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UniProtKB/Swiss-Prot entry A8A3S9

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

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Entry information
Entry name QUEF_ECOHS
Primary accession number A8A3S9
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on October 23, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 13)
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
OrderedLocusNames: EcHS_A2938
From
Escherichia coli O9:H4 (strain HS) [TaxID: 331112] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00619-08; PubMed=18676672 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.;
"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates.";
J. Bacteriol. 190:6881-6893(2008).
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
CP000802; ABV07183.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001459566.1; -.
3D structure databases
ModBase A8A3S9.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003934; Molecular function: GTP cyclohydrolase I activity (inferred from electronic annotation from InterPro).
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:0019438; Biological process: aromatic compound biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0008616; Biological process: queuosine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00817; -; 1.
PBIL [Tree]
InterPro IPR016428; CN_OxRdtase_NADPH-dep_YqcD.
IPR001474; GTP_CycOHase_I.
Graphical view of domain structure.
Pfam PF01227; GTP_cyclohydroI; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF004750; Nitrile_oxidored_YqcD_prd; 1.
TIGRFAMs TIGR03138; QueF; 1.
Genome annotation databases
GeneID 5593734; -.
GenomeReviews CP000802_GR; EcHS_A2938.
KEGG ecx:EcHS_A2938; -.
CMR A8A3S9; EcHS_A2938.
Other
ProtoNet A8A3S9.
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   282  282     NADPH-dependent 7-cyano-7-deazaguanine reductase. PRO_1000062339
Sequence information
Length: 282 AA [This is the length of the unprocessed precursor] Molecular weight: 32588 Da [This is the MW of the unprocessed precursor] CRC64: 3C2409BCCC13C12D [This is a checksum on the sequence] 
        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 IQIQYRGRQI DREKLLRYLV SFRHHNEFHE QCVERIFNDL 

       250        260        270        280 
LRFCQPEKLS VYARYTRRGG LDINPWRSNS DFVPSTTRLV RQ
A8A3S9 in FASTA format

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