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Database: UniProt
Entry: A0A117MF53_9EURY
LinkDB: A0A117MF53_9EURY
Original site: A0A117MF53_9EURY 
ID   A0A117MF53_9EURY        Unreviewed;       380 AA.
AC   A0A117MF53;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Probable thymidylate kinase {ECO:0000256|ARBA:ARBA00013355, ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980, ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00029962, ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN   ORFNames=XE10_1327 {ECO:0000313|EMBL:KUL00645.1};
OS   Methanoculleus marisnigri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=2198 {ECO:0000313|EMBL:KUL00645.1, ECO:0000313|Proteomes:UP000054598};
RN   [1] {ECO:0000313|Proteomes:UP000054598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|RuleBase:RU003657}.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
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:KUL00645.1}.
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DR   EMBL; LGHE01000154; KUL00645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117MF53; -.
DR   PATRIC; fig|2198.3.peg.1247; -.
DR   Proteomes; UP000054598; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01672; TMPK; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   NCBIfam; TIGR00041; DTMP_kinase; 1.
DR   PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR   PANTHER; PTHR10344:SF4; UMP-CMP KINASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003657};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Histidine biosynthesis {ECO:0000256|RuleBase:RU003657};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:KUL00645.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   DOMAIN          180..363
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         182..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   380 AA;  41876 MW;  AFECC52D12114F6A CRC64;
     MELILAVDLA DGLVVHGKSG DRASYRPLTW GIAPSAEPEA YLSSLQPRYL YIADLESLQG
     RTPQDDLVRR CAARVEKCYL DRGCRSPAEC TAVVGVTPVV GTETAARAIE DLAAYEAGYL
     SIDVQRGRVL PWGIRPAEML ARASALSFEG CIILNIGAVG TERGLVHRVD PERIPVLITI
     EGIDGSGKST LLARLRELLA DLDPLFTREP GATWVGDSVR RAVAERMDPI TEALLFCADH
     AAHIDAVIRP ALDEGELVIS DRYSDSRFAY QPVVLDGLLP DPLLWLRRIH EGWSIRPDRT
     FLLVLPVEEA VSRLDPAKKR EYFESAGILA RVQENYLSLA ASDPARFVIV DALLKKEEVA
     RFIADEIRTS DRSSQSRPRA
//
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