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B4TUI7 (QUEF_SALSV) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 46. 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:SeSA_A3128
OrganismSalmonella schwarzengrund (strain CVM19633) [Complete proteome] [HAMAP]
Taxonomic identifier439843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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_1000213083

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
B4TUI7 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 2DDE959770707D26

FASTA28232,643
        10         20         30         40         50         60 
MSSYENHQAL DGLTLGKSTD YRDNYDASLL QGVPRSLNRD PLGLTADNLP FHGADIWTLY 

        70         80         90        100        110        120 
ELSWLNSRGL PQVAVGHVEL DYTSVNLIES KSFKLYLNSF NQTRFDTWET VRQTLERDLR 

       130        140        150        160        170        180 
ACAQGNVSVR LHRLDELEGQ PVAHFHGTCI DDQDISIDNY QFTTDYLQHA VSGEKQVEET 

       190        200        210        220        230        240 
LVSHLLKSNC LITHQPDWGS IQIQYRGRKI DREKLLRYLV SFRHHNEFHE QCVERIFNDI 

       250        260        270        280 
LRFCQPETLS VYARYTRRGG LDINPWRSNA DFVPATGRLA RQ 

« Hide

References

[1]"Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CVM19633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001127 Genomic DNA. Translation: ACF90450.1.
RefSeqYP_002115919.1. NC_011094.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439843.SeSA_A3128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF90450; ACF90450; SeSA_A3128.
PATRIC32374862. VBISalEnt87589_3152.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0780.
HOGENOMHOG000273755.
OMAIFCDLMH.
OrthoDBEOG6D5G0M.

Enzyme and pathway databases

BioCycSENT439843:GHHR-1882-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_SALSV
AccessionPrimary (citable) accession number: B4TUI7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 46 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