TYSY_HHV8P
ID TYSY_HHV8P Reviewed; 337 AA.
AC P90463; D0UZM0; Q2HRC4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Thymidylate synthase;
DE Short=TS;
DE Short=TSase;
DE EC=2.1.1.45;
GN Name=70;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8962146; DOI=10.1073/pnas.93.25.14862;
RA Russo J.J., Bohenzky R.A., Chien M.-C., Chen J., Yan M., Maddalena D.,
RA Parry J.P., Peruzzi D., Edelman I.S., Chang Y., Moore P.S.;
RT "Nucleotide sequence of the Kaposi sarcoma-associated herpesvirus (HHV8).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14862-14867(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9151804; DOI=10.1128/jvi.71.6.4187-4192.1997;
RA Neipel F., Albrecht J.-C., Fleckenstein B.;
RT "Cell-homologous genes in the Kaposi's sarcoma-associated rhadinovirus
RT human herpesvirus 8: determinants of its pathogenicity?";
RL J. Virol. 71:4187-4192(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-
CC dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422;
CC EC=2.1.1.45;
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR EMBL; U75698; AAC57092.1; -; Genomic_DNA.
DR EMBL; U83348; AAC56948.1; -; Genomic_DNA.
DR EMBL; U93872; AAB62673.1; -; Genomic_DNA.
DR EMBL; U71365; AAC34940.1; -; Genomic_DNA.
DR EMBL; AF148805; ABD28859.1; -; Genomic_DNA.
DR RefSeq; YP_001129361.1; NC_009333.1.
DR PDB; 5H38; X-ray; 1.70 A; A/B=51-334.
DR PDB; 5H39; X-ray; 2.00 A; A/B=51-335.
DR PDB; 5H3A; X-ray; 2.40 A; A/B=51-333.
DR PDBsum; 5H38; -.
DR PDBsum; 5H39; -.
DR PDBsum; 5H3A; -.
DR SMR; P90463; -.
DR BioGRID; 1776984; 10.
DR PRIDE; P90463; -.
DR DNASU; 4961481; -.
DR GeneID; 4961481; -.
DR KEGG; vg:4961481; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR Gene3D; 3.30.572.10; -; 1.
DR HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR InterPro; IPR000398; Thymidylate_synthase.
DR InterPro; IPR020940; Thymidylate_synthase_AS.
DR PANTHER; PTHR11548; PTHR11548; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF55831; SSF55831; 1.
DR TIGRFAMs; TIGR03284; thym_sym; 1.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..337
FT /note="Thymidylate synthase"
FT /id="PRO_0000141065"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 74
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 199..200
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 239..242
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 242
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 250
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 280..282
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT BINDING 336
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P0A884"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5H3A"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:5H38"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:5H3A"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 231..242
FT /evidence="ECO:0007829|PDB:5H38"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 247..265
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 268..282
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:5H38"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:5H39"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5H38"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:5H38"
SQ SEQUENCE 337 AA; 38555 MW; D0EB0CE60A3384EC CRC64;
MFPFVPLSLY VAKKLFRARG FRFCQKPGVL ALAPEVDPCS IQHEVTGAET PHEELQYLRQ
LREILCRGSD RLDRTGIGTL SLFGMQARYS LRDHFPLLTT KRVFWRGVVQ ELLWFLKGST
DSRELSRTGV KIWDKNGSRE FLAGRGLAHR REGDLGPVYG FQWRHFGAAY VDADADYTGQ
GFDQLSYIVD LIKNNPHDRR IIMCAWNPAD LSLMALPPCH LLCQFYVADG ELSCQLYQRS
GDMGLGVPFN IASYSLLTYM LAHVTGLRPG EFIHTLGDAH IYKTHIEPLR LQLTRTPRPF
PRLEILRSVS SMEEFTPDDF RLVDYCPHPT IRMEMAV
