Reviewed, UniProtKB/Swiss-Prot P51820 (DRTS_SOYBN)

Names and origin

Protein names	Recommended name:     Bifunctional dihydrofolate reductase-thymidylate synthase       Short name=DHFR-TS Including the following 2 domains:     1- Recommended name:             Dihydrofolate reductase               EC=1.5.1.3     2- Recommended name:             Thymidylate synthase               EC=2.1.1.45
Organism	Glycine max (Soybean)
Taxonomic identifier	3847 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH. 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1.
Miscellaneous	The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
Sequence similarities	In the N-terminal section; belongs to the dihydrofolate reductase family. In the C-terminal section; belongs to the thymidylate synthase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis One-carbon metabolism
Ligand	NADP
Molecular function	Methyltransferase Oxidoreductase Transferase
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	dTMP biosynthetic process Inferred from electronic annotation. Source: InterPro glycine biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon compound metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dihydrofolate reductase activity Inferred from electronic annotation. Source: InterPro thymidylate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 530	530	Bifunctional dihydrofolate reductase-thymidylate synthase		PRO_0000186359
Regions
	Domain	26 – 203	178	DHFR
	Region	206 – 530	325	Thymidylate synthase
Sites
	Active site	412	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51820-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: AFD710709FD5D820	FASTA	530	59,745
	10 20 30 40 50 60 MPSDSSVISN GHSNGSVNPL PNLQRTYQVV VAATQDWGIG KDGKLPWRLP TDLKFFKEIT 70 80 90 100 110 120 MKTSEPGKKN AIVMGRKTWE SIPLEYRPLS GRLNVVLTRS GSFDIATAEN VVICGSMSSA 130 140 150 160 170 180 LELLAASPYS LSIEKVFVIG GGQIFREALN VPGCEAIHLT EIQSSIECDT FMPPVDFTIF 190 200 210 220 230 240 RPWYSSFPKV ENNIRYSFTT YVRVRSSAAE SAGQNIDPLL DNNSESMKFE VKDFSFLPKM 250 260 270 280 290 300 ISERHEEYLY LKLVQDIIAE GTTKGDRTGT GTLSKFGCQM RFNLRGNFPL LTTKKVFWRG 310 320 330 340 350 360 VVEELLWFIS GSTNAKVLQE KGIHIWDGNA SREYLDGVGL TEREEGDLGP VYGFQWRHFG 370 380 390 400 410 420 ARYTDMHHDY SGQGFDQLLD VINKIKRNPD DRRIILSAWN PVDLKLMALP PCHMFAQFYV 430 440 450 460 470 480 AHGELSCQMY QRSADMGLGI PFNIASYALL TCMIAHVCDL IPGDFIHVIG DAHIYRNHVR 490 500 510 520 530 PLQEQLHNQP KPFPTLKINP KKKDIDSFVA ADFKLIGYDP HQKIDMKLSV

References

[1]	"Cloning, nucleotide sequence and expression of the bifunctional dihydrofolate reductase-thymidylate synthase from Glycine max." Wang M., Ratnam S., Freisheim J.H. Biochim. Biophys. Acta 1261:325-336(1995) [PubMed: 7742362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S78087 mRNA. Translation: AAB34317.1.
PIR	S55683.
UniGene	Gma.483
3D structure databases
HSSP	HSSP built from PDB template 1HW4 based on UniProtKB P04818.
ModBase	Search...
Family and domain databases
InterPro	IPR012262. DHFR-TS. IPR001796. DHFR_reg. IPR000398. Thymidylat_synth_C. [Graphical view]
Gene3D	G3DSA:3.30.572.10. Thymidylat_synth_C. 1 hit.
PANTHER	PTHR11549:SF2. Thymidylat_synth_C. 1 hit.
Pfam	PF00186. DHFR_1. 1 hit. PF00303. Thymidylat_synt. 1 hit. [Graphical view]
PIRSF	PIRSF000389. DHFR-TS. 1 hit.
PRINTS	PR00070. DHFR. PR00108. THYMDSNTHASE.
ProDom	PD001180. Thymidylat_synth. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03284. thym_sym. 1 hit.
PROSITE	PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. PS00091. THYMIDYLATE_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DRTS_SOYBN

Accession

Primary (citable) accession number: P51820

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)