KITH_EHV4
ID KITH_EHV4 Reviewed; 352 AA.
AC P24425;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_04029};
DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_04029};
GN Name=TK {ECO:0000255|HAMAP-Rule:MF_04029};
OS Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10333;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2391500; DOI=10.1099/0022-1317-71-8-1801;
RA Nicolson L., Cullinane A.A., Onions D.E.;
RT "The nucleotide sequence of the equine herpesvirus 4 thymidine kinase
RT gene.";
RL J. Gen. Virol. 71:1801-1805(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-352 IN COMPLEXES WITH
RP THYMIDINE; ADP AND BISUBSTRATE ANALOGS, ACTIVE SITE, CATALYTIC ACTIVITY,
RP AND SUBUNIT.
RX PubMed=14527394; DOI=10.1016/j.str.2003.09.003;
RA Gardberg A., Shuvalova L., Monnerjahn C., Konrad M., Lavie A.;
RT "Structural basis for the dual thymidine and thymidylate kinase activity of
RT herpes thymidine kinases.";
RL Structure 11:1265-1277(2003).
CC -!- FUNCTION: Catalyzes the transfer of the gamma-phospho group of ATP to
CC thymidine to generate dTMP in the salvage pathway of pyrimidine
CC synthesis. The dTMP serves as a substrate for DNA polymerase during
CC viral DNA replication. Allows the virus to be reactivated and to grow
CC in non-proliferative cells lacking a high concentration of
CC phosphorylated nucleic acid precursors. {ECO:0000255|HAMAP-
CC Rule:MF_04029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04029,
CC ECO:0000269|PubMed:14527394};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_04029,
CC ECO:0000269|PubMed:14527394}.
CC -!- SIMILARITY: Belongs to the herpesviridae thymidine kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_04029}.
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DR EMBL; D14486; BAA03378.1; -; Genomic_DNA.
DR PIR; A36657; KIBEE4.
DR PDB; 1P6X; X-ray; 2.00 A; A/B=23-352.
DR PDB; 1P72; X-ray; 2.10 A; A/B=23-352.
DR PDB; 1P73; X-ray; 2.70 A; A/B/C/D=23-352.
DR PDB; 1P75; X-ray; 3.02 A; A/B/C/D=23-352.
DR PDBsum; 1P6X; -.
DR PDBsum; 1P72; -.
DR PDBsum; 1P73; -.
DR PDBsum; 1P75; -.
DR SMR; P24425; -.
DR DrugBank; DB03280; p1-(5'-adenosyl)p5-(5'-thymidyl)pentaphosphate.
DR DrugBank; DB04485; Thymidine.
DR PRIDE; P24425; -.
DR EvolutionaryTrace; P24425; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006230; P:TMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04029; HSV_KITH; 1.
DR InterPro; IPR001889; Herpes_TK.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00693; Herpes_TK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA synthesis; Early protein; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..352
FT /note="Thymidine kinase"
FT /id="PRO_0000175067"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029,
FT ECO:0000269|PubMed:14527394, ECO:0007744|PDB:1P72"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029,
FT ECO:0000269|PubMed:14527394, ECO:0007744|PDB:1P72"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029,
FT ECO:0000269|PubMed:14527394, ECO:0007744|PDB:1P72"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14527394,
FT ECO:0007744|PDB:1P72"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14527394,
FT ECO:0007744|PDB:1P72"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029,
FT ECO:0000269|PubMed:14527394, ECO:0007744|PDB:1P72"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1P6X"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:1P6X"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 91..117
FT /evidence="ECO:0007829|PDB:1P6X"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1P6X"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:1P6X"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 205..226
FT /evidence="ECO:0007829|PDB:1P6X"
FT TURN 231..237
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:1P6X"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:1P6X"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:1P6X"
FT HELIX 333..350
FT /evidence="ECO:0007829|PDB:1P6X"
SQ SEQUENCE 352 AA; 38784 MW; F925ACF592077456 CRC64;
MAACVPPGEA PRSASGTPTR RQVTIVRIYL DGVYGIGKST TGRVMASAAS GGSPTLYFPE
PMAYWRTLFE TDVISGIYDT QNRKQQGNLA VDDAALITAH YQSRFTTPYL ILHDHTCTLF
GGNSLQRGTQ PDLTLVFDRH PVASTVCFPA ARYLLGDMSM CALMAMVATL PREPQGGNIV
VTTLNVEEHI RRLRTRARIG EQIDITLIAT LRNVYFMLVN TCHFLRSGRV WRDGWGELPT
SCGAYKHRAT QMDAFQERVS PELGDTLFAL FKTQELLDDR GVILEVHAWA LDALMLKLRN
LNVFSADLSG TPRQCAAVVE SLLPLMSSTL SDFDSASALE RAARTFNAEM GV
