ID   DRTS_ORYSJ              Reviewed;         494 AA.
AC   Q2QRX6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Putative 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   OrderedLocusNames=Os12g0446900, LOC_Os12g26060;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease
RT   resistance genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
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; DP000011; ABA98037.2; -; Genomic_DNA.
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   3: Inferred from homology;
KW   Methyltransferase; Multifunctional enzyme; NADP;
KW   Nucleotide biosynthesis; One-carbon metabolism; Oxidoreductase;
KW   Transferase.
FT   CHAIN         1    494       Putative bifunctional dihydrofolate
FT                                reductase-thymidylate synthase.
FT                                /FTId=PRO_0000247485.
FT   DOMAIN        1    167       DHFR.
FT   REGION      170    494       Thymidylate synthase.
FT   ACT_SITE    376    376       By similarity.
SQ   SEQUENCE   494 AA;  55977 MW;  1F7F2D5162109A1B CRC64;
     MGIGKDGTLP WKLPGDLKFF KDITVTTSDP SKKNAVVMGR KTWESIPLKF RPLPGRLNVI
     LTRSGSFDFA TAENVVICGS LDSALQLLAT TPYCLTVEKT FIIGGGEILR QSLNAPACEA
     IHLTDIESSI ECDTFIPPID LSMFHPWYSS FPVVENGIKH SFISFVRVTK SIAEANDSSG
     KELTGNDSKK VKFEIENFSF LPKMIFERHE EYQYLNLVQD IIRNGAKKND RTGTGTVSKF
     GCQMRFNLRR NFPLLTTKRV FWRGVLEELL WFISGSTNAK VLQEKGIHIW DGNASRQYLD
     SIGLTQREEG DLGPVYGFQW RHFGAEYTDM HADYVGKGFD QLMDVIDKIK NNPDDRRIIL
     SAWNPTDLKK MALPPCHMFA QFYVENGELS CQMYQRSADM GLGVPFNIAS YSLLTCMIAQ
     VCDLSPGDFV HVIGDAHVYR THVEALEEQM RKQPKPFPIL KINPVKKDID SFVTSDFKLV
     RYDPHHKIEM KMAV
//