ID E3PTR3_ACESD Unreviewed; 231 AA.
AC E3PTR3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Putative thymidylate kinase {ECO:0000313|EMBL:CBH22267.1};
DE EC=2.7.4.9 {ECO:0000313|EMBL:CBH22267.1};
GN OrderedLocusNames=CLOST_2147 {ECO:0000313|EMBL:CBH22267.1};
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH22267.1, ECO:0000313|Proteomes:UP000007041};
RN [1] {ECO:0000313|Proteomes:UP000007041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000313|Proteomes:UP000007041};
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
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};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|ARBA:ARBA00009776}.
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DR EMBL; FP565809; CBH22267.1; -; Genomic_DNA.
DR AlphaFoldDB; E3PTR3; -.
DR STRING; 1511.CLOST_2147; -.
DR KEGG; cst:CLOST_2147; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_1_0_9; -.
DR BioCyc; CSTI499177:GJE9-2212-MONOMER; -.
DR Proteomes; UP000007041; Chromosome.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR PANTHER; PTHR10344:SF4; THYMIDYLATE KINASE; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:CBH22267.1};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007041};
KW Transferase {ECO:0000313|EMBL:CBH22267.1}.
FT DOMAIN 10..201
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
SQ SEQUENCE 231 AA; 27031 MW; FDA1BE5E3DE78D07 CRC64;
MGRLFVVESG SDASGKATQT ELLYNKLKMD GYNVRKIEFP NYKSESSALV KMYLRGDFGS
KPEDVNPYIT STFYAVDRYA SFKTSWEEFY NNGGIIIADR YTTSNMVHQA AKYDDYNDKD
KFLQWLDEYE FDFYGLPRPT KVFFLNMPVE FSFKLMKNRK NKITGNVKKD IHEANKDYLE
KSYENALYVA KKYGWENIDC TSDDKLRQIK DIHEEIYSLI LKSLKSSEDG D
//
