ID KARG_LIMPO Reviewed; 357 AA. AC P51541; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Arginine kinase; DE Short=AK; DE EC=2.7.3.3 {ECO:0000269|PubMed:15236576}; OS Limulus polyphemus (Atlantic horseshoe crab). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata; OC Xiphosura; Limulidae; Limulus. OX NCBI_TaxID=6850; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Heart, and Skeletal muscle; RX PubMed=7819288; DOI=10.1016/0167-4838(94)00218-6; RA Strong S.J., Ellington W.R.; RT "Isolation and sequence analysis of the gene for arginine kinase from the RT chelicerate arthropod, Limulus polyphemus: insights into catalytically RT important residues."; RL Biochim. Biophys. Acta 1246:197-200(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH ARGININE; NITRATE RP AND ADP. RX PubMed=9671698; DOI=10.1073/pnas.95.15.8449; RA Zhou G., Somasundaram T., Blanc E., Parthasarathy G., Ellington W.R., RA Chapman M.S.; RT "Transition state structure of arginine kinase: implications for catalysis RT of bimolecular reactions."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8449-8454(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ARGININE; NITRATE AND RP ADP. RX PubMed=12454458; DOI=10.1107/s0907444902014683; RA Yousef M.S., Fabiola F., Gattis J.L., Somasundaram T., Chapman M.S.; RT "Refinement of the arginine kinase transition-state analogue complex at 1.2 RT A resolution: mechanistic insights."; RL Acta Crystallogr. D 58:2009-2017(2002). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS GLN-225 AND ASP-314 IN RP COMPLEX WITH ARGININE; NITRATE AND ADP, AND MUTAGENESIS OF GLU-225; RP ARG-312; GLU-314; HIS-315; GLU-317 AND GLU-319. RX PubMed=12732621; DOI=10.1074/jbc.m212931200; RA Pruett P.S., Azzi A., Clark S.A., Yousef M.S., Gattis J.L., RA Somasundaram T., Ellington W.R., Chapman M.S.; RT "The putative catalytic bases have, at most, an accessory role in the RT mechanism of arginine kinase."; RL J. Biol. Chem. 278:26952-26957(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH ADP. RX PubMed=14978299; DOI=10.1110/ps.03428304; RA Azzi A., Clark S.A., Ellington W.R., Chapman M.S.; RT "The role of phosphagen specificity loops in arginine kinase."; RL Protein Sci. 13:575-585(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-271 IN COMPLEX WITH RP TRANSITION STATE ANALOG, MUTAGENESIS OF CYS-271, FUNCTION, AND CATALYTIC RP ACTIVITY. RX PubMed=15236576; DOI=10.1021/bi049793i; RA Gattis J.L., Ruben E., Fenley M.O., Ellington W.R., Chapman M.S.; RT "The active site cysteine of arginine kinase: structural and functional RT analysis of partially active mutants."; RL Biochemistry 43:8680-8689(2004). CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphoryl CC group of ATP to L-arginine. {ECO:0000269|PubMed:15236576}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine; CC Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3; CC Evidence={ECO:0000269|PubMed:15236576}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22941; CC Evidence={ECO:0000305|PubMed:15236576}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12454458, CC ECO:0000269|PubMed:12732621, ECO:0000269|PubMed:14978299, CC ECO:0000269|PubMed:15236576, ECO:0000269|PubMed:9671698}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE- CC ProRule:PRU00843}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U09809; AAA82169.1; -; mRNA. DR PIR; S52098; S52098. DR RefSeq; NP_001301013.1; NM_001314084.1. DR PDB; 1BG0; X-ray; 1.86 A; A=2-357. DR PDB; 1M15; X-ray; 1.20 A; A=1-357. DR PDB; 1P50; X-ray; 2.80 A; A=2-357. DR PDB; 1P52; X-ray; 1.90 A; A=1-357. DR PDB; 1RL9; X-ray; 1.45 A; A=1-357. DR PDB; 1SD0; X-ray; 2.30 A; A=1-357. DR PDB; 3M10; X-ray; 2.35 A; A/B=1-357. DR PDB; 4GVY; X-ray; 2.09 A; A=1-357. DR PDB; 4GVZ; X-ray; 2.96 A; A=1-357. DR PDB; 4GW0; X-ray; 2.45 A; A=1-357. DR PDB; 4GW2; X-ray; 2.16 A; A=1-357. DR PDB; 5J99; X-ray; 1.70 A; A=1-357. DR PDB; 5J9A; X-ray; 2.00 A; A=1-357. DR PDBsum; 1BG0; -. DR PDBsum; 1M15; -. DR PDBsum; 1P50; -. DR PDBsum; 1P52; -. DR PDBsum; 1RL9; -. DR PDBsum; 1SD0; -. DR PDBsum; 3M10; -. DR PDBsum; 4GVY; -. DR PDBsum; 4GVZ; -. DR PDBsum; 4GW0; -. DR PDBsum; 4GW2; -. DR PDBsum; 5J99; -. DR PDBsum; 5J9A; -. DR AlphaFoldDB; P51541; -. DR BMRB; P51541; -. DR SMR; P51541; -. DR EnsemblMetazoa; NM_001314084.1; NP_001301013.1; LOC106471713. DR GeneID; 106471713; -. DR KEGG; lpol:106471713; -. DR OrthoDB; 35839at2759; -. DR BRENDA; 2.7.3.3; 3034. DR SABIO-RK; P51541; -. DR EvolutionaryTrace; P51541; -. DR Proteomes; UP000694941; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004054; F:arginine kinase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro. DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB. DR CDD; cd07932; arginine_kinase_like; 1. DR Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1. DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1. DR InterPro; IPR000749; ATP-guanido_PTrfase. DR InterPro; IPR022415; ATP-guanido_PTrfase_AS. DR InterPro; IPR022414; ATP-guanido_PTrfase_cat. DR InterPro; IPR022413; ATP-guanido_PTrfase_N. DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf. DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom. DR PANTHER; PTHR11547:SF38; ARGININE KINASE; 1. DR PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1. DR Pfam; PF00217; ATP-gua_Ptrans; 1. DR Pfam; PF02807; ATP-gua_PtransN; 1. DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1. DR SUPFAM; SSF48034; Guanido kinase N-terminal domain; 1. DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1. DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1. DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; KW Nucleotide-binding; Transferase. FT CHAIN 1..357 FT /note="Arginine kinase" FT /id="PRO_0000212000" FT DOMAIN 9..91 FT /note="Phosphagen kinase N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842" FT DOMAIN 119..356 FT /note="Phosphagen kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 64..68 FT /ligand="substrate" FT BINDING 122..126 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 225 FT /ligand="substrate" FT BINDING 229 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 271 FT /ligand="substrate" FT BINDING 280..284 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 309..314 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 314 FT /ligand="substrate" FT MUTAGEN 225 FT /note="E->A: Reduces catalytic activity by 99.9%." FT /evidence="ECO:0000269|PubMed:12732621" FT MUTAGEN 225 FT /note="E->D,Q: Reduces catalytic activity by 99.7%." FT /evidence="ECO:0000269|PubMed:12732621" FT MUTAGEN 271 FT /note="C->A,D,N,S: Decreases affinity for phosphoarginine FT and ADP and reduces catalytic activity by 99%." FT /evidence="ECO:0000269|PubMed:15236576" FT MUTAGEN 312 FT /note="R->G: Reduces catalytic activity by 20%; when FT associated with V-314; D-315; A-317 and V-319." FT /evidence="ECO:0000269|PubMed:12732621" FT MUTAGEN 314 FT /note="E->D: Reduces catalytic activity by 98.3%." FT /evidence="ECO:0000269|PubMed:12732621" FT MUTAGEN 314 FT /note="E->Q: Reduces catalytic activity by 99.7%. Reduces FT catalytic activity by 99.8%; when associated with Q-225." FT /evidence="ECO:0000269|PubMed:12732621" FT MUTAGEN 314 FT /note="E->V: Reduces catalytic activity by 20%; when FT associated with G-312; D-315; A-317 and V-319." FT /evidence="ECO:0000269|PubMed:12732621" FT MUTAGEN 315 FT /note="H->D: Reduces catalytic activity by 20%; when FT associated with G-312; V-314; A-317 and V-319." FT /evidence="ECO:0000269|PubMed:12732621" FT MUTAGEN 317 FT /note="E->A: Reduces catalytic activity by 20%; when FT associated with G-312; V-314; D-315 and V-319." FT /evidence="ECO:0000269|PubMed:12732621" FT MUTAGEN 319 FT /note="E->V: Reduces catalytic activity by 20%; when FT associated with G-312; V-314; D-315 and A-317." FT /evidence="ECO:0000269|PubMed:12732621" FT HELIX 4..19 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 26..30 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 33..39 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 50..59 FT /evidence="ECO:0007829|PDB:1M15" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:1P50" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 74..77 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 79..89 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:1M15" FT STRAND 118..129 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 142..156 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:1M15" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 175..183 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 193..197 FT /evidence="ECO:0007829|PDB:1M15" FT TURN 202..207 FT /evidence="ECO:0007829|PDB:1M15" FT STRAND 209..212 FT /evidence="ECO:0007829|PDB:1M15" FT STRAND 216..238 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 239..254 FT /evidence="ECO:0007829|PDB:1M15" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:1M15" FT STRAND 280..285 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 288..292 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:1M15" FT STRAND 306..310 FT /evidence="ECO:0007829|PDB:1M15" FT STRAND 322..327 FT /evidence="ECO:0007829|PDB:1M15" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:1M15" FT HELIX 335..355 FT /evidence="ECO:0007829|PDB:1M15" SQ SEQUENCE 357 AA; 40239 MW; D4AE7B46EE5A9DF1 CRC64; MVDQATLDKL EAGFKKLQEA SDCKSLLKKH LTKDVFDSIK NKKTGMGATL LDVIQSGVEN LDSGVGIYAP DAESYRTFGP LFDPIIDDYH GGFKLTDKHP PKEWGDINTL VDLDPGGQFI ISTRVRCGRS LQGYPFNPCL TAEQYKEMEE KVSSTLSSME DELKGTYYPL TGMSKATQQQ LIDDHFLFKE GDRFLQTANA CRYWPTGRGI FHNDAKTFLV WVNEEDHLRI ISMQKGGDLK TVYKRLVTAV DNIESKLPFS HDDRFGFLTF CPTNLGTTMR ASVHIQLPKL AKDRKVLEDI ASKFNLQVRG TRGEHTESEG GVYDISNKRR LGLTEYQAVR EMQDGILEMI KMEKAAA //