UniProtKB - Q46920 (QUEF_ECOLI)
Protein
NADPH-dependent 7-cyano-7-deazaguanine reductase
Gene
queF
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late step in the queuosine pathway. Is highly specific for its natural substrate preQ0, since it cannot use various aliphatic, aromatic, benzylic and heterocyclic nitriles, such as acetonitrile, benzonitrile, benzylcyanide and 2-cyanopyrrole, although it can reduce the substrate analog 5-cyanopyrrolo[2,3-d]pyrimidin-4-one with lesser efficiency.3 Publications
Catalytic activityi
- EC:1.7.1.132 Publications
Kineticsi
KM for preQ0 appears to be inferior to 1.5 µM, and kcat is 0.1268 sec(-1) (PubMed:23410922). kcat is 6.5 min(-1) with preQ0 as substrate and 3.6 min(-1) with 5-cyanopyrrolo[2,3-d]pyrimidin-4-one as substrate (PubMed:23595998).2 Publications
- KM=36 µM for NADPH3 Publications
- KM=6.0 µM for NADPH3 Publications
- KM=6.1 µM for 7-cyano-7-deazaguanine3 Publications
- KM=176 µM for 5-cyanopyrrolo[2,3-d]pyrimidin-4-one3 Publications
pH dependencei
Optimum pH is 7. Retains less than 20% of activity at pH 9 (PubMed:23410922).1 Publication
Temperature dependencei
Optimum temperature is 37 degrees Celsius. Displays a half life of 28.2 hours and 12.8 hours at 37 and 40 degrees Celsius, respectively, but at 50 degrees Celsius the half life time drops to 6 minutes (PubMed:23410922).1 Publication
: tRNA-queuosine biosynthesis Pathwayi
This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 190 | Thioimide intermediate1 Publication | 1 | |
Active sitei | 197 | Proton donor1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 90 – 91 | NADPHBy similarity | 2 | |
Nucleotide bindingi | 258 – 259 | NADPHBy similarity | 2 |
GO - Molecular functioni
- oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor Source: InterPro
- preQ1 synthase activity Source: EcoCyc
GO - Biological processi
- queuosine biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Queuosine biosynthesis |
Ligand | NADP |
Enzyme and pathway databases
BioCyci | EcoCyc:G7452-MONOMER MetaCyc:G7452-MONOMER |
BRENDAi | 1.7.1.13, 2026 |
UniPathwayi | UPA00392 |
Names & Taxonomyi
Protein namesi | Recommended 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 namesi | Name:queF Synonyms:yqcD Ordered Locus Names:b2794, JW2765 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm Curated
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 89 | E → A or L: Drastic decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 90 | S → A: 9-fold decrease in specific activity. 1 Publication | 1 | |
Mutagenesisi | 190 | C → A: Loss of catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 197 | D → N: Loss of catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 228 | F → W: 11-fold decrease in specific activity. 1 Publication | 1 | |
Mutagenesisi | 229 | H → A: 6.5-fold decrease in specific activity. 1 Publication | 1 | |
Mutagenesisi | 230 | E → Q: 26-fold decrease in specific activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000163031 | 1 – 282 | NADPH-dependent 7-cyano-7-deazaguanine reductaseAdd BLAST | 282 |
Proteomic databases
jPOSTi | Q46920 |
PaxDbi | Q46920 |
PRIDEi | Q46920 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4262149, 54 interactors |
DIPi | DIP-12848N |
IntActi | Q46920, 6 interactors |
STRINGi | 511145.b2794 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 88 – 90 | Substrate bindingCurated | 3 | |
Regioni | 229 – 230 | Substrate bindingCurated | 2 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0780, Bacteria COG2904, Bacteria |
HOGENOMi | CLU_054738_0_0_6 |
InParanoidi | Q46920 |
Family and domain databases
Gene3Di | 3.30.1130.10, 2 hits |
HAMAPi | MF_00817, QueF_type2, 1 hit |
InterProi | View protein in InterPro IPR043133, GTP-CH-I_C/QueF IPR029500, QueF IPR029139, QueF_N IPR016428, QueF_type2 |
Pfami | View protein in Pfam PF14489, QueF, 1 hit PF14819, QueF_N, 1 hit |
PIRSFi | PIRSF004750, Nitrile_oxidored_YqcD_prd, 1 hit |
TIGRFAMsi | TIGR03138, QueF, 1 hit |
i Sequence
Sequence statusi: Complete.
Q46920-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSSYANHQAL AGLTLGKSTD YRDTYDASLL QGVPRSLNRD PLGLKADNLP
60 70 80 90 100
FHGTDIWTLY ELSWLNAKGL PQVAVGHVEL DYTSVNLIES KSFKLYLNSF
110 120 130 140 150
NQTRFNNWDE VRQTLERDLS TCAQGKISVA LYRLDELEGQ PIGHFNGTCI
160 170 180 190 200
DDQDITIDNY EFTTDYLENA TCGEKVVEET LVSHLLKSNC LITHQPDWGS
210 220 230 240 250
LQIQYRGRQI DREKLLRYLV SFRHHNEFHE QCVERIFNDL LRFCQPEKLS
260 270 280
VYARYTRRGG LDINPWRSNS DFVPSTTRLV RQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U29581 Genomic DNA Translation: AAB40444.1 U00096 Genomic DNA Translation: AAC75836.1 AP009048 Genomic DNA Translation: BAE76866.1 |
PIRi | F65061 |
RefSeqi | NP_417274.1, NC_000913.3 WP_000100421.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75836; AAC75836; b2794 BAE76866; BAE76866; BAE76866 |
GeneIDi | 57730402 947270 |
KEGGi | ecj:JW2765 eco:b2794 |
PATRICi | fig|1411691.4.peg.3939 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U29581 Genomic DNA Translation: AAB40444.1 U00096 Genomic DNA Translation: AAC75836.1 AP009048 Genomic DNA Translation: BAE76866.1 |
PIRi | F65061 |
RefSeqi | NP_417274.1, NC_000913.3 WP_000100421.1, NZ_LN832404.1 |
3D structure databases
SMRi | Q46920 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4262149, 54 interactors |
DIPi | DIP-12848N |
IntActi | Q46920, 6 interactors |
STRINGi | 511145.b2794 |
Proteomic databases
jPOSTi | Q46920 |
PaxDbi | Q46920 |
PRIDEi | Q46920 |
Genome annotation databases
EnsemblBacteriai | AAC75836; AAC75836; b2794 BAE76866; BAE76866; BAE76866 |
GeneIDi | 57730402 947270 |
KEGGi | ecj:JW2765 eco:b2794 |
PATRICi | fig|1411691.4.peg.3939 |
Organism-specific databases
EchoBASEi | EB2965 |
Phylogenomic databases
eggNOGi | COG0780, Bacteria COG2904, Bacteria |
HOGENOMi | CLU_054738_0_0_6 |
InParanoidi | Q46920 |
Enzyme and pathway databases
UniPathwayi | UPA00392 |
BioCyci | EcoCyc:G7452-MONOMER MetaCyc:G7452-MONOMER |
BRENDAi | 1.7.1.13, 2026 |
Miscellaneous databases
PROi | PR:Q46920 |
Family and domain databases
Gene3Di | 3.30.1130.10, 2 hits |
HAMAPi | MF_00817, QueF_type2, 1 hit |
InterProi | View protein in InterPro IPR043133, GTP-CH-I_C/QueF IPR029500, QueF IPR029139, QueF_N IPR016428, QueF_type2 |
Pfami | View protein in Pfam PF14489, QueF, 1 hit PF14819, QueF_N, 1 hit |
PIRSFi | PIRSF004750, Nitrile_oxidored_YqcD_prd, 1 hit |
TIGRFAMsi | TIGR03138, QueF, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | QUEF_ECOLI | |
Accessioni | Q46920Primary (citable) accession number: Q46920 Secondary accession number(s): Q2MA40 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | November 1, 1996 | |
Last modified: | February 10, 2021 | |
This is version 146 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families