KARG_PENVA
ID KARG_PENVA Reviewed; 356 AA.
AC B0FRF9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Arginine kinase Lit v 2 {ECO:0000305};
DE EC=2.7.3.3 {ECO:0000269|PubMed:19239924};
DE AltName: Full=Arginine kinase {ECO:0000303|PubMed:19239924, ECO:0000312|EMBL:ABY57915.1};
DE Short=AK {ECO:0000303|PubMed:19239924};
DE AltName: Allergen=Lit v 2 {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:ABY57915.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Muscle {ECO:0000303|PubMed:19239924};
RX PubMed=19239924; DOI=10.1016/j.fsi.2009.02.012;
RA Yao C.L., Ji P.F., Kong P., Wang Z.Y., Xiang J.H.;
RT "Arginine kinase from Litopenaeus vannamei: cloning, expression and
RT catalytic properties.";
RL Fish Shellfish Immunol. 26:553-558(2009).
CC -!- FUNCTION: Catalyzes the reversible transfer of high energy ATP gamma-
CC phosphate group to L-arginine. {ECO:0000269|PubMed:19239924}.
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:19239924};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22941;
CC Evidence={ECO:0000305|PubMed:19239924};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22942;
CC Evidence={ECO:0000305|PubMed:19239924};
CC -!- ACTIVITY REGULATION: No change in activity after supplementation with
CC 10 mM glucose. However, activity decreases significantly when glucose
CC concentration is higher than 50 mM and almost all activity is lost with
CC 200 mM glucose. Activity is significantly increased after treatment
CC with 10 mM and 50 mM ATP. However, activity drops significantly with
CC 200 mM ATP. Inhibited by 10-200 mM alpha-ketoglutarate. No change in
CC activity after incubation with 10-200 mM L-citrulline, L-ornaline or
CC glycerol. {ECO:0000269|PubMed:19239924}.
CC -!- TISSUE SPECIFICITY: Expressed in muscle (at protein level). Expressed
CC in muscle, heart, nerve, stomach and hemocytes, with the highest
CC expression in muscle. Very low expression in eyestalk and intestine.
CC Not expressed in hepatopancreas, gill and skin.
CC {ECO:0000269|PubMed:19239924}.
CC -!- INDUCTION: By LPS immunostimulation. In hemocytes, expression increases
CC sharply at 3 hours, decreases slightly at 6 hours, increases
CC significantly again at 24 hours and decreases at 48 hours after LPS
CC injection. In muscle, expressed less than the control in the first 6
CC hours, then the expression increases strikingly from 6 to 24 hours and
CC decreases at 48 hours after LPS injection.
CC {ECO:0000269|PubMed:19239924}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE
CC (Probable). {ECO:0000305}.
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; EU346737; ABY57915.1; -; mRNA.
DR AlphaFoldDB; B0FRF9; -.
DR SMR; B0FRF9; -.
DR Allergome; 3544; Lit v 2.
DR BioCyc; MetaCyc:MON-18221; -.
DR BRENDA; 2.7.3.3; 4594.
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: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..356
FT /note="Arginine kinase Lit v 2"
FT /evidence="ECO:0000250|UniProtKB:Q004B5"
FT /id="PRO_0000447431"
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"
SQ SEQUENCE 356 AA; 40168 MW; E9C88AE671AB1BBB 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 KMEKEM
