ID A0A371IN67_9FIRM Unreviewed; 261 AA.
AC A0A371IN67;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BBG48_002120 {ECO:0000313|EMBL:RDY21890.1};
OS Criibacterium bergeronii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Criibacterium.
OX NCBI_TaxID=1871336 {ECO:0000313|EMBL:RDY21890.1, ECO:0000313|Proteomes:UP000093352};
RN [1] {ECO:0000313|EMBL:RDY21890.1, ECO:0000313|Proteomes:UP000093352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-22567 {ECO:0000313|EMBL:RDY21890.1,
RC ECO:0000313|Proteomes:UP000093352};
RX PubMed=27587833;
RA Maheux A.F., Berube E., Boudreau D.K., Raymond F., Corbeil J., Roy P.H.,
RA Boissinot M., Omar R.F.;
RT "Draft Genome Sequence of Criibacterium bergeronii gen. nov., sp. nov.,
RT Strain CCRI-22567T, Isolated from a Vaginal Sample from a Woman with
RT Bacterial Vaginosis.";
RL Genome Announc. 4:e00959-16(2016).
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:RDY21890.1}.
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DR EMBL; MBEW02000003; RDY21890.1; -; Genomic_DNA.
DR RefSeq; WP_068914209.1; NZ_MBEW02000003.1.
DR AlphaFoldDB; A0A371IN67; -.
DR STRING; 1871336.BBG48_07300; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000093352; 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:RDY21890.1}; NADP {ECO:0000256|HAMAP-Rule:MF_01408};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01408};
KW Reference proteome {ECO:0000313|Proteomes:UP000093352};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01408, ECO:0000313|EMBL:RDY21890.1}.
FT ACT_SITE 192
FT /note="Involved in ionization of N3 of dUMP, leading to its
FT activation"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT BINDING 55
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 76..79
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 79..81
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 87..91
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 87
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 165
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 181..183
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 187
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 192
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 261 AA; 30252 MW; 4220D57ADC62A082 CRC64;
MKVKLIAHTP KPDYVVAMSA KLCYSKVGAD EIAENLDDEK VDKFVDNLMS IGHQSPIEHV
SFTFMIEGIS RVCTHQLVRH RIASYSQQSQ RYVKLDQFEY IVPPQIENNE EAKKIFIKAM
EDDQKAYDEI VDKLMADNIQ YYLNEGKSEK QAKQMAQKKS IEDARYVFPN ACETKIIVTM
NARTLKNFFY TRLCERAQWE IREMAYLMLE EVKKVSKNLF KNAGPSCCSE GKCKEGNMTC
GHPEIPRNRL QEINKQTNQK N
//
