ID L0AM00_NATGS Unreviewed; 342 AA.
AC L0AM00;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Thymidylate synthase {ECO:0000256|ARBA:ARBA00011947, ECO:0000256|HAMAP-Rule:MF_00008};
DE Short=TS {ECO:0000256|HAMAP-Rule:MF_00008};
DE Short=TSase {ECO:0000256|HAMAP-Rule:MF_00008};
DE EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947, ECO:0000256|HAMAP-Rule:MF_00008};
GN Name=thyA {ECO:0000256|HAMAP-Rule:MF_00008,
GN ECO:0000313|EMBL:PLK21769.1};
GN OrderedLocusNames=Natgr_3361 {ECO:0000313|EMBL:AFZ74484.1};
GN ORFNames=C490_03843 {ECO:0000313|EMBL:ELY72446.1}, CYV19_02760
GN {ECO:0000313|EMBL:PLK21769.1};
OS Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS 104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronobacterium.
OX NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ74484.1, ECO:0000313|Proteomes:UP000010468};
RN [1] {ECO:0000313|Proteomes:UP000010468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC {ECO:0000313|Proteomes:UP000010468};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFZ74484.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SP2 {ECO:0000313|EMBL:AFZ74484.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY72446.1, ECO:0000313|Proteomes:UP000011613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:ELY72446.1,
RC ECO:0000313|Proteomes:UP000011613};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:PLK21769.1, ECO:0000313|Proteomes:UP000234484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:PLK21769.1,
RC ECO:0000313|Proteomes:UP000234484};
RC TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK21769.1};
RA Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA Huang J.;
RT "The characterization of oligonucleotides binding to NgAgo.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-
CC monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while
CC utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and
CC reductant in the reaction, yielding dihydrofolate (DHF) as a by-
CC product. This enzymatic reaction provides an intracellular de novo
CC source of dTMP, an essential precursor for DNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-
CC dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422;
CC EC=2.1.1.45; Evidence={ECO:0000256|HAMAP-Rule:MF_00008};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_00008}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. Bacterial-type
CC ThyA subfamily. {ECO:0000256|HAMAP-Rule:MF_00008}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00008}.
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DR EMBL; CP003377; AFZ74484.1; -; Genomic_DNA.
DR EMBL; AOIC01000026; ELY72446.1; -; Genomic_DNA.
DR EMBL; PKKI01000005; PLK21769.1; -; Genomic_DNA.
DR RefSeq; WP_005576871.1; NZ_PKKI01000005.1.
DR AlphaFoldDB; L0AM00; -.
DR STRING; 797304.Natgr_3361; -.
DR GeneID; 14209308; -.
DR KEGG; nge:Natgr_3361; -.
DR PATRIC; fig|797304.7.peg.771; -.
DR eggNOG; arCOG03214; Archaea.
DR HOGENOM; CLU_021669_0_0_2; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000010468; Chromosome.
DR Proteomes; UP000011613; Unassembled WGS sequence.
DR Proteomes; UP000234484; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR Gene3D; 3.30.572.10; Thymidylate synthase/dCMP hydroxymethylase domain; 2.
DR HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR InterPro; IPR000398; Thymidylate_synthase.
DR NCBIfam; TIGR03284; thym_sym; 1.
DR PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR PANTHER; PTHR11548:SF1; THYMIDYLATE SYNTHASE-RELATED; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00008};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00008}; Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00008};
KW Reference proteome {ECO:0000313|Proteomes:UP000010468};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00008}.
FT DOMAIN 2..341
FT /note="Thymidylate synthase/dCMP hydroxymethylase"
FT /evidence="ECO:0000259|Pfam:PF00303"
FT ACT_SITE 176
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT BINDING 21
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT BINDING 156..157
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT BINDING 196..199
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT BINDING 199
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT BINDING 207
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT BINDING 237..239
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
FT BINDING 341
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00008"
SQ SEQUENCE 342 AA; 38821 MW; F51D41ED2180CA8D CRC64;
MQQYLELVDS ALSGGTYKPN RTGVDTISSF SEHYEVDIKD GYPLLTTKQM DGYRWNSMLH
EVCWYLSGEE HVRNLREETK IWDAWADEEG RLDTAYGRFW RRYPVPDEGV QLAGESWPDD
GQQWVTVEET DDGESRRVFD QLQYVVDTLS DSPNSRRLVV NAWHPANAAV STLPPCHYTF
VFNVQGDRLN CHLTQRSGDI ALGVPFNIAA YALLTKVVAQ QTGFESGTFA HTVVDAHVYC
GRGDRGEWYD DNLEALQSRL AEADDREDYL SVKEWLESEA PPEAEGDERL DHVPGLLEQL
SRDPLERPTL EVADASIDDL TYEDVSLQGY ESHEGIQFSV AE
//
