F4KEV7 · FHIT_ARATH
- ProteinBifunctional bis(5'-adenosyl)-triphosphatase/adenylylsulfatase FHIT
- GeneFHIT
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids180 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Possesses dinucleoside triphosphate hydrolase activity (PubMed:18694747).
Cleaves P1-P3-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP (PubMed:18694747).
Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate (PubMed:18694747).
Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:18694747).
Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate (PubMed:26181368).
Cleaves P1-P3-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP (PubMed:18694747).
Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate (PubMed:18694747).
Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:18694747).
Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate (PubMed:26181368).
Catalytic activity
- H2O + P1,P3-bis(5'-adenosyl) triphosphate = ADP + AMP + 2 H+
- adenosine 5'-phosphoramidate + H2O = AMP + NH4+
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3 μM | adenosine 5'-phosphoramidate | 6.8 |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 52 | substrate | ||||
Sequence: N | ||||||
Binding site | 108 | substrate | ||||
Sequence: Q | ||||||
Active site | 121 | Tele-AMP-histidine intermediate | ||||
Sequence: H | ||||||
Binding site | 123 | substrate | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | adenosine 5'-monophosphoramidase activity | |
Molecular Function | adenylylsulfatase activity | |
Molecular Function | adenylylsulfate-ammonia adenylyltransferase activity | |
Molecular Function | bis(5'-adenosyl)-triphosphatase activity | |
Molecular Function | nucleotide binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional bis(5'-adenosyl)-triphosphatase/adenylylsulfatase FHIT
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionF4KEV7
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000436745 | 1-180 | Bifunctional bis(5'-adenosyl)-triphosphatase/adenylylsulfatase FHIT | |||
Sequence: MLNLQVTGKTILSSIRCQRKMSSTCSSYAFGPYKIDPREVFYATPLSYAMVNLRPLLPAHVLVCPRRLVPRFTDLTADETSDLWLTAQKVGSKLETFHNASSLTLAIQDGPQAGQTVPHVHIHILPRKGGDFEKNDEIYDALDEKEKELKQKLDLDKDRVDRSIQEMADEASQYRSLFDC |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-134 | HIT | ||||
Sequence: SYAFGPYKIDPREVFYATPLSYAMVNLRPLLPAHVLVCPRRLVPRFTDLTADETSDLWLTAQKVGSKLETFHNASSLTLAIQDGPQAGQTVPHVHIHILPRKGGDFEK | ||||||
Motif | 119-123 | Histidine triad motif | ||||
Sequence: HVHIH |
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
F4KEV7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length180
- Mass (Da)20,400
- Last updated2011-06-28 v1
- Checksum8C88EDB0E9D923FE
F4KEV7-2
- Name2
- Differences from canonical
- 1-20: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8BCS8 | A0A1P8BCS8_ARATH | FHIT | 128 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_058413 | 1-20 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 59 | in Ref. 3; AAO24535 and 4; BAF00120 | ||||
Sequence: A → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB019228 EMBL· GenBank· DDBJ | BAA96915.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED97022.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED97023.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT003103 EMBL· GenBank· DDBJ | AAO24535.1 EMBL· GenBank· DDBJ | mRNA | ||
AK228164 EMBL· GenBank· DDBJ | BAF00120.1 EMBL· GenBank· DDBJ | mRNA |