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Protein

GTP:AMP phosphotransferase AK3, mitochondrial

Gene

AK3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.UniRule annotation

Catalytic activityi

NTP + AMP = NDP + ADP.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381AMPUniRule annotation1 Publication
Binding sitei43 – 431AMPUniRule annotation
Binding sitei98 – 981AMPUniRule annotation1 Publication
Binding sitei128 – 1281GTPUniRule annotation
Binding sitei161 – 1611AMPUniRule annotation
Binding sitei172 – 1721AMPUniRule annotation
Binding sitei201 – 2011GTP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 226GTPUniRule annotation
Nucleotide bindingi64 – 663AMPUniRule annotation1 Publication
Nucleotide bindingi91 – 944AMPUniRule annotation
Nucleotide bindingi137 – 1382GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-983231. Factors involved in megakaryocyte development and platelet production.
SABIO-RKP08760.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP:AMP phosphotransferase AK3, mitochondrialUniRule annotation (EC:2.7.4.10UniRule annotation)
Alternative name(s):
Adenylate kinase 3UniRule annotation
Short name:
AK 3UniRule annotation
Adenylate kinase 3 alpha-like 1UniRule annotation
Gene namesi
Name:AK3UniRule annotation
Synonyms:AK3L1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 8

Subcellular locationi

  • Mitochondrion matrix UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedUniRule annotation1 Publication
Chaini2 – 227226GTP:AMP phosphotransferase AK3, mitochondrialPRO_0000158921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N6-succinyllysineBy similarity
Modified residuei29 – 291N6-acetyllysine; alternateBy similarity
Modified residuei29 – 291N6-succinyllysine; alternateBy similarity
Modified residuei34 – 341N6-acetyllysineBy similarity
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei64 – 641N6-acetyllysine; alternateBy similarity
Modified residuei64 – 641N6-succinyllysine; alternateBy similarity
Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
Modified residuei80 – 801N6-succinyllysine; alternateBy similarity
Modified residuei174 – 1741N6-acetyllysine; alternateBy similarity
Modified residuei174 – 1741N6-succinyllysine; alternateBy similarity
Modified residuei189 – 1891N6-acetyllysine; alternateBy similarity
Modified residuei189 – 1891N6-succinyllysine; alternateBy similarity
Modified residuei203 – 2031N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP08760.
PRIDEiP08760.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

IntActiP08760. 1 interaction.
STRINGi9913.ENSBTAP00000022789.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135Combined sources
Helixi20 – 3011Combined sources
Beta strandi34 – 374Combined sources
Helixi38 – 4710Combined sources
Helixi51 – 6111Combined sources
Helixi68 – 8215Combined sources
Beta strandi87 – 915Combined sources
Helixi96 – 1038Combined sources
Beta strandi110 – 1156Combined sources
Helixi118 – 1258Combined sources
Beta strandi128 – 1303Combined sources
Turni132 – 1343Combined sources
Beta strandi137 – 1393Combined sources
Turni140 – 1423Combined sources
Turni152 – 1543Combined sources
Helixi162 – 1643Combined sources
Helixi166 – 18924Combined sources
Beta strandi193 – 1975Combined sources
Helixi201 – 21313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AK3X-ray1.85A/B2-227[»]
ProteinModelPortaliP08760.
SMRiP08760. Positions 2-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08760.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 6630NMPbindUniRule annotation1 PublicationAdd
BLAST
Regioni127 – 16438LIDUniRule annotation1 PublicationAdd
BLAST

Domaini

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.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the adenylate kinase family. AK3 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00550000074679.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP08760.
KOiK00944.
OMAiNVPFQTI.
OrthoDBiEOG74TX0R.
TreeFamiTF312916.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/Ak4_mitochondrial.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF57774. SSF57774. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08760-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGASARLLRA AIMGAPGSGK GTVSSRITKH FELKHLSSGD LLRDNMLRGT
60 70 80 90 100
EIGVLAKTFI DQGKLIPDDV MTRLVLHELK NLTQYNWLLD GFPRTLPQAE
110 120 130 140 150
ALDRAYQIDT VINLNVPFEV IKQRLTARWI HPGSGRVYNI EFNPPKTMGI
160 170 180 190 200
DDLTGEPLVQ REDDRPETVV KRLKAYEAQT EPVLEYYRKK GVLETFSGTE
210 220
TNKIWPHVYA FLQTKLPQRS QETSVTP
Length:227
Mass (Da):25,671
Last modified:January 23, 2007 - v3
Checksum:i2C29AEF195FBFBFA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111Missing (Ref. 2) Curated
Sequence conflicti11 – 111Missing (PubMed:6088234).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25757 mRNA. Translation: AAA30705.1.
BC114157 mRNA. Translation: AAI14158.1.
D10376 Genomic DNA. Translation: BAA01210.1.
PIRiA34442.
RefSeqiNP_776662.1. NM_174237.2.
UniGeneiBt.5149.

Genome annotation databases

EnsembliENSBTAT00000022789; ENSBTAP00000022789; ENSBTAG00000017147.
GeneIDi281613.
KEGGibta:281613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25757 mRNA. Translation: AAA30705.1.
BC114157 mRNA. Translation: AAI14158.1.
D10376 Genomic DNA. Translation: BAA01210.1.
PIRiA34442.
RefSeqiNP_776662.1. NM_174237.2.
UniGeneiBt.5149.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AK3X-ray1.85A/B2-227[»]
ProteinModelPortaliP08760.
SMRiP08760. Positions 2-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08760. 1 interaction.
STRINGi9913.ENSBTAP00000022789.

Proteomic databases

PaxDbiP08760.
PRIDEiP08760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022789; ENSBTAP00000022789; ENSBTAG00000017147.
GeneIDi281613.
KEGGibta:281613.

Organism-specific databases

CTDi50808.

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00550000074679.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP08760.
KOiK00944.
OMAiNVPFQTI.
OrthoDBiEOG74TX0R.
TreeFamiTF312916.

Enzyme and pathway databases

ReactomeiR-BTA-983231. Factors involved in megakaryocyte development and platelet production.
SABIO-RKP08760.

Miscellaneous databases

EvolutionaryTraceiP08760.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/Ak4_mitochondrial.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF57774. SSF57774. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of cDNA for mitochondrial GTP:AMP phosphotransferase of bovine liver."
    Yamada M., Shahjahan M., Tanabe T., Kishi F., Nakazawa A.
    J. Biol. Chem. 264:19192-19199(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.
  3. "The amino acid sequence of GTP:AMP phosphotransferase from beef-heart mitochondria. Extensive homology with cytosolic adenylate kinase."
    Wieland B., Tomasselli A.G., Noda L.H., Frank R., Schulz G.E.
    Eur. J. Biochem. 143:331-339(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-227, SUBCELLULAR LOCATION.
    Tissue: Heart.
  4. "The complete primary structure of GTP:AMP phosphotransferase from beef heart mitochondria."
    Tomasselli A.G., Frank R., Schiltz E.
    FEBS Lett. 202:303-308(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-227.
    Tissue: Heart.
  5. "Cloning and characterization of the gene encoding bovine mitochondrial adenylate kinase isozyme 3."
    Shahjahan M., Yamada M., Tanaka H., Nakazawa A.
    Gene 107:313-317(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
  6. "Three-dimensional structure of the complex between the mitochondrial matrix adenylate kinase and its substrate AMP."
    Diederichs K., Schulz G.E.
    Biochemistry 29:8138-8144(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  7. "The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85-A resolution."
    Diederichs K., Schulz G.E.
    J. Mol. Biol. 217:541-549(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH AMP.

Entry informationi

Entry nameiKAD3_BOVIN
AccessioniPrimary (citable) accession number: P08760
Secondary accession number(s): Q29RI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.