KTHY2_SULTO
ID KTHY2_SULTO Reviewed; 213 AA.
AC Q970Q8; F9VNH1;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=tmk; OrderedLocusNames=STK_15430;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of dTMP kinase (ST1543) from Sulfolobus tokodaii strain
RT 7.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC ChEBI:CHEBI:456216; EC=2.7.4.9;
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR EMBL; BA000023; BAK54617.1; -; Genomic_DNA.
DR RefSeq; WP_010979593.1; NC_003106.2.
DR PDB; 2PLR; X-ray; 1.60 A; A/B=1-213.
DR PDB; 4NZY; X-ray; 2.15 A; A/B=1-213.
DR PDB; 4RZU; X-ray; 2.80 A; A/B=1-213.
DR PDB; 4RZX; X-ray; 2.30 A; A/B=1-213.
DR PDB; 5H70; X-ray; 2.40 A; A/B=1-213.
DR PDBsum; 2PLR; -.
DR PDBsum; 4NZY; -.
DR PDBsum; 4RZU; -.
DR PDBsum; 4RZX; -.
DR PDBsum; 5H70; -.
DR AlphaFoldDB; Q970Q8; -.
DR SMR; Q970Q8; -.
DR STRING; 273063.STK_15430; -.
DR EnsemblBacteria; BAK54617; BAK54617; STK_15430.
DR GeneID; 1459579; -.
DR KEGG; sto:STK_15430; -.
DR PATRIC; fig|273063.9.peg.1754; -.
DR eggNOG; arCOG01891; Archaea.
DR OMA; WIHEVIK; -.
DR OrthoDB; 114844at2157; -.
DR BRENDA; 2.7.4.9; 15396.
DR EvolutionaryTrace; Q970Q8; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..213
FT /note="Probable thymidylate kinase"
FT /id="PRO_0000155401"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2PLR"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2PLR"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:2PLR"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2PLR"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:2PLR"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:2PLR"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2PLR"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:2PLR"
FT TURN 148..155
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 161..179
FT /evidence="ECO:0007829|PDB:2PLR"
FT TURN 180..184
FT /evidence="ECO:0007829|PDB:2PLR"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:2PLR"
FT HELIX 194..210
FT /evidence="ECO:0007829|PDB:2PLR"
SQ SEQUENCE 213 AA; 24595 MW; 67B805796F6BE20D CRC64;
MKKGVLIAFE GIDGSGKSSQ ATLLKDWIEL KRDVYLTEWN SSDWIHDIIK EAKKKDLLTP
LTFSLIHATD FSDRYERYIL PMLKSGFIVI SDRYIYTAYA RDSVRGVDID WVKKLYSFAI
KPDITFYIRV SPDIALERIK KSKRKIKPQE AGADIFPGLS PEEGFLKYQG LITEVYDKLV
KDENFIVIDG TKTPKEIQIQ IRKFVGELID NSF
