KITH_CLOAB
ID KITH_CLOAB Reviewed; 195 AA.
AC Q97F65;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124};
DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124};
GN Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124}; OrderedLocusNames=CA_C2887;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-191 IN COMPLEX WITH ZINC IONS
RP AND ADP.
RG Northeast structural genomics consortium (NESG);
RT "X-ray structure of clostridium acetobutylicum genomics target CAR26.";
RL Submitted (FEB-2009) to the PDB data bank.
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_00124};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00124}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001437; AAK80830.1; -; Genomic_DNA.
DR PIR; C97255; C97255.
DR RefSeq; NP_349490.1; NC_003030.1.
DR RefSeq; WP_010966171.1; NC_003030.1.
DR PDB; 1XX6; X-ray; 2.00 A; A/B=1-191.
DR PDBsum; 1XX6; -.
DR AlphaFoldDB; Q97F65; -.
DR SMR; Q97F65; -.
DR STRING; 272562.CA_C2887; -.
DR EnsemblBacteria; AAK80830; AAK80830; CA_C2887.
DR GeneID; 44999375; -.
DR KEGG; cac:CA_C2887; -.
DR PATRIC; fig|272562.8.peg.3071; -.
DR eggNOG; COG1435; Bacteria.
DR HOGENOM; CLU_064400_3_0_9; -.
DR OMA; GWLELIC; -.
DR OrthoDB; 1279539at2; -.
DR BRENDA; 2.7.1.21; 1452.
DR EvolutionaryTrace; Q97F65; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00124; Thymidine_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; PTHR11441; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..195
FT /note="Thymidine kinase"
FT /id="PRO_0000174967"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 57..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 88..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:1XX6"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1XX6"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1XX6"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1XX6"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1XX6"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1XX6"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1XX6"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1XX6"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1XX6"
SQ SEQUENCE 195 AA; 22303 MW; 6EDB551986B203BA CRC64;
MYRPKDHGWV EVIVGPMYSG KSEELIRRIR RAKIAKQKIQ VFKPEIDNRY SKEDVVSHMG
EKEQAVAIKN SREILKYFEE DTEVIAIDEV QFFDDEIVEI VNKIAESGRR VICAGLDMDF
RGKPFGPIPE LMAIAEFVDK IQAICVVCGN PATRTQRLIN GKPAFYDDPV VLIGAMESYE
ARCRKCHVVP QKKEV
