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Protein

Adenylate kinase isoenzyme 1

Gene

AK1

Organism
Oryctolagus cuniculus (Rabbit)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391AMPUniRule annotation
Binding sitei44 – 441AMPUniRule annotation
Binding sitei101 – 1011AMPUniRule annotation
Binding sitei132 – 1321ATPUniRule annotation
Binding sitei138 – 1381AMPUniRule annotation
Binding sitei149 – 1491AMPUniRule annotation
Binding sitei177 – 1771ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 236ATPUniRule annotation
Nucleotide bindingi65 – 673AMPUniRule annotation
Nucleotide bindingi94 – 974AMPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP00569.

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5709.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Adenylate kinase isoenzyme 1PRO_0000158913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineUniRule annotation1 Publication
Modified residuei38 – 381PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00569.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000004478.

Chemistry

BindingDBiP00569.

Structurei

3D structure databases

ProteinModelPortaliP00569.
SMRiP00569. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 6730NMPbindUniRule annotationAdd
BLAST
Regioni131 – 14111LIDUniRule 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 ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiP00569.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03171. Adenylate_kinase_AK1.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
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.

P00569-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKLKKAKI IFVVGGPGSG KGTQCEKIVH KYGYTHLSTG DLLRAEVSSG
60 70 80 90 100
SARGKKLSEI MEKGQLVPLE TVLDMLRDAM VAKADTSKGF LIDGYPRQVQ
110 120 130 140 150
QGEEFERRIA QPTLLLYVDA GPETMQKRLL KRGETSGRVD DNEETIKKRL
160 170 180 190
ETYYKATEPV IAFYEKRGIV RKVNAEGSVD NVFSQVCTHL DALK
Length:194
Mass (Da):21,638
Last modified:July 21, 1986 - v1
Checksum:iB579871616963214
GO

Sequence databases

PIRiA00680. KIRBA.

Cross-referencesi

Sequence databases

PIRiA00680. KIRBA.

3D structure databases

ProteinModelPortaliP00569.
SMRiP00569. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000004478.

Chemistry

BindingDBiP00569.
ChEMBLiCHEMBL5709.

Proteomic databases

PRIDEiP00569.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiP00569.

Enzyme and pathway databases

SABIO-RKP00569.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03171. Adenylate_kinase_AK1.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
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...

Publicationsi

  1. "Studies on adenosine triphosphate transphosphorylases. Amino acid sequence of rabbit muscle ATP-AMP transphosphorylase."
    Kuby S.A., Palmieri R.H., Frischat A., Fischer A.H., Wu L.H., Maland L., Manship M.
    Biochemistry 23:2393-2399(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiKAD1_RABIT
AccessioniPrimary (citable) accession number: P00569
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 11, 2015
This is version 91 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

Complete proteome, Direct protein sequencing, 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.