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Database: UniProt
Entry: A0A2V1HT90_9MICO
LinkDB: A0A2V1HT90_9MICO
Original site: A0A2V1HT90_9MICO 
ID   A0A2V1HT90_9MICO        Unreviewed;       248 AA.
AC   A0A2V1HT90;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=DDQ50_14560 {ECO:0000313|EMBL:PVZ93537.1};
OS   Amnibacterium flavum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Amnibacterium.
OX   NCBI_TaxID=2173173 {ECO:0000313|EMBL:PVZ93537.1, ECO:0000313|Proteomes:UP000244893};
RN   [1] {ECO:0000313|EMBL:PVZ93537.1, ECO:0000313|Proteomes:UP000244893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8JJ-5 {ECO:0000313|EMBL:PVZ93537.1,
RC   ECO:0000313|Proteomes:UP000244893};
RA   Tuo L.;
RT   "Amnibacterium sp. M8JJ-5, whole genome shotgun sequence.";
RL   Submitted (MAY-2018) 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: 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:PVZ93537.1}.
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DR   EMBL; QEOP01000003; PVZ93537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1HT90; -.
DR   OrthoDB; 9774464at2; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000244893; 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|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01408};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01408};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01408};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01408};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW   Rule:MF_01408}; Reference proteome {ECO:0000313|Proteomes:UP000244893};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01408}.
FT   ACT_SITE        202
FT                   /note="Involved in ionization of N3 of dUMP, leading to its
FT                   activation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01408"
FT   BINDING         72
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         92..95
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         95..97
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         103..107
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         103
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         175
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         191..193
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         197
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         202
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   248 AA;  28449 MW;  C5792A934FB1F615 CRC64;
     MGAVPSTDEI QFRSDMTVEL VRSSAHDSDV LFAARVSTQG EKTLEAAQDG TEADEKRDRG
     LINYLMRDRH GSPFEHNSMT FYVQAPIFVF REFMRHRVAS YNEESGRYRE MRPVFYVPGA
     ERKLIQVGKP GAYDFEPGTP EMTELVSEQT RQVSTAAYDS YQRMLEAGIA REVARIVLPL
     NLYSSMYVTM NARALMNFLS LRTKREGTHF PSFPQREIEM VAEQMEDQWA TLMPLTYEAF
     QKNGRVAP
//
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