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UniProtKB/Swiss-Prot entry O31678


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name QUEF_BACSU
Primary accession number O31678
Secondary accession numbers None
Integrated into Swiss-Prot on November 22, 2005
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 45)
Name and origin of the protein
Protein name NADPH-dependent 7-cyano-7-deazaguanine reductase
Synonyms EC 1.7.1.13
7-cyano-7-carbaguanine reductase
PreQ(0) reductase
NADPH-dependent nitrile oxidoreductase
Gene name
Name: queF
Synonyms: ykvM
OrderedLocusNames: BSU13750
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[2]
INVOLVEMENT IN QUEUOSINE BIOSYNTHESIS, AND GENE NAME.
DOI=10.1074/jbc.M310858200; PubMed=14660578 [NCBI, ExPASy, EBI, Israel, Japan]
Reader J.S., Metzgar D., Schimmel P., de Crecy-Lagard V.;
"Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine.";
J. Biol. Chem. 279:6280-6285(2004).
[3]
FUNCTION, AND SUBUNIT.
DOI=10.1073/pnas.0408056102; PubMed=15767583 [NCBI, ExPASy, EBI, Israel, Japan]
Van Lanen S.G., Reader J.S., Swairjo M.A., de Crecy-Lagard V., Lee B., Iwata-Reuyl D.;
"From cyclohydrolase to oxidoreductase: discovery of nitrile reductase activity in a common fold.";
Proc. Natl. Acad. Sci. U.S.A. 102:4264-4269(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z99111; CAB13248.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D69868; D69868.
RefSeq NP_389258.1; -.
3D structure databases
ModBase O31678.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1377-MON; -.
Organism-specific databases
SubtiList BG13315; queF. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0046857; Molecular function: oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor (inferred from electronic annotation from HAMAP).
GO:0033739; Molecular function: queuine synthase activity (inferred from electronic annotation from EC).
GO:0008616; Biological process: queuosine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00818; -; 1.
PBIL [Tree]
InterPro IPR016856; CN_OxRdtase_NADPH-dep_QueF.
IPR001474; GTP_CycOHase_I.
Graphical view of domain structure.
Pfam PF01227; GTP_cyclohydroI; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF027377; Nitrile_oxidored_QueF; 1.
TIGRFAMs TIGR03139; QueF-II; 1.
BLOCKS O31678.
Genome annotation databases
GeneID 939296; -.
GenomeReviews AL009126_GR; BSU13750.
KEGG bsu:BSU13750; -.
NMPDR fig|224308.1.peg.1377; -.
Phylogenomic databases
HOGENOM O31678; -.
Genome annotation databases
CMR O31678; BSU13750.
Other
ProtoNet O31678.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   165  165     NADPH-dependent 7-cyano-7-deazaguanine reductase. PRO_0000162957
Sequence information
Length: 165 AA [This is the length of the unprocessed precursor] Molecular weight: 19375 Da [This is the MW of the unprocessed precursor] CRC64: E1CEF14D1EAA007D [This is a checksum on the sequence]
        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 

O31678 in FASTA format

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