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KTHY_AQUAE
ID   KTHY_AQUAE              Reviewed;         195 AA.
AC   O67099;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=tmk; OrderedLocusNames=aq_969;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000250}.
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; AE000657; AAC07063.1; -; Genomic_DNA.
DR   PIR; H70383; H70383.
DR   RefSeq; NP_213662.1; NC_000918.1.
DR   RefSeq; WP_010880600.1; NC_000918.1.
DR   PDB; 2PBR; X-ray; 1.96 A; A/B=1-195.
DR   PDB; 4S2E; X-ray; 2.35 A; A/B=1-195.
DR   PDB; 4S35; X-ray; 1.55 A; A/B=1-195.
DR   PDB; 5H56; X-ray; 1.70 A; A/B=1-195.
DR   PDB; 5H5B; X-ray; 2.05 A; A/B=1-195.
DR   PDB; 5H5K; X-ray; 2.30 A; A/B=1-195.
DR   PDB; 5XAI; X-ray; 2.00 A; A/B=1-195.
DR   PDB; 5XB2; X-ray; 2.16 A; A/B=1-195.
DR   PDB; 5XB3; X-ray; 1.77 A; A/B=1-195.
DR   PDB; 5XB5; X-ray; 2.23 A; A/B=1-195.
DR   PDB; 5XBH; X-ray; 2.23 A; A/B=1-195.
DR   PDBsum; 2PBR; -.
DR   PDBsum; 4S2E; -.
DR   PDBsum; 4S35; -.
DR   PDBsum; 5H56; -.
DR   PDBsum; 5H5B; -.
DR   PDBsum; 5H5K; -.
DR   PDBsum; 5XAI; -.
DR   PDBsum; 5XB2; -.
DR   PDBsum; 5XB3; -.
DR   PDBsum; 5XB5; -.
DR   PDBsum; 5XBH; -.
DR   AlphaFoldDB; O67099; -.
DR   SMR; O67099; -.
DR   STRING; 224324.aq_969; -.
DR   EnsemblBacteria; AAC07063; AAC07063; aq_969.
DR   KEGG; aae:aq_969; -.
DR   PATRIC; fig|224324.8.peg.762; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_2_0; -.
DR   InParanoid; O67099; -.
DR   OMA; VMTREPG; -.
DR   OrthoDB; 1585072at2; -.
DR   EvolutionaryTrace; O67099; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central.
DR   GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
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; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_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..195
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155230"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   HELIX           13..26
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   STRAND          31..37
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   HELIX           41..52
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   HELIX           57..74
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   HELIX           76..81
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   STRAND          85..90
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   HELIX           92..99
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   TURN            100..103
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   HELIX           107..118
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   HELIX           133..138
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:5H56"
FT   HELIX           149..165
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   STRAND          166..173
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   HELIX           178..189
FT                   /evidence="ECO:0007829|PDB:4S35"
FT   TURN            190..192
FT                   /evidence="ECO:0007829|PDB:4S35"
SQ   SEQUENCE   195 AA;  22370 MW;  F3C2A94D4930956E CRC64;
     MLIAFEGIDG SGKTTQAKKL YEYLKQKGYF VSLYREPGGT KVGEVLREIL LTEELDERTE
     LLLFEASRSK LIEEKIIPDL KRDKVVILDR FVLSTIAYQG YGKGLDVEFI KNLNEFATRG
     VKPDITLLLD IPVDIALRRL KEKNRFENKE FLEKVRKGFL ELAKEEENVV VIDASGEEEE
     VFKEILRALS GVLRV
 
 
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