ID A0A0Q9M1Q6_9MICO Unreviewed; 224 AA.
AC A0A0Q9M1Q6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ORFNames=ASG70_09485 {ECO:0000313|EMBL:KRE55561.1};
OS Phycicoccus sp. Soil748.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE55561.1, ECO:0000313|Proteomes:UP000051855};
RN [1] {ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE55561.1, ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE55561.1,
RC ECO:0000313|Proteomes:UP000051855};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRE55561.1}.
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DR EMBL; LMSC01000007; KRE55561.1; -; Genomic_DNA.
DR RefSeq; WP_056883988.1; NZ_LMSC01000007.1.
DR AlphaFoldDB; A0A0Q9M1Q6; -.
DR STRING; 1736397.ASG70_09485; -.
DR OrthoDB; 9781579at2; -.
DR Proteomes; UP000051855; Unassembled WGS sequence.
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 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.
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 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ SEQUENCE 224 AA; 24766 MW; 4C8438577A2DEC52 CRC64;
MAELVFFSGT MDCGKSTLAL QMDHNHRARG RSGIIYTKLD RAGTDVLSSR LGLSTPAHEV
GDELDFWDAV VEHATQGLRI DYLICDEVQF YTPAQVEQLA RLVDEMGIDV FAFGITADFR
TQLFPGSRRM IELADKVQVL QVEALCWCGR RATHNARVVD GAMVVEGEQV VVGDTKAGTE
TLVEYEVLCR RHFMRRMNSA AARAAASSPD VLPFDLDLCP VPPC
//
