KARG_STIJA
ID KARG_STIJA Reviewed; 370 AA.
AC Q9XY07;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Arginine kinase;
DE Short=AK;
DE EC=2.7.3.3;
GN Name=AK;
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 13-20; 28-36; 163-168;
RP 173-196; 214-228; 265-279; 311-321 AND 361-265.
RC TISSUE=Muscle;
RX PubMed=10359650; DOI=10.1042/bj3400671;
RA Suzuki T., Kamidochi M., Inoue N., Kawamichi H., Yazawa Y., Furukohri T.,
RA Ellington R.W.;
RT "Arginine kinase evolved twice: evidence that echinoderm arginine kinase
RT originated from creatine kinase.";
RL Biochem. J. 340:671-675(1999).
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: Homodimer.
CC -!- PTM: The N-terminus is blocked.
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; AB025275; BAA76385.1; -; mRNA.
DR PDB; 3JU5; X-ray; 1.75 A; A/B/C/D=1-370.
DR PDB; 3JU6; X-ray; 2.45 A; A/B/C/D=1-370.
DR PDBsum; 3JU5; -.
DR PDBsum; 3JU6; -.
DR AlphaFoldDB; Q9XY07; -.
DR SMR; Q9XY07; -.
DR EvolutionaryTrace; Q9XY07; -.
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 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; 2.
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; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..370
FT /note="Arginine kinase"
FT /id="PRO_0000212005"
FT DOMAIN 6..89
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 115..358
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 118..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 181
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 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 311..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3JU6"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3JU5"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:3JU5"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:3JU5"
FT TURN 195..204
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 213..235
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 236..258
FT /evidence="ECO:0007829|PDB:3JU5"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:3JU5"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 337..359
FT /evidence="ECO:0007829|PDB:3JU5"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:3JU5"
SQ SEQUENCE 370 AA; 42048 MW; FD9DA776E685EDAB CRC64;
MANLNQKKYP AKDDFPNFEG HKSLLSKYLT ADMYAKLRDV ATPSGYTLDR AIQNGVDNPD
FHLGLLAGDE ETYTVFADLF DPVIEEYHNG FKKTDNHKTD LDASKILDDV LDPAYVISSR
VRTGRNIRGM ALSPHVCRSE RRAIEKMVSE ALNSLAADLK GKYYSLMKMD EKTQQQLIDD
HFLFDRPVSR HFTSGGMARD FPDGRGIWHN DKKNFLVWIN EEDHTRIISM QMGGNMKEVF
ERFTRGLTEV EKHIKDKTGK EFMKNDHLGF VLTCPSNLGT GVRCSVHAKL PHMAKDKRFE
EICTKMRLQK RGTSGEFTES VGGVYDISNL DRLGSSEVEQ VNCVIKGVKV LIEMEKKLEK
GESIDDLVPK
