KARG_POLPT
ID KARG_POLPT Reviewed; 357 AA.
AC A0A286R7K5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Arginine kinase {ECO:0000303|PubMed:28924503};
DE Short=AK {ECO:0000303|PubMed:28924503};
DE EC=2.7.3.3 {ECO:0000269|PubMed:28924503};
OS Polybetes pythagoricus (South American huntsman spider) (Ocypete
OS pythagorica).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Dionycha; Sparassidae; Polybetes.
OX NCBI_TaxID=881871;
RN [1] {ECO:0007744|PDB:5U8E, ECO:0007744|PDB:5U92}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN APO
RP FORM AND IN COMPLEX WITH ARGININE, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28924503; DOI=10.7717/peerj.3787;
RA Laino A., Lopez-Zavala A.A., Garcia-Orozco K.D., Carrasco-Miranda J.S.,
RA Santana M., Stojanoff V., Sotelo-Mundo R.R., Garcia C.F.;
RT "Biochemical and structural characterization of a novel arginine kinase
RT from the spider Polybetes pythagoricus.";
RL PeerJ 5:e3787-e3787(2017).
CC -!- FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-
CC phosphate group to L-arginine. {ECO:0000269|PubMed:28924503}.
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:28924503};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for L-arginine {ECO:0000269|PubMed:28924503};
CC Note=kcat is 75 sec(-1) for L-arginine.
CC {ECO:0000269|PubMed:28924503};
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; MF001441; ASV64865.1; -; mRNA.
DR PDB; 5U8E; X-ray; 2.18 A; A=1-357.
DR PDB; 5U92; X-ray; 2.00 A; A=1-357.
DR PDBsum; 5U8E; -.
DR PDBsum; 5U92; -.
DR AlphaFoldDB; A0A286R7K5; -.
DR SMR; A0A286R7K5; -.
DR BRENDA; 2.7.3.3; 17871.
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; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..357
FT /note="Arginine kinase"
FT /id="PRO_0000451077"
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..66
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:28924503,
FT ECO:0007744|PDB:5U92"
FT BINDING 122..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 225
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:28924503,
FT ECO:0007744|PDB:5U92"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 271
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:28924503,
FT ECO:0007744|PDB:5U92"
FT BINDING 280..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 309..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:5U92"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 216..236
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 239..256
FT /evidence="ECO:0007829|PDB:5U92"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:5U92"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:5U92"
FT HELIX 335..355
FT /evidence="ECO:0007829|PDB:5U92"
SQ SEQUENCE 357 AA; 40087 MW; 8AAF5203C6F3A4D7 CRC64;
MVDQATLDKL EAGFKKLQDA TDCKSLLKKY LNREVFDQCK SLKTALGATL LDCIQSGVEN
LDSGVGIYAP DAEAYTLFAP IFNPIIEDYH EGFKPTDKHP PTDFGDINTI VNVDPSGKYV
VSTHVRCGRS LKGYPFNPCL TEANYKEMED KVSAIFGTFE GELKGKYYPL TGMDKATQQQ
LIDDHFLFKE GDRFLQAANA CRYWPTGRGI YHNDAKTFLV WVNEEDHLRI ISMQKGGDLK
TIFQRLVNAV NTIESKLPFS RDDRLGFLTF CPTNLGTTIR ASVHIALPKL AKDKKQLEAI
AAKFNLQVRG TRGEHTESEG GVYDISNKRR MGLTEYQAVK EMQDGILEMI KMEEAAP
