Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9KTK0 (QUEF_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. 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
Ordered Locus Names:VC_0902
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length281 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) Probable. Ref.2

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.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00817.

Sequence similarities

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

Sequence caution

The sequence AAF94064.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processQueuosine biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference 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 – 281281NADPH-dependent 7-cyano-7-deazaguanine reductase HAMAP-Rule MF_00817
PRO_0000163062

Regions

Nucleotide binding89 – 902NADPH HAMAP-Rule MF_00817
Nucleotide binding256 – 2572NADPH HAMAP-Rule MF_00817
Region87 – 893Substrate binding HAMAP-Rule MF_00817
Region227 – 2282Substrate binding HAMAP-Rule MF_00817

Sites

Active site1881Thioimide intermediate Ref.3
Active site1951Proton donor By similarity

Secondary structure

............................................... 281
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KTK0 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: 9059809F7D2D5B02

FASTA28131,969
        10         20         30         40         50         60 
MSKYSDAKEL ASLTLGKKTE YANQYDPSLL QPVPRSLNRN DLHLSATLPF QGCDIWTLYE 

        70         80         90        100        110        120 
LSWLNQKGLP QVAIGEVSIP ATSANLIESK SFKLYLNSYN QTRFASWDEV QTRLVHDLSA 

       130        140        150        160        170        180 
CAGETVTVNV KSLNEYTAEP IVTMQGECID DQDIEIANYE FDDALLQGAA QGEEVSEVLH 

       190        200        210        220        230        240 
SHLLKSNCLI TNQPDWGSVE IAYHGAKMNR EALLRYLVSF REHNEFHEQC VERIFTDIMR 

       250        260        270        280 
YCQPQSLTVY ARYTRRGGLD INPFRSSHQS APNHNQRMAR Q 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae."
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. expand/collapse author list , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.
Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39315 / El Tor Inaba N16961.
[2]"High-resolution structure of the nitrile reductase QueF combined with molecular simulations provide insight into enzyme mechanism."
Kim Y., Zhou M., Moy S., Morales J., Cunningham M.A., Joachimiak A.
J. Mol. Biol. 404:127-137(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) IN COMPLEX WITH GUANINE, FUNCTION, SUBUNIT, REACTION MECHANISM.
Strain: ATCC 39315 / El Tor Inaba N16961.
[3]"Crystal structures of 7-cyano-7-deazaguanine reductase, QueF, from Vibrio cholerae."
Center for structural genomics of infectious diseases (CSGID)
Submitted (JAN-2013) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-188; ALA-227 AND LEU-256 IN COMPLEXES WITH NADP AND SUBSTRATE PREQ0 TRAPPED AS A COVALENT THIOIMIDE INTERMEDIATE, ACTIVE SITE CYS-188.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF94064.1. Different initiation.
PIRF82265.
RefSeqNP_230549.2. NC_002505.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BP1X-ray1.53A/B/C/D1-281[»]
3RJ4X-ray1.75A/B1-281[»]
3RZPX-ray2.00A/B/C/D1-281[»]
3S19X-ray1.50A/B/C/D1-281[»]
3UXJX-ray1.40A/B/C/D1-281[»]
3UXVX-ray1.56A/B/C/D1-281[»]
4GHMX-ray1.62A/B1-281[»]
4IQIX-ray1.50A/B1-281[»]
ProteinModelPortalQ9KTK0.
SMRQ9KTK0. Positions 21-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC0902.

Protocols and materials databases

DNASU2614193.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94064; AAF94064; VC_0902.
GeneID2614193.
KEGGvch:VC0902.
PATRIC20080902. VBIVibCho83274_0859.

Phylogenomic databases

eggNOGCOG0780.
KOK06879.
OMAQCVERIY.
OrthoDBEOG6D5G0M.
ProtClustDBPRK11792.

Enzyme and pathway databases

UniPathwayUPA00392.

Family and domain databases

HAMAPMF_00817. QueF_type2.
InterProIPR016428. QueF_type2.
[Graphical view]
PIRSFPIRSF004750. Nitrile_oxidored_YqcD_prd. 1 hit.
TIGRFAMsTIGR03138. QueF. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9KTK0.

Entry information

Entry nameQUEF_VIBCH
AccessionPrimary (citable) accession number: Q9KTK0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 87 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways