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P51541 (KARG_LIMPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine kinase

Short name=AK
EC=2.7.3.3
OrganismLimulus polyphemus (Atlantic horseshoe crab)
Taxonomic identifier6850 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataMerostomataXiphosuraLimulidaeLimulus

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-arginine = ADP + N(omega)-phospho-L-arginine.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processphosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

arginine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357Arginine kinase
PRO_0000212000

Regions

Domain9 – 9183Phosphagen kinase N-terminal
Domain119 – 356238Phosphagen kinase C-terminal
Nucleotide binding122 – 1265ATP
Nucleotide binding280 – 2845ATP
Nucleotide binding309 – 3146ATP
Region64 – 685Substrate binding

Sites

Binding site1851ATP
Binding site2251Substrate
Binding site2291ATP
Binding site2711Substrate
Binding site3141Substrate

Experimental info

Mutagenesis2251E → A: Reduces catalytic activity by 99.9%. Ref.4
Mutagenesis2251E → D or Q: Reduces catalytic activity by 99.7%. Ref.4
Mutagenesis2711C → A, D, N or S: Decreases affinity for phosphoarginine and ADP and reduces catalytic activity by 99%. Ref.6
Mutagenesis3121R → G: Reduces catalytic activity by 20%; when associated with V-314; D-315; A-317 and V-319. Ref.4
Mutagenesis3141E → D: Reduces catalytic activity by 98.3%. Ref.4
Mutagenesis3141E → Q: Reduces catalytic activity by 99.7%. Reduces catalytic activity by 99.8%; when associated with Q-225. Ref.4
Mutagenesis3141E → V: Reduces catalytic activity by 20%; when associated with G-312; D-315; A-317 and V-319. Ref.4
Mutagenesis3151H → D: Reduces catalytic activity by 20%; when associated with G-312; V-314; A-317 and V-319. Ref.4
Mutagenesis3171E → A: Reduces catalytic activity by 20%; when associated with G-312; V-314; D-315 and V-319. Ref.4
Mutagenesis3191E → V: Reduces catalytic activity by 20%; when associated with G-312; V-314; D-315 and A-317. Ref.4

Secondary structure

......................................................... 357
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51541 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D4AE7B46EE5A9DF1

FASTA35740,239
        10         20         30         40         50         60 
MVDQATLDKL EAGFKKLQEA SDCKSLLKKH LTKDVFDSIK NKKTGMGATL LDVIQSGVEN 

        70         80         90        100        110        120 
LDSGVGIYAP DAESYRTFGP LFDPIIDDYH GGFKLTDKHP PKEWGDINTL VDLDPGGQFI 

       130        140        150        160        170        180 
ISTRVRCGRS LQGYPFNPCL TAEQYKEMEE KVSSTLSSME DELKGTYYPL TGMSKATQQQ 

       190        200        210        220        230        240 
LIDDHFLFKE GDRFLQTANA CRYWPTGRGI FHNDAKTFLV WVNEEDHLRI ISMQKGGDLK 

       250        260        270        280        290        300 
TVYKRLVTAV DNIESKLPFS HDDRFGFLTF CPTNLGTTMR ASVHIQLPKL AKDRKVLEDI 

       310        320        330        340        350 
ASKFNLQVRG TRGEHTESEG GVYDISNKRR LGLTEYQAVR EMQDGILEMI KMEKAAA 

« Hide

References

[1]"Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues."
Strong S.J., Ellington W.R.
Biochim. Biophys. Acta 1246:197-200(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Heart and Skeletal muscle.
[2]"Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions."
Zhou G., Somasundaram T., Blanc E., Parthasarathy G., Ellington W.R., Chapman M.S.
Proc. Natl. Acad. Sci. U.S.A. 95:8449-8454(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH ARGININE; NITRATE AND ADP.
[3]"Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights."
Yousef M.S., Fabiola F., Gattis J.L., Somasundaram T., Chapman M.S.
Acta Crystallogr. D 58:2009-2017(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ARGININE; NITRATE AND ADP.
[4]"The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase."
Pruett P.S., Azzi A., Clark S.A., Yousef M.S., Gattis J.L., Somasundaram T., Ellington W.R., Chapman M.S.
J. Biol. Chem. 278:26952-26957(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS GLN-225 AND ASP-314 IN COMPLEX WITH ARGININE; NITRATE AND ADP, MUTAGENESIS OF GLU-225; ARG-312; GLU-314; HIS-315; GLU-317 AND GLU-319.
[5]"The role of phosphagen specificity loops in arginine kinase."
Azzi A., Clark S.A., Ellington W.R., Chapman M.S.
Protein Sci. 13:575-585(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH ADP.
[6]"The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants."
Gattis J.L., Ruben E., Fenley M.O., Ellington W.R., Chapman M.S.
Biochemistry 43:8680-8689(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-271 IN COMPLEX WITH TRANSITION STATE ANALOG, MUTAGENESIS OF CYS-271.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09809 mRNA. Translation: AAA82169.1.
PIRS52098.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG0X-ray1.86A2-357[»]
1M15X-ray1.20A1-357[»]
1P50X-ray2.80A2-357[»]
1P52X-ray1.90A1-357[»]
1RL9X-ray1.45A1-357[»]
1SD0X-ray2.30A1-357[»]
3M10X-ray2.35A/B1-357[»]
4GVYX-ray2.09A1-357[»]
4GVZX-ray2.96A1-357[»]
4GW0X-ray2.45A1-357[»]
4GW2X-ray2.16A1-357[»]
ProteinModelPortalP51541.
SMRP51541. Positions 2-357.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP51541.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP51541.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. SSF48034. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51541.

Entry information

Entry nameKARG_LIMPO
AccessionPrimary (citable) accession number: P51541
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references