ID R5VJZ6_9FIRM Unreviewed; 262 AA.
AC R5VJZ6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=BN566_00171 {ECO:0000313|EMBL:CCZ83866.1};
OS Ruminococcus sp. CAG:254.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262953 {ECO:0000313|EMBL:CCZ83866.1, ECO:0000313|Proteomes:UP000018181};
RN [1] {ECO:0000313|EMBL:CCZ83866.1, ECO:0000313|Proteomes:UP000018181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:254 {ECO:0000313|Proteomes:UP000018181};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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,
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:CCZ83866.1}.
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DR EMBL; CBAR010000168; CCZ83866.1; -; Genomic_DNA.
DR AlphaFoldDB; R5VJZ6; -.
DR STRING; 1262953.BN566_00171; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000018181; 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 NADP {ECO:0000256|HAMAP-Rule:MF_01408};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01408};
KW Reference proteome {ECO:0000313|Proteomes:UP000018181};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01408}.
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 89..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 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 262 AA; 28935 MW; C7E753208D43CAB1 CRC64;
MTVTLISHTP QPEQIIAAAA KLCYSDTTVE DLMDGLSAEQ AEKFVGMLET MGHESPVEHV
TFTFGIAGVS RSLLAQITRH RIASFSVQSQ RYVRKNQFTY VTPPAIAADE AAAALYHQTM
EQTVQAYNAL ADRLQATYYP QFLAEGCTEK AARSKAEKKA IEDARYVLPN ACETKMMVTM
NVRSLRHFFQ LRCCNRAQWE IRDLATQMLK LCCEAAPALF RHAGPACCQG GCPEGKMTCG
QMAAVRERFA ALHAAPSTAE TR
//
