P51541 (KARG_LIMPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Arginine kinase Short name=AK EC=2.7.3.3
Organism	Limulus polyphemus (Atlantic horseshoe crab)
Taxonomic identifier	6850 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Chelicerata › Merostomata › Xiphosura › Limulidae › Limulus

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 357

357

Arginine kinase

PRO_0000212000

Regions

Domain

9 – 91

83

Phosphagen kinase N-terminal

Domain

119 – 356

238

Phosphagen kinase C-terminal

Nucleotide binding

122 – 126

5

ATP

Nucleotide binding

280 – 284

5

ATP

Nucleotide binding

309 – 314

6

ATP

Region

64 – 68

5

Substrate binding

Sites

Binding site

185

1

ATP

Binding site

225

1

Substrate

Binding site

229

1

ATP

Binding site

271

1

Substrate

Binding site

314

1

Substrate

Experimental info

Mutagenesis

225

1

E → A: Reduces catalytic activity by 99.9%. Ref.4

Mutagenesis

225

1

E → D or Q: Reduces catalytic activity by 99.7%. Ref.4

Mutagenesis

271

1

C → A, D, N or S: Decreases affinity for phosphoarginine and ADP and reduces catalytic activity by 99%. Ref.6

Mutagenesis

312

1

R → G: Reduces catalytic activity by 20%; when associated with V-314; D-315; A-317 and V-319. Ref.4

Mutagenesis

314

1

E → D: Reduces catalytic activity by 98.3%. Ref.4

Mutagenesis

314

1

E → Q: Reduces catalytic activity by 99.7%. Reduces catalytic activity by 99.8%; when associated with Q-225. Ref.4

Mutagenesis

314

1

E → V: Reduces catalytic activity by 20%; when associated with G-312; D-315; A-317 and V-319. Ref.4

Mutagenesis

315

1

H → D: Reduces catalytic activity by 20%; when associated with G-312; V-314; A-317 and V-319. Ref.4

Mutagenesis

317

1

E → A: Reduces catalytic activity by 20%; when associated with G-312; V-314; D-315 and V-319. Ref.4

Mutagenesis

319

1

E → V: Reduces catalytic activity by 20%; when associated with G-312; V-314; D-315 and A-317. Ref.4

Secondary structure

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357

Helix Strand Turn

Details...

Helix

4 – 19

16

Helix

26 – 30

5

Helix

33 – 39

7

Helix

50 – 59

10

Turn

60 – 62

3

Beta strand

70 – 72

3

Helix

74 – 77

4

Helix

79 – 89

11

Helix

107 – 109

3

Beta strand

118 – 129

12

Helix

137 – 139

3

Helix

142 – 156

15

Helix

161 – 163

3

Beta strand

166 – 170

5

Helix

175 – 183

9

Helix

193 – 197

5

Turn

202 – 207

6

Beta strand

209 – 212

4

Beta strand

216 – 238

23

Helix

239 – 254

16

Turn

263 – 265

3

Helix

272 – 274

3

Beta strand

280 – 285

6

Helix

288 – 292

5

Helix

294 – 303

10

Beta strand

306 – 310

5

Beta strand

322 – 327

6

Beta strand

331 – 333

3

Helix

335 – 355

21

Sequences

	Sequence		Length	Mass (Da)
	P51541 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D4AE7B46EE5A9DF1	FASTA	357	40,239
	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

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.

PIR

S52098.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BG0	X-ray	1.86	A	2-357	[»]
1M15	X-ray	1.20	A	1-357	[»]
1P50	X-ray	2.80	A	2-357	[»]
1P52	X-ray	1.90	A	1-357	[»]
1RL9	X-ray	1.45	A	1-357	[»]
1SD0	X-ray	2.30	A	1-357	[»]
3M10	X-ray	2.35	A/B	1-357	[»]
4GVY	X-ray	2.09	A	1-357	[»]
4GVZ	X-ray	2.96	A	1-357	[»]
4GW0	X-ray	2.45	A	1-357	[»]
4GW2	X-ray	2.16	A	1-357	[»]

ProteinModelPortal

P51541.

SMR

P51541. Positions 2-357.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P51541.

Family and domain databases

Gene3D

1.10.135.10. 1 hit.
3.30.590.10. 1 hit.

InterPro

IPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]

PANTHER

PTHR11547. PTHR11547. 1 hit.

Pfam

PF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]

SUPFAM

SSF48034. ATP-gua_Ptrans. 1 hit.

PROSITE

PS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P51541.

Entry information

Entry name

KARG_LIMPO

Accession

Primary (citable) accession number: P51541

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)