KARG_METEN
ID KARG_METEN Reviewed; 357 AA.
AC B1PVZ9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Arginine kinase Met e 2 {ECO:0000303|PubMed:12496430, ECO:0000303|PubMed:19341812, ECO:0000303|PubMed:21507330, ECO:0000303|PubMed:21645540};
DE Short=AK {ECO:0000303|PubMed:19341812, ECO:0000303|PubMed:21507330, ECO:0000303|PubMed:21645540};
DE EC=2.7.3.3 {ECO:0000269|PubMed:12496430, ECO:0000269|PubMed:19341812, ECO:0000269|PubMed:21507330, ECO:0000269|PubMed:21645540};
DE AltName: Allergen=Met e 2 {ECO:0000305};
OS Metapenaeus ensis (Greasyback shrimp) (Penaeus ensis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Metapenaeus.
OX NCBI_TaxID=32278;
RN [1] {ECO:0000312|EMBL:ACA51932.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Muscle {ECO:0000303|PubMed:19341812};
RX PubMed=19341812; DOI=10.1016/j.cbpb.2009.03.010;
RA Wang J.S., Zheng Z.L., Lei J., Pan J.C., Zou G.L.;
RT "Cloning, expression, characterization and phylogenetic analysis of
RT arginine kinase from greasyback shrimp (Metapenaeus ensis).";
RL Comp. Biochem. Physiol. 153:268-274(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND ALLERGEN.
RX PubMed=12496430; DOI=10.4049/jimmunol.170.1.445;
RA Yu C.J., Lin Y.F., Chiang B.L., Chow L.P.;
RT "Proteomics and immunological analysis of a novel shrimp allergen, Pen m
RT 2.";
RL J. Immunol. 170:445-453(2003).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=17487536; DOI=10.1007/s10126-007-9006-4;
RA Lo T.S., Cui Z., Mong J.L., Wong Q.W., Chan S.M., Kwan H.S., Chu K.H.;
RT "Molecular coordinated regulation of gene expression during ovarian
RT development in the penaeid shrimp.";
RL Mar. Biotechnol. 9:459-468(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-271.
RX PubMed=21507330; DOI=10.1016/j.ijbiomac.2011.04.002;
RA Liu N., Wang J.S., Wang W.D., Pan J.C.;
RT "The role of Cys271 in conformational changes of arginine kinase.";
RL Int. J. Biol. Macromol. 49:98-102(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-62 AND ARG-193.
RX PubMed=21645540; DOI=10.1016/j.ijbiomac.2011.05.022;
RA Liu N., Wang J.S., Wang W.D., Pan J.C.;
RT "The interaction between residues 62 and 193 play a key role in activity
RT and structural stability of arginine kinase.";
RL Int. J. Biol. Macromol. 49:402-408(2011).
CC -!- FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-
CC phosphate group to L-arginine. {ECO:0000269|PubMed:12496430,
CC ECO:0000269|PubMed:19341812, ECO:0000269|PubMed:21507330,
CC ECO:0000269|PubMed:21645540}.
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:12496430, ECO:0000269|PubMed:19341812,
CC ECO:0000269|PubMed:21507330, ECO:0000269|PubMed:21645540};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22941;
CC Evidence={ECO:0000305|PubMed:12496430, ECO:0000305|PubMed:19341812,
CC ECO:0000305|PubMed:21507330, ECO:0000305|PubMed:21645540};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22942;
CC Evidence={ECO:0000305|PubMed:12496430, ECO:0000305|PubMed:19341812,
CC ECO:0000305|PubMed:21507330, ECO:0000305|PubMed:21645540};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.33 mM for ATP (at pH 8.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19341812};
CC KM=1.59 mM for L-arginine (at pH 8.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19341812};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:19341812};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:19341812};
CC -!- DEVELOPMENTAL STAGE: Expressed during ovarian development. The highest
CC expression level is detected at stages I (immature with gonado-somatic
CC index (GSI) <2%) and II (late immature with GSI 2% to 3%) of ovarian
CC maturation. Expression decreases from stage III (early mature with GSI
CC 3% to 6%) to V (ripe with GSI >9%), but increases in between at stage
CC IV (late mature with GSI 6% to 9%) of ovarian maturation.
CC {ECO:0000269|PubMed:17487536}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 100% of
CC the 13 shrimp-allergic patients tested. {ECO:0000269|PubMed:12496430}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00843, ECO:0000255|RuleBase:RU000505,
CC ECO:0000305}.
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DR EMBL; EU497674; ACA51932.1; -; mRNA.
DR AlphaFoldDB; B1PVZ9; -.
DR SMR; B1PVZ9; -.
DR Allergome; 793; Met e 2.
DR BRENDA; 2.7.3.3; 9650.
DR GO; GO:0004054; F:arginine kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR GO; GO:0008585; P:female gonad development; IEP:UniProtKB.
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 Allergen; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT CHAIN 2..357
FT /note="Arginine kinase Met e 2"
FT /id="PRO_0000447430"
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|UniProtKB:Q004B5"
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|UniProtKB:Q004B5"
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|UniProtKB:Q004B5"
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|UniProtKB:Q004B5"
FT MUTAGEN 62
FT /note="D->E: Retains almost 90% of the catalytic activity
FT of the wild-type in the forward reaction. Altered three-
FT dimensional conformation and impaired structural stability
FT of the protein."
FT /evidence="ECO:0000269|PubMed:21645540"
FT MUTAGEN 62
FT /note="D->G: Significantly reduced catalytic activity in
FT the forward reaction. Altered three-dimensional
FT conformation and impaired structural stability of the
FT protein."
FT /evidence="ECO:0000269|PubMed:21645540"
FT MUTAGEN 193
FT /note="R->G: Significantly reduced catalytic activity in
FT the forward reaction. Altered three-dimensional
FT conformation and impaired structural stability of the
FT protein."
FT /evidence="ECO:0000269|PubMed:21645540"
FT MUTAGEN 193
FT /note="R->K: Retains almost 90% of the catalytic activity
FT of the wild-type in the forward reaction. Altered three-
FT dimensional conformation and impaired structural stability
FT of the protein."
FT /evidence="ECO:0000269|PubMed:21645540"
FT MUTAGEN 271
FT /note="C->S,A: Loss of catalytic activity in the forward
FT reaction, but has ability to bind the substrate."
FT /evidence="ECO:0000269|PubMed:21507330"
SQ SEQUENCE 357 AA; 40263 MW; 9A89C88AE6776B1B CRC64;
MADAAVIEKL EAGFKKLEAA TDCKSLLKKY LTKEVFDKLK DKKTSLGATL LDVIQSGVEN
LDSGVGIYAP DAEAYTLFAP LFDPIIEDYH VGFKQTDKHP NKDFGDVNSF VNVDPEGKFV
ISTRVRCGRS MQGYPFNPCL TESQYKEMEA KVSSTLSSLE GELKGTYYPL TGMSKEVQQK
LIDDHFLFKE GDRFLQAANA CRYWPAGRGI YHNDNKTFLV WVNEEDHLRI ISMQMGGDLG
QVFRRLTSAV NEIEKRIPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKL AANREKLEEV
AGKYNLQVRG TRGEHTEAEG GIYDISNKRR MGLTEFQAVK EMQDGILELI KIEKEMI
