UniProt/TrEMBL: A0A174WDH3

Database: UniProt/TrEMBL
Entry: A0A174WDH3_9BACE

LinkDB:  A0A174WDH3_9BACE 
Original site:  A0A174WDH3_9BACE

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (7)   
   EMBL (7)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   A0A174WDH3_9BACE        Unreviewed;       199 AA.
AC   A0A174WDH3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ECO:0000313|EMBL:CUQ42477.1};
GN   ORFNames=DWY26_16715 {ECO:0000313|EMBL:RGR68119.1}, DXA49_21750
GN   {ECO:0000313|EMBL:RGY21041.1}, ERS852558_03227
GN   {ECO:0000313|EMBL:CUQ42477.1}, F2Y31_14490
GN   {ECO:0000313|EMBL:KAA5497350.1}, F2Y35_17310
GN   {ECO:0000313|EMBL:KAA5488979.1}, F2Y36_09315
GN   {ECO:0000313|EMBL:KAA5463787.1}, F2Y39_17060
GN   {ECO:0000313|EMBL:KAA5474295.1};
OS   Bacteroides caccae.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=47678 {ECO:0000313|EMBL:CUQ42477.1, ECO:0000313|Proteomes:UP000095725};
RN   [1] {ECO:0000313|EMBL:CUQ42477.1, ECO:0000313|Proteomes:UP000095725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5834946 {ECO:0000313|EMBL:CUQ42477.1,
RC   ECO:0000313|Proteomes:UP000095725};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000284205, ECO:0000313|Proteomes:UP000284431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF24-29LB {ECO:0000313|EMBL:RGR68119.1,
RC   ECO:0000313|Proteomes:UP000284205}, and OF02-6LB
RC   {ECO:0000313|EMBL:RGY21041.1, ECO:0000313|Proteomes:UP000284431};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000368418, ECO:0000313|Proteomes:UP000427825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIOML-A19 {ECO:0000313|EMBL:KAA5497350.1,
RC   ECO:0000313|Proteomes:UP000368418}, BIOML-A21
RC   {ECO:0000313|EMBL:KAA5488979.1, ECO:0000313|Proteomes:UP000491168},
RC   BIOML-A25 {ECO:0000313|EMBL:KAA5474295.1,
RC   ECO:0000313|Proteomes:UP000427825}, and BIOML-A31
RC   {ECO:0000313|EMBL:KAA5463787.1, ECO:0000313|Proteomes:UP000475905};
RX   PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA   Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA   Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA   Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA   Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA   Xavier R.J., Alm E.J.;
RT   "A library of human gut bacterial isolates paired with longitudinal
RT   multiomics data enables mechanistic microbiome research.";
RL   Nat. Med. 25:1442-1452(2019).
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; CZBL01000014; CUQ42477.1; -; Genomic_DNA.
DR   EMBL; VVYP01000009; KAA5463787.1; -; Genomic_DNA.
DR   EMBL; VVYJ01000010; KAA5474295.1; -; Genomic_DNA.
DR   EMBL; VVYF01000019; KAA5488979.1; -; Genomic_DNA.
DR   EMBL; VVYD01000013; KAA5497350.1; -; Genomic_DNA.
DR   EMBL; QRUO01000018; RGR68119.1; -; Genomic_DNA.
DR   EMBL; QSCS01000058; RGY21041.1; -; Genomic_DNA.
DR   RefSeq; WP_005678627.1; NZ_VVYQ01000017.1.
DR   GeneID; 75111303; -.
DR   KEGG; bcac:CGC64_00480; -.
DR   Proteomes; UP000095725; Unassembled WGS sequence.
DR   Proteomes; UP000284205; Unassembled WGS sequence.
DR   Proteomes; UP000284431; Unassembled WGS sequence.
DR   Proteomes; UP000368418; Unassembled WGS sequence.
DR   Proteomes; UP000427825; Unassembled WGS sequence.
DR   Proteomes; UP000475905; Unassembled WGS sequence.
DR   Proteomes; UP000491168; Unassembled WGS sequence.
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   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|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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT   ACT_SITE        96
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124,
FT                   ECO:0000256|PIRSR:PIRSR035805-1"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         95..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
SQ   SEQUENCE   199 AA;  22257 MW;  E788881EA29FFAE8 CRC64;
     MVLFSEDHIQ ETKRRGRIEV ICGSMFSGKT EELIRRMKRA KFARQRVEIF KPAIDTRYSE
     EDVVSHDSHS IASTPIDSSA SILLFTSEID VVGIDEAQFF DSGLIDICNQ LANNGVRVII
     AGLDMDFKGN PFGPMPQLCA IADEVSKVHA ICVKCGQLAS FSHRTVKNDK QVLLGETAEY
     EPLCRECYLR ALEEDGQKI
//

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