Q43295 · APK1_ARATH
- ProteinAdenylyl-sulfate kinase 1, chloroplastic
- GeneAPK1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids276 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates.
Catalytic activity
- adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H+This reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.14 μM | adenosine 5'-phosphosulfate | |||||
5.3 μM | adenosine 5'-phosphosulfate | |||||
147 μM | ATP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
7.35 mmol/min/mg | |||||
20.1 mmol/min/mg |
Pathway
Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 108-116 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLSGSGKST | ||||||
Binding site | 138 | substrate | ||||
Sequence: D | ||||||
Binding site | 141 | substrate | ||||
Sequence: R | ||||||
Site | 150 | Participates in a stacking interaction with the adenine ring of adenylyl-sulfate | ||||
Sequence: F | ||||||
Binding site | 155 | substrate | ||||
Sequence: R | ||||||
Binding site | 158 | substrate | ||||
Sequence: N | ||||||
Binding site | 181-182 | substrate | ||||
Sequence: IS | ||||||
Active site | 182 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 231 | substrate | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | plastid | |
Molecular Function | adenylylsulfate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | identical protein binding | |
Biological Process | cysteine biosynthetic process | |
Biological Process | hydrogen sulfide biosynthetic process | |
Biological Process | phosphorylation | |
Biological Process | sulfate assimilation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylyl-sulfate kinase 1, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ43295
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions. Apk1 and apk2 double mutant exhibits a semi-dwarf phenotype.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 86 | Increased catalytic efficiency in oxidative conditions; when associated with Ala-119. | ||||
Sequence: C → A | ||||||
Mutagenesis | 119 | Increased catalytic efficiency in oxidative conditions; when associated with Ala-86. | ||||
Sequence: C → A | ||||||
Mutagenesis | 136 | Decreases affinity for substrate and catalytic efficiency. | ||||
Sequence: D → A or N | ||||||
Mutagenesis | 182 | No effect on catalytic activity. | ||||
Sequence: S → C or F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 19 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-38 | Chloroplast | ||||
Sequence: MIAAGAKSLLGLSMASPKGIFDSNSMSNSRSVVVVRAC | ||||||
Chain | PRO_0000006635 | 39-276 | Adenylyl-sulfate kinase 1, chloroplastic | |||
Sequence: VSMDGSQTLSHNKNGSIPEVKSINGHTGQKQGPLSTVGNSTNIKWHECSVEKVDRQRLLDQKGCVIWVTGLSGSGKSTLACALNQMLYQKGKLCYILDGDNVRHGLNRDLSFKAEDRAENIRRVGEVAKLFADAGIICIASLISPYRTDRDACRSLLPEGDFVEVFMDVPLSVCEARDPKGLYKLARAGKIKGFTGIDDPYEPPLNCEISLGREGGTSPIEMAEKVVGYLDNKGYLQA | ||||||
Disulfide bond | 86 | Interchain (with C-119) | ||||
Sequence: C | ||||||
Disulfide bond | 119 | Interchain (with C-86) | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in root vasculature, root tips, leaf epidermal and guard cells, pollen grains and funiculus of developing seeds.
Gene expression databases
Interaction
Subunit
Homodimer; disulfide-linked. Interacts with APK2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q43295 | APK1 Q43295 | 3 | EBI-4438040, EBI-4438040 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 46-74 | Disordered | ||||
Sequence: TLSHNKNGSIPEVKSINGHTGQKQGPLST |
Sequence similarities
Belongs to the APS kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length276
- Mass (Da)29,787
- Last updated1996-11-01 v1
- ChecksumCB698643AA09D811
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 41 | in Ref. 7; AAM62496 | ||||
Sequence: M → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X75782 EMBL· GenBank· DDBJ | CAA53426.1 EMBL· GenBank· DDBJ | mRNA | ||
U05238 EMBL· GenBank· DDBJ | AAC50035.1 EMBL· GenBank· DDBJ | mRNA | ||
U59759 EMBL· GenBank· DDBJ | AAC50034.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC004705 EMBL· GenBank· DDBJ | AAC24182.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC06330.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY054287 EMBL· GenBank· DDBJ | AAL06946.1 EMBL· GenBank· DDBJ | mRNA | ||
AY132010 EMBL· GenBank· DDBJ | AAM91043.1 EMBL· GenBank· DDBJ | mRNA | ||
AY085264 EMBL· GenBank· DDBJ | AAM62496.1 EMBL· GenBank· DDBJ | mRNA |