ID Q2CF80_OCEGH Unreviewed; 301 AA.
AC Q2CF80;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Flavin-dependent thymidylate synthase {ECO:0000256|HAMAP-Rule:MF_01408};
DE Short=FDTS {ECO:0000256|HAMAP-Rule:MF_01408};
DE EC=2.1.1.148 {ECO:0000256|HAMAP-Rule:MF_01408};
DE AltName: Full=FAD-dependent thymidylate synthase {ECO:0000256|HAMAP-Rule:MF_01408};
DE AltName: Full=Thymidylate synthase ThyX {ECO:0000256|HAMAP-Rule:MF_01408};
DE Short=TS {ECO:0000256|HAMAP-Rule:MF_01408};
DE Short=TSase {ECO:0000256|HAMAP-Rule:MF_01408};
GN Name=thyX {ECO:0000256|HAMAP-Rule:MF_01408};
GN ORFNames=OG2516_15664 {ECO:0000313|EMBL:EAR51415.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR51415.1, ECO:0000313|Proteomes:UP000003635};
RN [1] {ECO:0000313|EMBL:EAR51415.1, ECO:0000313|Proteomes:UP000003635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000313|Proteomes:UP000003635};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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,
CC and NADPH and FADH(2) as the reductant. {ECO:0000256|HAMAP-
CC Rule:MF_01408}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) +
CC NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+);
CC Xref=Rhea:RHEA:29043, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.148;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01408};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01408};
CC Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three
CC monomers. {ECO:0000256|HAMAP-Rule:MF_01408};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_01408}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01408}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase ThyX family.
CC {ECO:0000256|HAMAP-Rule:MF_01408}.
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:EAR51415.1}.
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DR EMBL; AAOT01000013; EAR51415.1; -; Genomic_DNA.
DR RefSeq; WP_007256647.1; NZ_CH724108.1.
DR AlphaFoldDB; Q2CF80; -.
DR STRING; 314256.OG2516_15664; -.
DR eggNOG; COG1351; Bacteria.
DR HOGENOM; CLU_067790_0_0_5; -.
DR OrthoDB; 9774464at2; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000003635; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050797; F:thymidylate synthase (FAD) 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; cd20175; ThyX; 1.
DR Gene3D; 3.30.1360.170; -; 1.
DR HAMAP; MF_01408; ThyX; 1.
DR InterPro; IPR003669; Thymidylate_synthase_ThyX.
DR InterPro; IPR036098; Thymidylate_synthase_ThyX_sf.
DR NCBIfam; TIGR02170; thyX; 1.
DR PANTHER; PTHR34934; FLAVIN-DEPENDENT THYMIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR34934:SF1; FLAVIN-DEPENDENT THYMIDYLATE SYNTHASE; 1.
DR Pfam; PF02511; Thy1; 1.
DR SUPFAM; SSF69796; Thymidylate synthase-complementing protein Thy1; 1.
DR PROSITE; PS51331; THYX; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_01408};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01408};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01408,
KW ECO:0000313|EMBL:EAR51415.1}; NADP {ECO:0000256|HAMAP-Rule:MF_01408};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01408};
KW Reference proteome {ECO:0000313|Proteomes:UP000003635};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01408, ECO:0000313|EMBL:EAR51415.1}.
FT ACT_SITE 223
FT /note="Involved in ionization of N3 of dUMP, leading to its
FT activation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT BINDING 109..112
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT BINDING 112..114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT BINDING 120..124
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_01408"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT BINDING 196
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_01408"
FT BINDING 212..214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT BINDING 223
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
SQ SEQUENCE 301 AA; 34387 MW; 40020D049AEB9BF4 CRC64;
MTLTPEQQAE IDELRATPRP TLRAVSEGME GHLYKANPVL DHGFVRVIDY MGDDAAICQA
ARVSYGRGTK AVSNDEGLIR YLMRHWHSTP FEMCEVKLHV KLPVFVARQW IRHRTANVNE
YSARYSILDR EFYIPEPEKL AAQSVTNNQG RGEALGPEEG ARVLEWLKAD AARAYDHYEA
MIGQDGQQGL ARELARMNLP ANIYTQWYWK VDLHNLFHFL RLRADAHAQY EIRVYAEEIC
RLVKDWVPHA YAAFEDYRLG GATLSGKALE CLRRMLAGEA VTQETSGMSK GEWREFQAVL
G
//
