ID   DRTS_MAIZE              Reviewed;         521 AA.
AC   O81395;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Bifunctional dihydrofolate reductase-thymidylate synthase;
DE            Short=DHFR-TS;
DE   Includes:
DE     RecName: Full=Dihydrofolate reductase;
DE              EC=1.5.1.3;
DE   Includes:
DE     RecName: Full=Thymidylate synthase;
DE              EC=2.1.1.45;
GN   Name=DRTS;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACCAD clade; Panicoideae; Andropogoneae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20199399; PubMed=10737138; DOI=10.1023/A:1006324328355;
RA   Cox K.M., Robertson D., Fites R.C.;
RT   "Mapping and expression of a bifunctional thymidylate synthase,
RT   dihydrofolate reductase gene from maize.";
RL   Plant Mol. Biol. 41:733-739(1999).
CC   -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
CC       dihydrofolate + NADPH.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP =
CC       dihydrofolate + dTMP.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC       tetrahydrofolate from dihydrofolate: step 1/1.
CC   -!- MISCELLANEOUS: The reaction catalyzed by this enzyme represents an
CC       essential step for de novo glycine and purine synthesis, DNA
CC       precursor synthesis, and for the conversion of dUMP to dTMP.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       dihydrofolate reductase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the thymidylate
CC       synthase family.
CC   -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF073488; AAC26003.1; -; mRNA.
DR   PIR; T01684; T01684.
DR   RefSeq; NP_001104916.1; -.
DR   UniGene; Zm.482; -.
DR   HSSP; P13100; 1CI7.
DR   GeneID; 541707; -.
DR   Gramene; O81395; -.
DR   BRENDA; 1.5.1.3; 289.
DR   BRENDA; 2.1.1.45; 289.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:EC.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:EC.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012262; DHFR-TS.
DR   InterPro; IPR001796; DHFR_reg.
DR   InterPro; IPR017925; Dihydrofolate_reductase_CS.
DR   InterPro; IPR000398; Thymidylat_synth_C.
DR   Gene3D; G3DSA:3.30.572.10; Thymidylat_synth_C; 1.
DR   PANTHER; PTHR11549:SF2; Thymidylat_synth_C; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PIRSF; PIRSF000389; DHFR-TS; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   ProDom; PD001180; Thymidylat_synth; 1.
DR   TIGRFAMs; TIGR03284; thym_sym; 1.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Multifunctional enzyme; NADP;
KW   Nucleotide biosynthesis; One-carbon metabolism; Oxidoreductase;
KW   Transferase.
FT   CHAIN         1    521       Bifunctional dihydrofolate reductase-
FT                                thymidylate synthase.
FT                                /FTId=PRO_0000186358.
FT   DOMAIN       17    194       DHFR.
FT   REGION      197    521       Thymidylate synthase.
FT   ACT_SITE    403    403       By similarity.
SQ   SEQUENCE   521 AA;  58966 MW;  81266F8652625F06 CRC64;
     MAAVLANGDS QGRPQRNYQV VVAGTRDMGI GKDGVLPWKL PGDLKFFKEL TLTTSDPVKK
     NAVIMGRKTW ESIPVKSRPL PGRLNVILTR SGSFDFATVE NVVICGSMES ALELLASTPY
     CLSIEKVFVI GGGQVLREYL KGPACEAIHL TDIQSSIECD TFIPPVDFSV FQPWYSSFPV
     IESNIRHSFV SFVRVRKSVA ETHESNGKES TEVDTKNDKF ETENFSFLPK MVYDRHEEYQ
     YLNLVEDIIR SGAQKNDRTG TGTLSKFGCQ MRFNLRKNFP LLTTKRVFWR GVVEELLWFI
     SGSTNAKVLQ EKGIHIWDGN ASREYLNSVG LAHREEGDLG PIYGFQWRHF GAEYTDMHAD
     YTGKGFDQLM DVIDKIKNDP EDRRIILSAW NPSDLKKMAL PPCHMFAQFY VENGELSCQM
     YQRSADMGLG VPFNIASYSL LTYMIAQVCD LSPGDFVHVI GDAHVYRNHV RALEEQIQKM
     PKPFPILKIN PSKKDIDSFM ASDFKLVGYD PHQKIEMKMA V
//