Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenylate kinase isoenzyme 1

Gene

AK1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.UniRule annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei39AMPUniRule annotation1
Binding sitei44AMPUniRule annotation1
Binding sitei101AMPUniRule annotation1
Binding sitei132ATPUniRule annotation1
Binding sitei138AMPUniRule annotation1
Binding sitei149AMPUniRule annotation1
Binding sitei177ATP; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 23ATPUniRule annotation1 Publication6
Nucleotide bindingi65 – 67AMPUniRule annotation3
Nucleotide bindingi94 – 97AMPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SSC-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase isoenzyme 1UniRule annotation (EC:2.7.4.3UniRule annotation, EC:2.7.4.6UniRule annotation)
Short name:
AK 1UniRule annotation
Alternative name(s):
ATP-AMP transphosphorylase 1UniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
MyokinaseUniRule annotation
Gene namesi
Name:AK1UniRule annotation
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001589121 – 194Adenylate kinase isoenzyme 1Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineUniRule annotation1 Publication1
Modified residuei38PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00571.
PeptideAtlasiP00571.

Expressioni

Gene expression databases

BgeeiENSSSCG00000005627.
GenevisibleiP00571. SS.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006028.

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 6Combined sources5
Beta strandi10 – 15Combined sources6
Helixi21 – 31Combined sources11
Beta strandi35 – 38Combined sources4
Helixi39 – 49Combined sources11
Helixi52 – 61Combined sources10
Turni62 – 64Combined sources3
Helixi69 – 81Combined sources13
Turni82 – 86Combined sources5
Beta strandi90 – 94Combined sources5
Helixi99 – 108Combined sources10
Beta strandi113 – 119Combined sources7
Helixi122 – 136Combined sources15
Helixi146 – 156Combined sources11
Helixi158 – 164Combined sources7
Turni165 – 168Combined sources4
Beta strandi170 – 174Combined sources5
Helixi179 – 191Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ADKX-ray2.10A1-194[»]
ProteinModelPortaliP00571.
SMRiP00571.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00571.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 67NMPbindUniRule annotation2 PublicationsAdd BLAST30
Regioni131 – 141LIDUniRule annotation2 PublicationsAdd BLAST11

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 ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation2 Publications

Sequence similaritiesi

Belongs to the adenylate kinase family. AK1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiP00571.
KOiK00939.
OMAiPREKNQG.
OrthoDBiEOG091G0OQ7.
TreeFamiTF354283.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03171. Adenylate_kinase_AK1. 1 hit.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01360. aden_kin_iso1. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00571-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKLKKSKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG
60 70 80 90 100
SARGKMLSEI MEKGQLVPLE TVLDMLRDAM VAKVDTSKGF LIDGYPREVK
110 120 130 140 150
QGEEFERKIG QPTLLLYVDA GPETMTKRLL KRGETSGRVD DNEETIKKRL
160 170 180 190
ETYYKATEPV IAFYEKRGIV RKVNAEGSVD DVFSQVCTHL DTLK
Length:194
Mass (Da):21,639
Last modified:July 21, 1986 - v1
Checksum:i554202B49B1E74B4
GO

Sequence databases

PIRiA00682. KIPGA.
RefSeqiXP_003122225.3. XM_003122177.5.
XP_005660509.1. XM_005660452.2.
UniGeneiSsc.17611.

Genome annotation databases

EnsembliENSSSCT00000006187; ENSSSCP00000006028; ENSSSCG00000005627.
GeneIDi100521423.
KEGGissc:100521423.

Cross-referencesi

Sequence databases

PIRiA00682. KIPGA.
RefSeqiXP_003122225.3. XM_003122177.5.
XP_005660509.1. XM_005660452.2.
UniGeneiSsc.17611.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ADKX-ray2.10A1-194[»]
ProteinModelPortaliP00571.
SMRiP00571.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006028.

Proteomic databases

PaxDbiP00571.
PeptideAtlasiP00571.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000006187; ENSSSCP00000006028; ENSSSCG00000005627.
GeneIDi100521423.
KEGGissc:100521423.

Organism-specific databases

CTDi203.

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiP00571.
KOiK00939.
OMAiPREKNQG.
OrthoDBiEOG091G0OQ7.
TreeFamiTF354283.

Enzyme and pathway databases

ReactomeiR-SSC-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

EvolutionaryTraceiP00571.

Gene expression databases

BgeeiENSSSCG00000005627.
GenevisibleiP00571. SS.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03171. Adenylate_kinase_AK1. 1 hit.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01360. aden_kin_iso1. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAD1_PIG
AccessioniPrimary (citable) accession number: P00571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 123 of the entry and version 1 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.