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Protein

GTP:AMP phosphotransferase AK3, mitochondrial

Gene

Ak3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 annotation
Binding sitei43 – 431AMPUniRule annotation
Binding sitei98 – 981AMPUniRule annotation
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 annotation
Nucleotide bindingi91 – 944AMPUniRule annotation
Nucleotide bindingi137 – 1382GTPUniRule annotation

GO - Molecular functioni

  • adenylate kinase activity Source: RGD
  • ATP binding Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: RGD
  • nucleoside triphosphate adenylate kinase activity Source: UniProtKB-HAMAP

GO - Biological processi

  • ADP biosynthetic process Source: RGD
  • AMP phosphorylation Source: RGD
  • ATP metabolic process Source: RGD
  • cerebellum development Source: RGD
  • dATP metabolic process Source: RGD
  • GTP metabolic process Source: UniProtKB-HAMAP
  • ITP metabolic process Source: UniProtKB-HAMAP
  • liver development Source: RGD
  • muscle organ development Source: RGD
  • nucleotide phosphorylation Source: GOC
  • olfactory bulb development Source: RGD
  • protein homooligomerization Source: RGD
  • response to starvation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

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:Ak3
Synonyms:Ak3l1, Akl3l
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619885. Ak3.

Subcellular locationi

  • Mitochondrion matrix UniRule annotation

GO - Cellular componenti

  • mitochondrial intermembrane space Source: RGD
  • mitochondrial matrix Source: RGD
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 227226GTP:AMP phosphotransferase AK3, mitochondrialPRO_0000158925Add
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

PaxDbiP29411.
PRIDEiP29411.

PTM databases

iPTMnetiP29411.
PhosphoSiteiP29411.

Interactioni

Subunit structurei

Monomer.UniRule annotation

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020744.

Chemistry

BindingDBiP29411.

Structurei

3D structure databases

ProteinModelPortaliP29411.
SMRiP29411. Positions 2-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP29411.
KOiK00944.
PhylomeDBiP29411.

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.

P29411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGASGRLLRA VIMGAPGSGK GTGSSRITKH FELKHLSSGD LLRQNMLQGT
60 70 80 90 100
EIAVLAKSFI DQGKLIPDDD MTRLALHELK NLTQCSWLLD GFPRTLPQAE
110 120 130 140 150
ALDRVYQIDT VINLNVPFEV IKLRLTARWI HPASGRVYNI EFNPPKTVGI
160 170 180 190 200
DDLTGEPLIQ REDDKPETVI KRLKAYEAQT EPVLQYYQKK GVLETFSGTE
210 220
TNKIRPHVYS FLQMKVPETI QKASVTP
Length:227
Mass (Da):25,438
Last modified:January 23, 2007 - v2
Checksum:iD2229F7E3BF65676
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13062 mRNA. Translation: BAA02379.1.
PIRiJQ1945.
RefSeqiNP_037350.1. NM_013218.1.
UniGeneiRn.60.

Genome annotation databases

GeneIDi26956.
KEGGirno:26956.
UCSCiRGD:619885. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13062 mRNA. Translation: BAA02379.1.
PIRiJQ1945.
RefSeqiNP_037350.1. NM_013218.1.
UniGeneiRn.60.

3D structure databases

ProteinModelPortaliP29411.
SMRiP29411. Positions 2-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020744.

Chemistry

BindingDBiP29411.
ChEMBLiCHEMBL4799.

PTM databases

iPTMnetiP29411.
PhosphoSiteiP29411.

Proteomic databases

PaxDbiP29411.
PRIDEiP29411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi26956.
KEGGirno:26956.
UCSCiRGD:619885. rat.

Organism-specific databases

CTDi50808.
RGDi619885. Ak3.

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP29411.
KOiK00944.
PhylomeDBiP29411.

Miscellaneous databases

NextBioi608029.
PROiP29411.

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

  1. "Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes."
    Tanabe T., Yamada M., Noma T., Kajii T., Nakazawa A.
    J. Biochem. 113:200-207(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiKAD3_RAT
AccessioniPrimary (citable) accession number: P29411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.