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UniProtKB/Swiss-Prot entry A1TLC4


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

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Entry information
Entry name QUEF_ACIAC
Primary accession number A1TLC4
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on February 6, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 20)
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: Aave_1170
From
Acidovorax avenae subsp. citrulli (strain AAC00-1) [TaxID: 397945] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Acidovorax.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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
CP000512; ABM31762.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_969536.1; -.
3D structure databases
ModBase A1TLC4.
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.
ProtoNet A1TLC4.
Genome annotation databases
GeneID 4665187; -.
GenomeReviews CP000512_GR; Aave_1170.
KEGG aav:Aave_1170; -.
NMPDR fig|397945.5.peg.1021; -.
CMR A1TLC4; Aave_1170.
Other
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   281  281     NADPH-dependent 7-cyano-7-deazaguanine reductase. PRO_1000062324
Sequence information
Length: 281 AA [This is the length of the unprocessed precursor] Molecular weight: 31823 Da [This is the MW of the unprocessed precursor] CRC64: EC5942465BC95F6E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNTPDQSQLG RVSGYADQYD ASLLFPLPRQ PKRHEIGVTG TPPFFGADLW TAFELSWLNL 

        70         80         90        100        110        120 
RGKPQVALAH ITVPCETPNI IESKSFKLYL NSFNNTRFAD AAQVQTRIRT DISEAAWRGS 

       130        140        150        160        170        180 
DRQATVGVKL VLPEMFDREP VQELDGLLLD RLDVECTHYT PAPELLHANH GEAPVTETLT 

       190        200        210        220        230        240 
SHLLKSNCLV TGQPDWGSVR IEYSGAQIDQ SGLLRYLVSF RNHNEFHEQC VERIFMDLWT 

       250        260        270        280 
RCRPIKLSVY ARYTRRGGLD INPLRTSHPQ ALPANVRTAR Q 

A1TLC4 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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