ID KARG_HALMK Reviewed; 358 AA.
AC P51544;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 22-FEB-2023, entry version 73.
DE RecName: Full=Arginine kinase;
DE Short=AK;
DE EC=2.7.3.3;
OS Haliotis madaka (Giant abalone) (Nordotis madaka).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX NCBI_TaxID=81897;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=8145248; DOI=10.1006/jmbi.1994.1237;
RA Suzuki T., Furukohri T.;
RT "Evolution of phosphagen kinase. Primary structure of glycocyamine kinase
RT and arginine kinase from invertebrates.";
RL J. Mol. Biol. 237:353-357(1994).
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 -!- SUBUNIT: Monomer.
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; D26104; BAA05100.1; -; mRNA.
DR PIR; S46407; S46407.
DR AlphaFoldDB; P51544; -.
DR SMR; P51544; -.
DR GO; GO:0004054; F:arginine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..358
FT /note="Arginine kinase"
FT /id="PRO_0000212002"
FT DOMAIN 6..88
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 116..353
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 61..65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 306..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 39814 MW; 35ABACE7EC8A2D1E CRC64;
MLAMASVEEL WAKLDGAADC KSLLKNNLTK ERYEALKDKK TKFGGTLADC IRSGCLNLDS
GVGIYACDPD AYTVFADVLD AVIKEYHKVP ELKHPEPEMG DLDKLNFGDL DPSGEYIVST
RVRVGRSHDS YGFPPVLTKQ ERLKMEEDTK AAFEKFSGEL AGKYFPLEGM SKEDQKQMTE
DHFLFKDDDR FLRDAGGYND WCSGRGIFFN TAKNFLVWVN EEDHLRLISM QKGGDLAAVY
KRLVVAINTM TASGLSFAKR DGLGYLTFCP SNLGTALRAS VHMKIPNLAA SPEFKSFCDN
LNIQARGIHG EHTESVGGVY DLSNKRRLGL TEYQAVEEMR VGVEACLAKE KELAAAKK
//
