UniProtKB - P67603 (AC4CH_ECOLI)
Protein
N(4)-acetylcytidine amidohydrolase
Gene
yqfB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the hydrolysis of N4-acetylcytidine (ac4C). Can also hydrolyze N4-acetyl-2'-deoxycytidine and N4-acetylcytosine with lower efficiency. Has weaker activity towards a wide range of structurally different N4-acylated cytosines and cytidines.1 Publication
Catalytic activityi
- EC:3.5.1.135UniRule annotation1 Publication
- EC:3.5.1.135UniRule annotation1 Publication
- EC:3.5.1.135UniRule annotation1 Publication
Activity regulationi
Unaffected by known inhibitors of amidohydrolases: PMSF, p-hydroxymercuribenzoate, p-chloromercuribenzoate and EDTA.1 Publication
Kineticsi
kcat is 157 sec(-1) with N4-acetylcytidine as substrate. kcat is 101 sec(-1) with N4-acetyl-2'deoxycytidine as substrate. kcat is 70 sec(-1) with N4-acetylcytosine as substrate. kcat is 24 sec(-1) with N4-hexanoyl-2'-deoxycytidine as substrate. kcat is 90 sec(-1) with N4-acetyl-5-fluorocytosine as substrate. kcat is 75 sec(-1) with N4-isobutyryl-2'-deoxycytidine as substrate. kcat is 1.8 sec(-1) with N4-benzoylcytidine as substrate. kcat is 0.07 sec(-1) with N4-benzoyl-2'-deoxycytidine as substrate.1 Publication
- KM=62 µM for N4-acetylcytidine1 Publication
- KM=400 µM for N4-acetyl-2'deoxycytidine1 Publication
- KM=70 µM for N4-acetylcytosine1 Publication
- KM=140 µM for N4-hexanoyl-2'-deoxycytidine1 Publication
- KM=2100 µM for N4-acetyl-5-fluorocytosine1 Publication
- KM=1900 µM for N4-isobutyryl-2'-deoxycytidine1 Publication
- KM=5100 µM for N4-benzoylcytidine1 Publication
- KM=300 µM for N4-benzoyl-2'-deoxycytidine1 Publication
pH dependencei
Optimum pH is 8.0.1 Publication
Temperature dependencei
Optimum temperature is below 20 degrees Celsius.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 21 | Proton acceptorUniRule annotation1 Publication | 1 | |
Active sitei | 24 | NucleophileUniRule annotation1 Publication | 1 | |
Active sitei | 74 | Proton donorUniRule annotation1 Publication | 1 |
GO - Molecular functioni
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines Source: UniProtKB-UniRule
- N4-acetylcytidine amidohydrolase activity Source: RHEA
Keywordsi
Molecular function | Hydrolase |
Enzyme and pathway databases
BioCyci | EcoCyc:G7513-MONOMER MetaCyc:G7513-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: N(4)-acetylcytidine amidohydrolaseUniRule annotationCurated (EC:3.5.1.135UniRule annotation1 Publication)Short name: ac4C amidohydrolaseUniRule annotationCurated |
Gene namesi | Name:yqfB Ordered Locus Names:b2900, JW2868 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
The mutant lacking the yqfB gene retains the ability to grow, albeit poorly, on N4-acetylcytosine as a source of uracil.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 21 | K → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 24 | T → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 26 | R → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 27 | D → A: 2-fold decrease in catalytic efficiency toward N(4)-acetylcytidine and 3-fold decrease in catalytic efficiency toward N(4)-acetylcytosine. 1 Publication | 1 | |
Mutagenesisi | 70 | H → A: 5-fold decrease in catalytic efficiency toward N(4)-acetylcytidine and 14-fold decrease in catalytic efficiency toward N(4)-acetylcytosine. 1 Publication | 1 | |
Mutagenesisi | 74 | E → A: 73-fold decrease in catalytic efficiency toward N(4)-acetylcytidine and 143-fold decrease in catalytic efficiency toward N(4)-acetylcytosine. 1 Publication | 1 | |
Mutagenesisi | 89 | Y → A: 115-fold decrease in catalytic efficiency toward N(4)-acetylcytidine and 312-fold decrease in catalytic efficiency toward N(4)-acetylcytosine. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000214600 | 1 – 103 | N(4)-acetylcytidine amidohydrolaseAdd BLAST | 103 |
Proteomic databases
jPOSTi | P67603 |
PaxDbi | P67603 |
PRIDEi | P67603 |
Interactioni
Subunit structurei
Monomer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4263159, 125 interactors |
IntActi | P67603, 1 interactor |
STRINGi | 511145.b2900 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P67603 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P67603 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 6 – 101 | ASCHSequence analysisAdd BLAST | 96 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG3097, Bacteria |
HOGENOMi | CLU_152586_0_0_6 |
InParanoidi | P67603 |
Family and domain databases
HAMAPi | MF_00684, ac4C_amidohydr, 1 hit |
InterProi | View protein in InterPro IPR008314, AC4CH IPR007374, ASCH_domain IPR015947, PUA-like_sf |
PANTHERi | PTHR38088, PTHR38088, 1 hit |
Pfami | View protein in Pfam PF04266, ASCH, 1 hit |
PIRSFi | PIRSF029143, UCP029143, 1 hit |
SMARTi | View protein in SMART SM01022, ASCH, 1 hit |
SUPFAMi | SSF88697, SSF88697, 1 hit |
i Sequence
Sequence statusi: Complete.
P67603-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQPNDITFFQ RFQDDILAGR KTITIRDESE SHFKTGDVLR VGRFEDDGYF
60 70 80 90 100
CTIEVTATST VTLDTLTEKH AEQENMTLTE LKKVIADIYP GQTQFYVIEF
KCL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U28375 Genomic DNA Translation: AAA83081.1 U00096 Genomic DNA Translation: AAC75938.1 AP009048 Genomic DNA Translation: BAE76965.1 |
PIRi | D65074 |
RefSeqi | NP_417376.1, NC_000913.3 WP_001182957.1, NZ_SSUV01000019.1 |
Genome annotation databases
EnsemblBacteriai | AAC75938; AAC75938; b2900 BAE76965; BAE76965; BAE76965 |
GeneIDi | 56815490 947380 |
KEGGi | ecj:JW2868 eco:b2900 |
PATRICi | fig|511145.12.peg.2995 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U28375 Genomic DNA Translation: AAA83081.1 U00096 Genomic DNA Translation: AAC75938.1 AP009048 Genomic DNA Translation: BAE76965.1 |
PIRi | D65074 |
RefSeqi | NP_417376.1, NC_000913.3 WP_001182957.1, NZ_SSUV01000019.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1TE7 | NMR | - | A | 1-103 | [»] | |
SMRi | P67603 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263159, 125 interactors |
IntActi | P67603, 1 interactor |
STRINGi | 511145.b2900 |
Proteomic databases
jPOSTi | P67603 |
PaxDbi | P67603 |
PRIDEi | P67603 |
Protocols and materials databases
DNASUi | 947380 |
Genome annotation databases
EnsemblBacteriai | AAC75938; AAC75938; b2900 BAE76965; BAE76965; BAE76965 |
GeneIDi | 56815490 947380 |
KEGGi | ecj:JW2868 eco:b2900 |
PATRICi | fig|511145.12.peg.2995 |
Organism-specific databases
EchoBASEi | EB2888 |
Phylogenomic databases
eggNOGi | COG3097, Bacteria |
HOGENOMi | CLU_152586_0_0_6 |
InParanoidi | P67603 |
Enzyme and pathway databases
BioCyci | EcoCyc:G7513-MONOMER MetaCyc:G7513-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P67603 |
PROi | PR:P67603 |
Family and domain databases
HAMAPi | MF_00684, ac4C_amidohydr, 1 hit |
InterProi | View protein in InterPro IPR008314, AC4CH IPR007374, ASCH_domain IPR015947, PUA-like_sf |
PANTHERi | PTHR38088, PTHR38088, 1 hit |
Pfami | View protein in Pfam PF04266, ASCH, 1 hit |
PIRSFi | PIRSF029143, UCP029143, 1 hit |
SMARTi | View protein in SMART SM01022, ASCH, 1 hit |
SUPFAMi | SSF88697, SSF88697, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | AC4CH_ECOLI | |
Accessioni | P67603Primary (citable) accession number: P67603 Secondary accession number(s): Q2M9U1, Q46828 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 11, 2004 |
Last sequence update: | October 11, 2004 | |
Last modified: | April 7, 2021 | |
This is version 113 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
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families