KARG_LIMPO
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 03-AUG-2022, entry version 96.
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}.
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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 GeneID; 106471713; -.
DR OrthoDB; 825025at2759; -.
DR BRENDA; 2.7.3.3; 3034.
DR SABIO-RK; P51541; -.
DR EvolutionaryTrace; P51541; -.
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 Gene3D; 1.10.135.10; -; 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; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 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
