KITM_MACFA
ID KITM_MACFA Reviewed; 265 AA.
AC Q9N0C5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Thymidine kinase 2, mitochondrial {ECO:0000305};
DE EC=2.7.1.21 {ECO:0000250|UniProtKB:Q9R088};
DE AltName: Full=2'-deoxyuridine kinase TK2 {ECO:0000305};
DE EC=2.7.1.74 {ECO:0000250|UniProtKB:Q9R088};
DE AltName: Full=Deoxycytidine kinase TK2 {ECO:0000305};
DE EC=2.7.1.- {ECO:0000250|UniProtKB:Q9R088};
DE Flags: Precursor;
GN Name=TK2; ORFNames=QccE-13136;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates thymidine, deoxycytidine, and deoxyuridine in
CC the mitochondrial matrix (By similarity). In non-replicating cells,
CC where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis
CC depends solely on TK2 and DGUOK (By similarity).
CC {ECO:0000250|UniProtKB:O00142, ECO:0000250|UniProtKB:Q9R088}.
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:0000250|UniProtKB:Q9R088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19130;
CC Evidence={ECO:0000250|UniProtKB:Q9R088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine + ATP = ADP + dCMP + H(+);
CC Xref=Rhea:RHEA:46040, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:456216;
CC EC=2.7.1.74; Evidence={ECO:0000250|UniProtKB:Q9R088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46041;
CC Evidence={ECO:0000250|UniProtKB:Q9R088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyuridine + ATP = ADP + dUMP + H(+);
CC Xref=Rhea:RHEA:28206, ChEBI:CHEBI:15378, ChEBI:CHEBI:16450,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:246422, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9R088};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28207;
CC Evidence={ECO:0000250|UniProtKB:Q9R088};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9R088}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9R088}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; AB046005; BAB01587.1; -; mRNA.
DR RefSeq; NP_001272031.1; NM_001285102.1.
DR AlphaFoldDB; Q9N0C5; -.
DR SMR; Q9N0C5; -.
DR STRING; 9541.XP_005592209.1; -.
DR GeneID; 102139352; -.
DR CTD; 7084; -.
DR eggNOG; KOG4235; Eukaryota.
DR OrthoDB; 1505356at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA synthesis; Kinase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..265
FT /note="Thymidine kinase 2, mitochondrial"
FT /id="PRO_0000016843"
FT REGION 21..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O57203"
FT BINDING 57..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O57203"
SQ SEQUENCE 265 AA; 30744 MW; 6104E608C0E809A0 CRC64;
MLLRPLRGWA ALALRCFEPG SPGSPASGPG SRRVQRGAWP SDKEREKEKK SVICVEGNIA
SGKTTCLEFF SNATDIEVLT EPVSKWRNVR GHNPLGLMYQ DASRWGLTLQ TYVQLTMLDR
HTCPQVSSVR LMERSIHSAR YIFVENLYRS GKMPEVDYVV LSEWFDWILR NMDVSIDLIV
YLRTNPETCY QRLKRRCREE EKVIPLEYLE AIHHLHEEWL IKGSLFPVAA PVLVIEADHH
MERMLQLFEQ NRDRILTPEN RKLGP