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Q46920 (QUEF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:yqcD
Ordered Locus Names:b2794, JW2765
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). Ref.3

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. Ref.3

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00817.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=36 µM for NADPH Ref.3

Ontologies

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

Inferred from mutant phenotype Ref.3. Source: EcoCyc

   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: HAMAP

preQ1 synthase activity

Inferred from direct assay Ref.3. Source: EcoCyc

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_0000163031

Sequences

Sequence LengthMass (Da)Tools
Q46920 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3C22B9BA7AA3C79D

FASTA28232,588
        10         20         30         40         50         60 
MSSYANHQAL AGLTLGKSTD YRDTYDASLL QGVPRSLNRD PLGLKADNLP FHGTDIWTLY 

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

       130        140        150        160        170        180 
TCAQGKISVA LYRLDELEGQ PIGHFNGTCI DDQDITIDNY EFTTDYLENA TCGEKVVEET 

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

       250        260        270        280 
LRFCQPEKLS VYARYTRRGG LDINPWRSNS DFVPSTTRLV RQ 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"From cyclohydrolase to oxidoreductase: discovery of nitrile reductase activity in a common fold."
Van Lanen S.G., Reader J.S., Swairjo M.A., de Crecy-Lagard V., Lee B., Iwata-Reuyl D.
Proc. Natl. Acad. Sci. U.S.A. 102:4264-4269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29581 Genomic DNA. Translation: AAB40444.1.
U00096 Genomic DNA. Translation: AAC75836.1.
AP009048 Genomic DNA. Translation: BAE76866.1.
PIRF65061.
RefSeqNP_417274.1. NC_000913.2.
YP_491002.1. NC_007779.1.

3D structure databases

ProteinModelPortalQ46920.
SMRQ46920. Positions 23-282.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-12848N.
IntActQ46920. 6 interactions.
MINTMINT-1288325.
STRING511145.b2794.

Proteomic databases

PaxDbQ46920.
PRIDEQ46920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75836; AAC75836; b2794.
BAE76866; BAE76866; BAE76866.
GeneID12933155.
947270.
KEGGecj:Y75_p2731.
eco:b2794.
PATRIC32121004. VBIEscCol129921_2894.

Organism-specific databases

EchoBASEEB2965.
EcoGeneEG13173. queF.

Phylogenomic databases

eggNOGCOG0780.
HOGENOMHOG000273755.
KOK06879.
OMAERIFCDL.
ProtClustDBPRK11792.

Enzyme and pathway databases

BioCycEcoCyc:G7452-MONOMER.
ECOL316407:JW2765-MONOMER.
MetaCyc:G7452-MONOMER.
UniPathwayUPA00392.

Gene expression databases

GenevestigatorQ46920.

Family and domain databases

HAMAPMF_00817. QueF_type2.
InterProIPR016428. CN_OxRdtase_NADPH-dep_YqcD.
IPR020602. GTP_CycHdrlase_I/CN_OxRdtase.
[Graphical view]
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
PIRSFPIRSF004750. Nitrile_oxidored_YqcD_prd. 1 hit.
TIGRFAMsTIGR03138. QueF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQUEF_ECOLI
AccessionPrimary (citable) accession number: Q46920
Secondary accession number(s): Q2MA40
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families