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Database: UniProt/TrEMBL
Entry: M4UMG2_9GAMM
LinkDB: M4UMG2_9GAMM
Original site: M4UMG2_9GAMM 
ID   M4UMG2_9GAMM            Unreviewed;       194 AA.
AC   M4UMG2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124};
DE            EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124};
GN   Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124};
GN   ORFNames=PCNPT3_08660 {ECO:0000313|EMBL:AGH81670.1};
OS   Psychromonas sp. CNPT3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH81670.1, ECO:0000313|Proteomes:UP000010320};
RN   [1] {ECO:0000313|EMBL:AGH81670.1, ECO:0000313|Proteomes:UP000010320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNPT3 {ECO:0000313|EMBL:AGH81670.1,
RC   ECO:0000313|Proteomes:UP000010320};
RA   Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J.,
RA   Yayanos A.A., Bartlett D.H.;
RT   "The complete genome sequence of the deep-sea bacterium Psychromonas
RT   CNPT2.";
RL   Submitted (MAR-2013) 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|HAMAP-Rule:MF_00124,
CC         ECO:0000256|RuleBase:RU000544};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|HAMAP-Rule:MF_00124,
CC       ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CP004404; AGH81670.1; -; Genomic_DNA.
DR   RefSeq; WP_015465549.1; NC_020802.1.
DR   AlphaFoldDB; M4UMG2; -.
DR   STRING; 314282.PCNPT3_08660; -.
DR   KEGG; psy:PCNPT3_08660; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_2_1_6; -.
DR   OrthoDB; 9781579at2; -.
DR   Proteomes; UP000010320; 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; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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|HAMAP-
KW   Rule:MF_00124}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634, ECO:0000256|HAMAP-
KW   Rule:MF_00124};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00124};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00124}; Reference proteome {ECO:0000313|Proteomes:UP000010320};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   ACT_SITE        88
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124,
FT                   ECO:0000256|PIRSR:PIRSR035805-1"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         87..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
SQ   SEQUENCE   194 AA;  21827 MW;  F1168E4DA6539764 CRC64;
     MAQLYFYYSA MNAGKSTALL QSSYNYRERG MNTLVLTPSI DDRAGVGKVA SRIGLECDAQ
     AFTVNDNLAN IIEASHKEKK QHCILFDEAQ FLTKEQVKQL TYVVDILDIP VLCYGIKTDF
     QGELFSGSHY LLAWADKLVE LKTICHCGRK ANMILRLDSQ GNVISEGDQI SIGGNESYES
     VCRKHFRDVV WDVK
//
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