KARG_HOMGA
ID KARG_HOMGA Reviewed; 356 AA.
AC P14208;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Arginine kinase;
DE Short=AK;
DE EC=2.7.3.3;
OS Homarus gammarus (European lobster) (Homarus vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Nephropoidea; Nephropidae; Homarus.
OX NCBI_TaxID=6707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=8408011; DOI=10.1016/s0021-9258(20)80583-3;
RA Dumas C., Camonis J.;
RT "Cloning and sequence analysis of the cDNA for arginine kinase of lobster
RT muscle.";
RL J. Biol. Chem. 268:21599-21605(1993).
RN [2]
RP PRELIMINARY PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2.
RX PubMed=6262257; DOI=10.1111/j.1399-3011.1981.tb01977.x;
RA Regnouf F., Kassab R., Debuire B., Richard C., Han K.K.;
RT "Primary structure of lobster-muscle arginine kinase. Amino and carboxyl-
RT terminal structure of the enzyme and complete alignment of the cyanogen-
RT bromide peptides.";
RL Int. J. Pept. Protein Res. 17:143-155(1981).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 176-233.
RX PubMed=16871; DOI=10.1093/oxfordjournals.jbchem.a131496;
RA Debuire B., Han K.K., Dautrevaux M., Biserte G., Regnouf F., Kassab R.;
RT "Amino acid sequence of a cyanogen bromide fragment containing the two
RT tryptophanyl residues of lobster arginine kinase (Homarus vulgaris).";
RL J. Biochem. 81:611-619(1977).
RN [4]
RP PROTEIN SEQUENCE OF 332-342.
RX PubMed=164417; DOI=10.1111/j.1399-3011.1975.tb02415.x;
RA Debuire B., Han K.K., Dautrevaux M., Biserte G.;
RT "Isolation and characterization of the cyanogen bromide fragments of
RT lobster arginine kinase (homarus vulgaris).";
RL Int. J. Pept. Protein Res. 7:69-80(1975).
RN [5]
RP PRELIMINARY PARTIAL PROTEIN SEQUENCE.
RX PubMed=4622086;
RA Han K.K., Debuire B., Dautrevaux M., Biserte G., Fattoum A., Regnouf F.,
RA Kassab R., Pradel L.A.;
RT "Amino acid sequence of a fragment obtained by the cleavage of lobster
RT (Homarus gammarus L.) arginine-kinase by cyanogen bromide.";
RL C. R. Hebd. Seances Acad. Sci., D, Sci. Nat. 274:324-326(1972).
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 -!- 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; X68703; CAA48654.1; -; mRNA.
DR PIR; A48590; AKLO.
DR AlphaFoldDB; P14208; -.
DR SMR; P14208; -.
DR Allergome; 791; Hom g 2.
DR iPTMnet; P14208; -.
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; 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 Acetylation; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..356
FT /note="Arginine kinase"
FT /id="PRO_0000211999"
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 /evidence="ECO:0000250"
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="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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 BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:6262257"
SQ SEQUENCE 356 AA; 39984 MW; F0A77136EBC0CA99 CRC64;
MADAATIAKL EEGFKKLEAA TDCKSLLKKY LSKDIFDSLK AKKTSLGATL LDVIQSGVEN
LDSGVGIYAP DAEAYSLFAP LFDPIIEDYH KGFKQTDKHP AKDFGDVSKF INVDPEGTFV
ISTRVRCGRS MEGYPFNPCL TEAQYKEMEE KVSSTLSGLE GELKGSYFPL TGMTKEVQQK
LIDDHFLFKE GDRFLQAANA CRYWPAGRGI YHNDNKTFLV WCNEEDHLRI ISMQMGGDLG
QVYRRLVSAV NDIEKRVPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKL AANREKLEEV
AAKFSLQVRG TRGEHTEAEG GIYDISNKRR MGLTEFQAVK EMQDGILELI KIEKEM
