ID G8C2K3_9MOLU Unreviewed; 194 AA.
AC G8C2K3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
GN Name=tdk {ECO:0000313|EMBL:CCE66551.1};
GN ORFNames=MHM_00330 {ECO:0000313|EMBL:CCE66551.1};
OS Candidatus Mycoplasma haematominutum 'Birmingham 1'.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1116213 {ECO:0000313|EMBL:CCE66551.1};
RN [1] {ECO:0000313|EMBL:CCE66551.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Birmingham 1 {ECO:0000313|EMBL:CCE66551.1};
RA Barker E.N., Darby A.C., Helps C.R., Peters I.R., Hughes M.A.,
RA Radford A.D., Novacco M., Boretti F., Hofmann-Lehmann R., Tasker S.;
RT "Complete genome sequence of Candidatus Mycoplasma haemominutum.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCE66551.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Birmingham 1 {ECO:0000313|EMBL:CCE66551.1};
RA Barker E.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU000544};
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR EMBL; HE613254; CCE66551.1; -; Genomic_DNA.
DR RefSeq; WP_015511416.1; NC_021007.1.
DR AlphaFoldDB; G8C2K3; -.
DR KEGG; mhb:MHM_00330; -.
DR PATRIC; fig|1116213.3.peg.32; -.
DR HOGENOM; CLU_064400_3_0_14; -.
DR OrthoDB; 9781579at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000544};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU000544};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ SEQUENCE 194 AA; 22002 MW; D252E6EDADC99BDB CRC64;
MNSSSAILTV ICGPMKSGKS KELFSIIDRL NYQKIKYIIF KPKIDSRNEN TISSRYYSQS
NEAIIIDEQN PQEILNYIPE NSLEPLTTLI DEAHFFSSEL ISVVKSLLSK EVNVIISGLD
LDANMKTFGP MGDLLALSNK IKKLNSVCER CYNVANFSAL KDSQQSFEKD NILVGNEQYI
VLCRNCYLRH TQKC
//
