
KOiK18800
OMAiCHPVGGQ
PhylomeDBiP25535

Family and domain databases

Gene3Di3.50.50.60, 3 hits
InterProiView protein in InterPro
IPR002938 FAD-bd
IPR036188 FAD/NAD-bd_sf
IPR018168 Ubi_Hdrlase_CS
IPR010971 UbiH/COQ6
PfamiView protein in Pfam
PF01494 FAD_binding_3, 1 hit
SUPFAMiSSF51905 SSF51905, 2 hits
TIGRFAMsiTIGR01988 Ubi-OHases, 1 hit
PROSITEiView protein in PROSITE
PS01304 UBIH, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti26G → A in BAA14327 (PubMed:1339425).Curated1
Sequence conflicti383P → A in BAA14327 (PubMed:1339425).Curated1

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
PATRICifig|511145.12.peg.3001

Entry informationi

Entry nameiUBII_ECOLI
AccessioniPrimary (citable) accession number: P25535
Secondary accession number(s): Q2M9T5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: August 29, 2003
Last modified: March 28, 2018
This is version 133 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health