ID W6PSH6_PENRF Unreviewed; 336 AA.
AC W6PSH6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=thymidylate synthase {ECO:0000256|ARBA:ARBA00011947};
DE EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947};
GN Name=CDC21 {ECO:0000313|EMBL:CDM26795.1};
GN ORFNames=PROQFM164_S01g000604 {ECO:0000313|EMBL:CDM26795.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM26795.1};
RN [1] {ECO:0000313|EMBL:CDM26795.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM26795.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-
CC dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422;
CC EC=2.1.1.45; Evidence={ECO:0000256|ARBA:ARBA00001707};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004992}.
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DR EMBL; HG792015; CDM26795.1; -; Genomic_DNA.
DR AlphaFoldDB; W6PSH6; -.
DR STRING; 1365484.W6PSH6; -.
DR OMA; IVYELLW; -.
DR OrthoDB; 1118873at2759; -.
DR UniPathway; UPA00575; -.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR Gene3D; 3.30.572.10; Thymidylate synthase/dCMP hydroxymethylase domain; 1.
DR HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR InterPro; IPR000398; Thymidylate_synthase.
DR InterPro; IPR020940; Thymidylate_synthase_AS.
DR NCBIfam; TIGR03284; thym_sym; 1.
DR PANTHER; PTHR11548:SF2; THYMIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 1.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..336
FT /note="Thymidylate synthase/dCMP hydroxymethylase"
FT /evidence="ECO:0000259|Pfam:PF00303"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
SQ SEQUENCE 336 AA; 37426 MW; 46F18A349D66C408 CRC64;
MTQDQVAAVP AASSPPSDPP HEEHQYLNLI RAILSEGEHR PDRTGTGTQS IFAPPQLRFS
LSKPNPEGGE PIPILPLLTT KRVFLRAVLA ELLWFISGCT SSLPLSEAGI KIWDGNGSRE
FLDKSGLGHR EEGDLGPVYG FQWRHFGAEY VDAKTDYTSQ GIDQLKDVVH KLIHNPFDRR
IIMSAWNPAD LKKMALPPCH MFAQFYVSFP PGMKLDEKTG RPSKNGTLSC LLYQRSCDMG
LGVPFNIASY ALLTHILAHA ADLHPGTLIH TMGDAHVYLD HVDALNEQLA REPTEFPELR
IKRDDRGSAV VDGWKEDEFE VIGYKPHKAI KMKMSV
//
