ID   DRTS_SOYBN              Reviewed;         530 AA.
AC   P51820;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 49.
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;
OS   Glycine max (Soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Glycine.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=95260857; PubMed=7742362; DOI=10.1016/0167-4781(94)00251-W;
RA   Wang M., Ratnam S., Freisheim J.H.;
RT   "Cloning, nucleotide sequence and expression of the bifunctional
RT   dihydrofolate reductase-thymidylate synthase from Glycine max.";
RL   Biochim. Biophys. Acta 1261:325-336(1995).
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.
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DR   EMBL; S78087; AAB34317.1; -; mRNA.
DR   PIR; S55683; S55683.
DR   UniGene; Gma.483; -.
DR   HSSP; P04818; 1HW4.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:InterPro.
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:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012262; DHFR-TS.
DR   InterPro; IPR001796; DHFR_reg.
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; PR00070; DHFR.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Methyltransferase; Multifunctional enzyme;
KW   NADP; Nucleotide biosynthesis; One-carbon metabolism; Oxidoreductase;
KW   Transferase.
FT   CHAIN         1    530       Bifunctional dihydrofolate reductase-
FT                                thymidylate synthase.
FT                                /FTId=PRO_0000186359.
FT   DOMAIN       26    203       DHFR.
FT   REGION      206    530       Thymidylate synthase.
FT   ACT_SITE    412    412       By similarity.
SQ   SEQUENCE   530 AA;  59745 MW;  AFD710709FD5D820 CRC64;
     MPSDSSVISN GHSNGSVNPL PNLQRTYQVV VAATQDWGIG KDGKLPWRLP TDLKFFKEIT
     MKTSEPGKKN AIVMGRKTWE SIPLEYRPLS GRLNVVLTRS GSFDIATAEN VVICGSMSSA
     LELLAASPYS LSIEKVFVIG GGQIFREALN VPGCEAIHLT EIQSSIECDT FMPPVDFTIF
     RPWYSSFPKV ENNIRYSFTT YVRVRSSAAE SAGQNIDPLL DNNSESMKFE VKDFSFLPKM
     ISERHEEYLY LKLVQDIIAE GTTKGDRTGT GTLSKFGCQM RFNLRGNFPL LTTKKVFWRG
     VVEELLWFIS GSTNAKVLQE KGIHIWDGNA SREYLDGVGL TEREEGDLGP VYGFQWRHFG
     ARYTDMHHDY SGQGFDQLLD VINKIKRNPD DRRIILSAWN PVDLKLMALP PCHMFAQFYV
     AHGELSCQMY QRSADMGLGI PFNIASYALL TCMIAHVCDL IPGDFIHVIG DAHIYRNHVR
     PLQEQLHNQP KPFPTLKINP KKKDIDSFVA ADFKLIGYDP HQKIDMKLSV
//