[1]	PROTEIN SEQUENCE. TISSUE=Skeletal muscle; PubMed=4366177 [NCBI, ExPASy, EBI, Israel, Japan] Heil A., Mueller G., Noda L., Pinder T., Schirmer R.H., Schirmer I., von Zabern I.; "The amino-acid sequence of sarcine adenylate kinase from skeletal muscle."; Eur. J. Biochem. 43:131-144(1974).
[2]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1038/250120a0; PubMed=4367210 [NCBI, ExPASy, EBI, Israel, Japan] Schulz G.E., Elzinga M., Marx F., Schirmer R.H.; "Three dimensional structure of adenyl kinase."; Nature 250:120-123(1974).
[3]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). DOI=10.1016/0022-2836(88)90319-1; PubMed=2832612 [NCBI, ExPASy, EBI, Israel, Japan] Dreusicke D., Karplus P.A., Schulz G.E.; "Refined structure of porcine cytosolic adenylate kinase at 2.1 A resolution."; J. Mol. Biol. 199:359-371(1988).
[4]	ATP-BINDING SITE. PubMed=2869483 [NCBI, ExPASy, EBI, Israel, Japan] Fry D.C., Kuby S.A., Mildvan A.S.; "ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins."; Proc. Natl. Acad. Sci. U.S.A. 83:907-911(1986).

Comments

FUNCTION: This small ubiquitous enzyme is essential for maintenance and cell growth.
CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the adenylate kinase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A00682; KIPGA.

3D structure databases

PDB

3ADK; X-ray; 2.10 A; A=1-194.

[ExPASy / RCSB / EBI]

PDBsum

3ADK; -.

ModBase

P00571.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from sequence or structural similarity from AgBase).
QuickGo view.

Family and domain databases

InterPro

IPR000850; Adenylate_kin.
IPR006267; Adenylate_kin1.
Graphical view of domain structure.

PANTHER

PTHR23359; Adenylate_kin; 1.

Pfam

PF00406; ADK; 1.
Pfam graphical view of domain structure.

PRINTS

PR00094; ADENYLTKNASE.

ProDom

PD000657; Adenylate_kin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01360; aden_kin_iso1; 1.

PROSITE

PS00113; ADENYLATE_KINASE; 1.

Other

Phylogenomic databases

HOVERGEN

P00571; -.

Other

LinkHub

P00571; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 194`	`194`	`Adenylate kinase isoenzyme 1.`	`PRO_0000158912`
`NP_BIND`	`15 23`	`9`	`ATP.`
`MOD_RES`	`1 1`		`N-acetylmethionine.`
`HELIX`	`2 6`	`5`
`STRAND`	`10 15`	`6`
`HELIX`	`21 31`	`11`
`STRAND`	`35 38`	`4`
`HELIX`	`39 49`	`11`
`HELIX`	`52 61`	`10`
`TURN`	`62 64`	`3`
`HELIX`	`69 81`	`13`
`TURN`	`82 86`	`5`
`STRAND`	`90 94`	`5`
`HELIX`	`99 108`	`10`
`STRAND`	`113 119`	`7`
`HELIX`	`122 136`	`15`
`HELIX`	`146 156`	`11`
`HELIX`	`158 164`	`7`
`TURN`	`165 168`	`4`
`STRAND`	`170 174`	`5`
`HELIX`	`179 191`	`13`

Sequence information

Length: 194 AA [This is the length of the unprocessed precursor]

Molecular weight: 21639 Da [This is the MW of the unprocessed precursor]

CRC64: 554202B49B1E74B4 [This is a checksum on the sequence]

        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

P00571 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools