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Reviewed, UniProtKB/Swiss-Prot P00571 (KAD1_PIG)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Adenylate kinase isoenzyme 1
      Short name=AK 1
    EC=2.7.4.3
Alternative name(s):
    ATP-AMP transphosphorylase 1
    Myokinase
Gene names
Name: AK1
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth.

Catalytic activity

ATP + AMP = 2 ADP.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the adenylate kinase family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processATP metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from sequence or structural similarity. Source: AgBase

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Adenylate kinase isoenzyme 1
PRO_0000158912

Regions

Nucleotide binding15 – 239ATP
Nucleotide binding94 – 1018AMP By similarity

Sites

Binding site391AMP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1

Secondary structure

1 ................................. 194
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00571-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 554202B49B1E74B4

FASTA19421,639
        10         20         30         40         50         60 
MEEKLKKSKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG SARGKMLSEI 

        70         80         90        100        110        120 
MEKGQLVPLE TVLDMLRDAM VAKVDTSKGF LIDGYPREVK QGEEFERKIG QPTLLLYVDA 

       130        140        150        160        170        180 
GPETMTKRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD 

       190 
DVFSQVCTHL DTLK

« Hide

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References

[1]"The amino-acid sequence of sarcine adenylate kinase from skeletal muscle."
Heil A., Mueller G., Noda L., Pinder T., Schirmer R.H., Schirmer I., von Zabern I.
Eur. J. Biochem. 43:131-144(1974) [PubMed: 4366177] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Skeletal muscle.
[2]"ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins."
Fry D.C., Kuby S.A., Mildvan A.S.
Proc. Natl. Acad. Sci. U.S.A. 83:907-911(1986) [PubMed: 2869483] [Abstract]
Cited for: ATP-BINDING SITE.
[3]"Three dimensional structure of adenyl kinase."
Schulz G.E., Elzinga M., Marx F., Schirmer R.H.
Nature 250:120-123(1974) [PubMed: 4367210] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[4]"Refined structure of porcine cytosolic adenylate kinase at 2.1 A resolution."
Dreusicke D., Karplus P.A., Schulz G.E.
J. Mol. Biol. 199:359-371(1988) [PubMed: 2832612] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

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Cross-references

Sequence databases

PIRKIPGA. A00682.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3ADKX-ray2.10A1-194[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP00571.

Enzyme and pathway databases

BRENDA2.7.4.3. 249.

Family and domain databases

InterProIPR000850. Adenylate_kin.
IPR006267. Adenylate_kin1.
[Graphical view]
PANTHERPTHR23359. Adenylate_kin. 1 hit.
PfamPF00406. ADK. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
ProDomPD000657. Adenylate_kin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01360. aden_kin_iso1. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameKAD1_PIG
AccessionPrimary (citable) accession number: P00571
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents