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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
 
 
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