KARG0_PENVA
ID KARG0_PENVA Reviewed; 356 AA.
AC Q004B5;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Arginine kinase Lit v 2.0101 {ECO:0000305};
DE EC=2.7.3.3 {ECO:0000269|PubMed:17496423, ECO:0000269|PubMed:22750864, ECO:0000269|PubMed:23873077, ECO:0000269|PubMed:27072556};
DE AltName: Full=Allergen Lit v 2 {ECO:0000303|PubMed:17496423};
DE AltName: Full=Arginine kinase {ECO:0000303|PubMed:17496423, ECO:0000303|PubMed:22750864, ECO:0000303|PubMed:23873077, ECO:0000303|PubMed:27072556, ECO:0000312|EMBL:ABI98020.1};
DE Short=AK {ECO:0000303|PubMed:17496423, ECO:0000303|PubMed:22750864, ECO:0000303|PubMed:23873077, ECO:0000303|PubMed:27072556};
DE AltName: Full=LvAK {ECO:0000303|PubMed:22750864, ECO:0000303|PubMed:23873077, ECO:0000303|PubMed:27072556};
DE AltName: Allergen=Lit v 2.0101 {ECO:0000305};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689;
RN [1] {ECO:0000312|EMBL:ABI98020.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-15; 310-328; 316-329 AND
RP 331-340, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Muscle {ECO:0000303|PubMed:17496423, ECO:0000312|EMBL:ABI98020.1};
RX PubMed=17496423; DOI=10.1159/000102610;
RA Garcia-Orozco K.D., Aispuro-Hernandez E., Yepiz-Plascencia G.,
RA Calderon-de-la-Barca A.M., Sotelo-Mundo R.R.;
RT "Molecular characterization of arginine kinase, an allergen from the shrimp
RT Litopenaeus vannamei.";
RL Int. Arch. Allergy Immunol. 144:23-28(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND TISSUE SPECIFICITY.
RX PubMed=27072556; DOI=10.1007/s10863-016-9660-1;
RA Lopez-Zavala A.A., Sotelo-Mundo R.R., Hernandez-Flores J.M.,
RA Lugo-Sanchez M.E., Sugich-Miranda R., Garcia-Orozco K.D.;
RT "Arginine kinase shows nucleoside diphosphate kinase-like activity toward
RT deoxythymidine diphosphate.";
RL J. Bioenerg. Biomembr. 48:301-308(2016).
RN [3] {ECO:0007744|PDB:4AM1}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-356, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=22750864; DOI=10.1107/s1744309112020180;
RA Lopez-Zavala A.A., Sotelo-Mundo R.R., Garcia-Orozco K.D., Isac-Martinez F.,
RA Brieba L.G., Rudino-Pinera E.;
RT "Crystallization and X-ray diffraction studies of arginine kinase from the
RT white Pacific shrimp Litopenaeus vannamei.";
RL Acta Crystallogr. F Struct. Biol. Commun. 68:783-785(2012).
RN [4] {ECO:0007744|PDB:4BG4, ECO:0007744|PDB:4BHL}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ADP AND ARGININE,
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=23873077; DOI=10.1007/s10863-013-9521-0;
RA Lopez-Zavala A.A., Garcia-Orozco K.D., Carrasco-Miranda J.S.,
RA Sugich-Miranda R., Velazquez-Contreras E.F., Criscitiello M.F.,
RA Brieba L.G., Rudino-Pinera E., Sotelo-Mundo R.R.;
RT "Crystal structure of shrimp arginine kinase in binary complex with
RT arginine-a molecular view of the phosphagen precursor binding to the
RT enzyme.";
RL J. Bioenerg. Biomembr. 45:511-518(2013).
CC -!- FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-
CC phosphate group to L-arginine (PubMed:17496423, PubMed:27072556,
CC PubMed:22750864, PubMed:23873077). Has nucleoside diphosphate kinase-
CC like activity toward dTDP. Binds and phosphorylates dTDP using ATP as a
CC phosphate donor. Does not phosphorylate dADP, dCDP, dGDP, dTMP or
CC thymidine (PubMed:27072556). {ECO:0000269|PubMed:17496423,
CC ECO:0000269|PubMed:22750864, ECO:0000269|PubMed:23873077,
CC ECO:0000269|PubMed:27072556}.
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:17496423, ECO:0000269|PubMed:22750864,
CC ECO:0000269|PubMed:23873077, ECO:0000269|PubMed:27072556};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22941;
CC Evidence={ECO:0000305|PubMed:17496423, ECO:0000305|PubMed:22750864,
CC ECO:0000305|PubMed:23873077, ECO:0000305|PubMed:27072556};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22942;
CC Evidence={ECO:0000305|PubMed:17496423, ECO:0000305|PubMed:22750864,
CC ECO:0000305|PubMed:23873077, ECO:0000305|PubMed:27072556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:27072556};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.099 mM for ATP (at pH 8.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27072556};
CC KM=0.322 mM for L-arginine (at pH 8.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27072556};
CC KM=0.653 mM for dTDP (at pH 8.6 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:27072556};
CC Vmax=1.43 umol/min/mg enzyme toward dTDP (at pH 8.6 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:27072556};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22750864}.
CC -!- TISSUE SPECIFICITY: Muscle (at protein level).
CC {ECO:0000269|PubMed:17496423, ECO:0000269|PubMed:22750864,
CC ECO:0000269|PubMed:23873077, ECO:0000269|PubMed:27072556}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 100% of
CC the 5 shrimp-allergic patients tested. {ECO:0000269|PubMed:17496423}.
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; DQ975203; ABI98020.1; -; mRNA.
DR PDB; 4AM1; X-ray; 1.25 A; A=2-356.
DR PDB; 4BG4; X-ray; 1.60 A; A/B=1-356.
DR PDB; 4BHL; X-ray; 1.90 A; A=1-356.
DR PDBsum; 4AM1; -.
DR PDBsum; 4BG4; -.
DR PDBsum; 4BHL; -.
DR AlphaFoldDB; Q004B5; -.
DR SMR; Q004B5; -.
DR Allergome; 3544; Lit v 2.
DR Allergome; 3616; Lit v 2.0101.
DR BRENDA; 2.7.3.3; 4594.
DR GO; GO:0034618; F:arginine binding; IDA:UniProtKB.
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:0046072; P:dTDP metabolic process; IDA: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 3D-structure; Allergen; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17496423"
FT CHAIN 2..356
FT /note="Arginine kinase Lit v 2.0101"
FT /evidence="ECO:0000305|PubMed:17496423"
FT /id="PRO_0000447429"
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:0000269|PubMed:23873077,
FT ECO:0007744|PDB:4BG4, ECO:0007744|PDB:4BHL"
FT BINDING 122..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843,
FT ECO:0000269|PubMed:23873077, ECO:0007744|PDB:4BG4"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843,
FT ECO:0000269|PubMed:23873077, ECO:0007744|PDB:4BG4"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23873077,
FT ECO:0007744|PDB:4BG4, ECO:0007744|PDB:4BHL"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843,
FT ECO:0000269|PubMed:23873077, ECO:0007744|PDB:4BG4"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23873077,
FT ECO:0007744|PDB:4BG4"
FT BINDING 280..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843,
FT ECO:0000269|PubMed:23873077, ECO:0007744|PDB:4BG4"
FT BINDING 309..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843,
FT ECO:0000269|PubMed:23873077, ECO:0007744|PDB:4BG4"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23873077,
FT ECO:0007744|PDB:4BG4"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:4AM1"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4BG4"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4BG4"
FT STRAND 118..129
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:4AM1"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 218..238
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 239..256
FT /evidence="ECO:0007829|PDB:4AM1"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:4AM1"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:4AM1"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4AM1"
FT HELIX 335..354
FT /evidence="ECO:0007829|PDB:4AM1"
SQ SEQUENCE 356 AA; 40160 MW; 1CFF023A35E0036A CRC64;
MADAAVIEKL EAGFKKLEAA TDCKSLLKKY LTKEVFDKLK DKRTSLGATL LDVIQSGVEN
LDSGVGIYAP DAEAYTLFAP LFDPIIEDYH VGFKQTDKHP NKDFGDVNSF VNVDPEGKFV
ISTRVRCGRS LQGYPFNPCL TESQYKEMEA KVSSTLSSLE GELKGTYYPL TGMSKEVQQK
LIDDHFLFKE GDRFLQAANA CRYWPAGRGI YHNDNKTFLV WVNEEDHLRI ISMQMGGDLG
QVFRRLTSAV NEIEKRIPFS HHDRLGFLTF CPTNLGTTVR ASVHIKLPKL AANREKLEEV
AGKYNLQVRG TRGEHTEAEG GIYDISNKRR MGLTEFQAVK EMQDGILELI KIEKEM
