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O31678 (QUEF_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:ykvM
Ordered Locus Names:BSU13750
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length165 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 MF_00818

Pathway

tRNA modification; tRNA-queuosine biosynthesis. HAMAP MF_00818

Subunit structure

Homododecamer. Ref.3

Subcellular location

Cytoplasm Probable HAMAP MF_00818.

Sequence similarities

Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 165165NADPH-dependent 7-cyano-7-deazaguanine reductase HAMAP MF_00818
PRO_0000162957

Sequences

Sequence LengthMass (Da)Tools
O31678 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E1CEF14D1EAA007D

FASTA16519,375
        10         20         30         40         50         60 
MTTRKESELE GVTLLGNQGT NYLFEYAPDV LESFPNKHVN RDYFVKFNCP EFTSLCPKTG 

        70         80         90        100        110        120 
QPDFATIYIS YIPDEKMVES KSLKLYLFSF RNHGDFHEDC MNIIMNDLIE LMDPRYIEVW 

       130        140        150        160 
GKFTPRGGIS IDPYTNYGKP GTKYEKMAEY RMMNHDLYPE TIDNR

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine."
Reader J.S., Metzgar D., Schimmel P., de Crecy-Lagard V.
J. Biol. Chem. 279:6280-6285(2004) [PubMed: 14660578] [Abstract]
Cited for: INVOLVEMENT IN QUEUOSINE BIOSYNTHESIS, GENE NAME.
[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: 15767583] [Abstract]
Cited for: FUNCTION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB13248.1.
PIRD69868.
RefSeqNP_389258.1. NC_000964.3.

3D structure databases

ProteinModelPortalO31678.
SMRO31678. Positions 7-139.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001500; EBBACP00000001500; EBBACG00000001498.
GeneID939296.
GenomeReviewsGene locus BSU13750 in contig AL009126_GR.
KEGGbsu:BSU13750.
NMPDRfig|224308.1.peg.1377.
PATRIC18974519. VBIBacSub10457_1451.

Organism-specific databases

GenoListBSU13750. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002144.
HOGENOMHBG294103.
OMACINTILL.
PhylomeDBO31678.
ProtClustDBPRK13258.

Enzyme and pathway databases

BioCycBSUB:BSU13750-MONOMER.
BRENDA1.7.1.13. 700.

Family and domain databases

HAMAPMF_00818. QueF_type1.
[Tree]
InterProIPR016856. CN_OxRdtase_NADPH-dep_QueF.
IPR020602. GTP_CycHdrlase_I/CN_OxRdtase.
[Graphical view]
KOK09457.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
PIRSFPIRSF027377. Nitrile_oxidored_QueF. 1 hit.
TIGRFAMsTIGR03139. QueF-II. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQUEF_BACSU
AccessionPrimary (citable) accession number: O31678
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents