Q9UIJ7 · KAD3_HUMAN
- ProteinGTP:AMP phosphotransferase AK3, mitochondrial
- GeneAK3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids227 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mitochondrial adenylate kinase with a specific GTP:AMP phosphotransferase activity (PubMed:11485571, PubMed:32822537).
Could also use ITP as phosphate donor (PubMed:11485571).
Its physiological function is to recycle GTP into GDP which is necessary for the TCA cycle in the mitochondrial matrix (Probable)
Could also use ITP as phosphate donor (PubMed:11485571).
Its physiological function is to recycle GTP into GDP which is necessary for the TCA cycle in the mitochondrial matrix (Probable)
Catalytic activity
- a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP
- AMP + GTP = ADP + GDP
- AMP + ITP = ADP + IDP
Activity regulation
Inhibited by ATP.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
10 μM | GTP |
kcat is 57 sec-1 with GTP as phosphate donor.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 17 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 19 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 20 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 21 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 22 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 38 | AMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 43 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 64 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 91 | AMP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 94 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 98 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 128 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 138 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 139 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 161 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 172 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 201 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | GTP binding | |
Molecular Function | nucleoside triphosphate adenylate kinase activity | |
Biological Process | ADP biosynthetic process | |
Biological Process | AMP metabolic process | |
Biological Process | blood coagulation | |
Biological Process | GTP metabolic process | |
Biological Process | ITP metabolic process | |
Biological Process | nucleoside triphosphate biosynthetic process | |
Biological Process | UTP metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGTP:AMP phosphotransferase AK3, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UIJ7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 372 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000158922 | 1-227 | UniProt | GTP:AMP phosphotransferase AK3, mitochondrial | |||
Sequence: MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFIDQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVIKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQTKPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP | |||||||
Modified residue | 20 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 34 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 37 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 38 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 57 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 64 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 64 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 80 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 80 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 174 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 174 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 189 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 189 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 203 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Interaction
Subunit
Monomer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UIJ7 | APOE P02649 | 3 | EBI-3916527, EBI-1222467 | |
BINARY | Q9UIJ7 | APPBP2 Q92624 | 6 | EBI-3916527, EBI-743771 | |
BINARY | Q9UIJ7 | BDNF P23560-2 | 3 | EBI-3916527, EBI-12275524 | |
BINARY | Q9UIJ7 | FBLN1 P23142-4 | 3 | EBI-3916527, EBI-11956479 | |
BINARY | Q9UIJ7 | GAPDH P04406 | 3 | EBI-3916527, EBI-354056 | |
BINARY | Q9UIJ7 | GRN P28799 | 3 | EBI-3916527, EBI-747754 | |
BINARY | Q9UIJ7 | HTT P42858 | 9 | EBI-3916527, EBI-466029 | |
BINARY | Q9UIJ7 | JPH3 Q8WXH2 | 3 | EBI-3916527, EBI-1055254 | |
BINARY | Q9UIJ7 | KRTAP10-8 P60410 | 3 | EBI-3916527, EBI-10171774 | |
BINARY | Q9UIJ7 | WFS1 O76024 | 3 | EBI-3916527, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 37-66 | NMP | ||||
Sequence: SSGDLLRDNMLRGTEIGVLAKAFIDQGKLI | ||||||
Region | 127-164 | LID | ||||
Sequence: ARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDD |
Domain
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis.
Sequence similarities
Belongs to the adenylate kinase family. AK3 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9UIJ7-1
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
- Length227
- Mass (Da)25,565
- Last updated2007-01-23 v4
- Checksum98A0EDF4FD9C9CEF
Q9UIJ7-2
- Name2
- Differences from canonical
- 1-70: Missing
Q9UIJ7-3
- Name3
- Differences from canonical
- 51-90: Missing
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043090 | 1-70 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 5 | in Ref. 1; BAA87913 | ||||
Sequence: A → G | ||||||
Sequence conflict | 38 | in Ref. 1; BAA87913 | ||||
Sequence: S → R | ||||||
Alternative sequence | VSP_044876 | 51-90 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 57 | in Ref. 1; BAA87913 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 69-71 | in Ref. 1; BAA87913 | ||||
Sequence: DVM → YVT | ||||||
Sequence conflict | 181 | in Ref. 3; BAG60470 | ||||
Sequence: K → E |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB021870 EMBL· GenBank· DDBJ | BAA87913.1 EMBL· GenBank· DDBJ | mRNA | ||
AF183419 EMBL· GenBank· DDBJ | AAG09688.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001553 EMBL· GenBank· DDBJ | BAA91753.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001951 EMBL· GenBank· DDBJ | BAA91996.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027534 EMBL· GenBank· DDBJ | BAB55183.1 EMBL· GenBank· DDBJ | mRNA | ||
AK098205 EMBL· GenBank· DDBJ | BAG53592.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298200 EMBL· GenBank· DDBJ | BAG60470.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136231 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL353151 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471071 EMBL· GenBank· DDBJ | EAW58779.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471071 EMBL· GenBank· DDBJ | EAW58780.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471071 EMBL· GenBank· DDBJ | EAW58781.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC013771 EMBL· GenBank· DDBJ | AAH13771.1 EMBL· GenBank· DDBJ | mRNA |