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B1LQY7 (QUEF_ECOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH-dependent 7-cyano-7-deazaguanine reductase

EC=1.7.1.13
Alternative name(s):
7-cyano-7-carbaguanine reductase
NADPH-dependent nitrile oxidoreductase
PreQ(0) reductase
Gene names
Name:queF
Ordered Locus Names:EcSMS35_2934
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1) By similarity. HAMAP-Rule MF_00817

Catalytic activity

7-aminomethyl-7-carbaguanine + 2 NADP+ = 7-cyano-7-carbaguanine + 2 NADPH. HAMAP-Rule MF_00817

Pathway

tRNA modification; tRNA-queuosine biosynthesis. HAMAP-Rule MF_00817

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00817

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00817.

Sequence similarities

Belongs to the GTP cyclohydrolase I family. QueF type 2 subfamily.

Ontologies

Keywords
   Biological processQueuosine biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processqueuosine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor

Inferred from electronic annotation. Source: InterPro

preQ1 synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282NADPH-dependent 7-cyano-7-deazaguanine reductase HAMAP-Rule MF_00817
PRO_1000213066

Regions

Nucleotide binding90 – 912NADPH By similarity
Nucleotide binding258 – 2592NADPH By similarity
Region88 – 903Substrate binding By similarity
Region229 – 2302Substrate binding By similarity

Sites

Active site1901Thioimide intermediate By similarity
Active site1971Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LQY7 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 83B7798A769831DE

FASTA28232,529
        10         20         30         40         50         60 
MSSYANHQAL AGLTLGKSTD YRDTYDASLL QGVPRSLNRD PLGLKADNLP FHGTDIWTLY 

        70         80         90        100        110        120 
ELSWLNAKGL PQVAVGHVEL DYTSANLIES KSFKLYLNSF NQTRFNNWDE VRQTLERDLS 

       130        140        150        160        170        180 
TCAQGKVSVA LYRLDELEGQ PIGHFNGTCI DDQDITIDNY EFTTDYLENA TSGEKVVEET 

       190        200        210        220        230        240 
LVSHLLKSNC LITHQPDWGS IQIQYRGRQI DREKLLRYLV SFRHHNEFHE QCVERIFNDL 

       250        260        270        280 
LRFCQPEKLS VYARYTRRGG LDINPWRSNS DFVPSTTRLV RQ 

« Hide

References

[1]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SMS-3-5 / SECEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000970 Genomic DNA. Translation: ACB19943.1.
RefSeqYP_001744958.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LQY7.
SMRB1LQY7. Positions 21-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439855.EcSMS35_2934.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB19943; ACB19943; EcSMS35_2934.
GeneID6142799.
KEGGecm:EcSMS35_2934.
PATRIC18434782. VBIEscCol6161_3090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0780.
HOGENOMHOG000273755.
KOK06879.
OMAIFCDLMH.
OrthoDBEOG6D5G0M.

Enzyme and pathway databases

BioCycECOL439855:GHHB-2930-MONOMER.
UniPathwayUPA00392.

Family and domain databases

HAMAPMF_00817. QueF_type2.
InterProIPR029500. QueF.
IPR029139. QueF_N.
IPR016428. QueF_type2.
[Graphical view]
PfamPF14489. QueF. 1 hit.
PF14819. QueF_N. 1 hit.
[Graphical view]
PIRSFPIRSF004750. Nitrile_oxidored_YqcD_prd. 1 hit.
TIGRFAMsTIGR03138. QueF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQUEF_ECOSM
AccessionPrimary (citable) accession number: B1LQY7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: April 29, 2008
Last modified: June 11, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways