THYX_CORGL
ID THYX_CORGL Reviewed; 250 AA.
AC P40111;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Flavin-dependent thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01408};
DE Short=FDTS {ECO:0000255|HAMAP-Rule:MF_01408};
DE EC=2.1.1.148 {ECO:0000255|HAMAP-Rule:MF_01408};
DE AltName: Full=FAD-dependent thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01408};
DE AltName: Full=Thymidylate synthase ThyX {ECO:0000255|HAMAP-Rule:MF_01408};
DE Short=TS {ECO:0000255|HAMAP-Rule:MF_01408};
DE Short=TSase {ECO:0000255|HAMAP-Rule:MF_01408};
GN Name=thyX {ECO:0000255|HAMAP-Rule:MF_01408};
GN OrderedLocusNames=Cgl1972, cg2162;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=8478336; DOI=10.1128/jb.175.9.2743-2749.1993;
RA Pisabarro A., Malumbres M., Mateos L.M., Oguiza J.A., Martin J.F.;
RT "A cluster of three genes (dapA, orf2, and dapB) of Brevibacterium
RT lactofermentum encodes dihydrodipicolinate synthase, dihydrodipicolinate
RT reductase, and a third polypeptide of unknown function.";
RL J. Bacteriol. 175:2743-2749(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_01408};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01408};
CC Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three
CC monomers. {ECO:0000255|HAMAP-Rule:MF_01408};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01408}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01408}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase ThyX family.
CC {ECO:0000255|HAMAP-Rule:MF_01408}.
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DR EMBL; Z21502; CAA79713.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99365.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20313.1; -; Genomic_DNA.
DR PIR; B40626; B40626.
DR RefSeq; NP_601178.1; NC_003450.3.
DR RefSeq; WP_011014793.1; NC_006958.1.
DR PDB; 3FNN; X-ray; 2.30 A; A=1-250.
DR PDB; 3GE9; X-ray; 2.61 A; A=1-250.
DR PDBsum; 3FNN; -.
DR PDBsum; 3GE9; -.
DR AlphaFoldDB; P40111; -.
DR SMR; P40111; -.
DR STRING; 196627.cg2162; -.
DR KEGG; cgb:cg2162; -.
DR KEGG; cgl:Cgl1972; -.
DR PATRIC; fig|196627.13.peg.1909; -.
DR eggNOG; COG1351; Bacteria.
DR HOGENOM; CLU_077585_1_0_11; -.
DR OMA; AKLGPRC; -.
DR UniPathway; UPA00575; -.
DR EvolutionaryTrace; P40111; -.
DR Proteomes; UP000000582; Chromosome.
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 Gene3D; 3.30.70.3180; -; 1.
DR HAMAP; MF_01408; ThyX; 1.
DR InterPro; IPR003669; Thymidylate_synthase_ThyX.
DR InterPro; IPR036098; Thymidylate_synthase_ThyX_sf.
DR PANTHER; PTHR34934; PTHR34934; 1.
DR Pfam; PF02511; Thy1; 1.
DR SUPFAM; SSF69796; SSF69796; 1.
DR TIGRFAMs; TIGR02170; thyX; 1.
DR PROSITE; PS51331; THYX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Methyltransferase; NADP;
KW Nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..250
FT /note="Flavin-dependent thymidylate synthase"
FT /id="PRO_0000175560"
FT DOMAIN 7..233
FT /note="ThyX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT MOTIF 95..105
FT /note="ThyX motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT ACT_SITE 199
FT /note="Involved in ionization of N3 of dUMP, leading to its
FT activation"
FT /evidence="ECO:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01408"
FT BINDING 172
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:0000255|HAMAP-Rule:MF_01408"
FT BINDING 188..190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between neighboring subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT BINDING 199
FT /ligand="dUMP"
FT /ligand_id="ChEBI:CHEBI:246422"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT CONFLICT 214
FT /note="E -> G (in Ref. 1; CAA79713)"
FT /evidence="ECO:0000305"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:3FNN"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:3FNN"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 126..152
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3FNN"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 206..222
FT /evidence="ECO:0007829|PDB:3FNN"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:3FNN"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3FNN"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:3FNN"
SQ SEQUENCE 250 AA; 28065 MW; E6C8FF5276BE6314 CRC64;
MAEQVKLSVE LIACSSFTPP ADVEWSTDVE GAEALVEFAG RACYETFDKP NPRTASNAAY
LRHIMEVGHT ALLEHANATM YIRGISRSAT HELVRHRHFS FSQLSQRFVH SGESEVVVPT
LIDEDPQLRE LFMHAMDESR FAFNELLNAL EEKLGDEPNA LLRKKQARQA ARAVLPNATE
SRIVVSGNFR TWRHFIGMRA SEHADVEIRE VAVECLRKLQ VAAPTVFGDF EIETLADGSQ
MATSPYVMDF
