Reviewed, UniProtKB/Swiss-Prot Q2QRX6 (DRTS_ORYSJ)

Names and origin

Protein names

Recommended name:
    Putative 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

Gene names

Ordered Locus Names:

Os12g0446900, LOC_Os12g26060

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP By similarity.
Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
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	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 metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dihydrofolate reductase activity Inferred from electronic annotation. Source: EC thymidylate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 494	494	Putative bifunctional dihydrofolate reductase-thymidylate synthase		PRO_0000247485
Regions
	Domain	1 – 167	167	DHFR
	Nucleotide binding	2 – 8	7	NADP By similarity
	Nucleotide binding	40 – 42	3	NADP By similarity
	Nucleotide binding	61 – 64	4	NADP By similarity
	Nucleotide binding	104 – 111	8	NADP By similarity
	Nucleotide binding	395 – 399	5	dUMP By similarity
	Nucleotide binding	437 – 439	3	dUMP By similarity
	Region	170 – 494	325	Thymidylate synthase
Sites
	Active site	376	1	By similarity
	Binding site	16	1	Substrate By similarity
	Binding site	103	1	Substrate; via carbonyl oxygen By similarity
	Binding site	124	1	Substrate By similarity
	Binding site	231	1	dUMP By similarity
	Binding site	377	1	dUMP By similarity
	Binding site	407	1	dUMP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2QRX6-1 [UniParc]. Last modified July 11, 2006. Version 2. Checksum: 1F7F2D5162109A1B	FASTA	494	55,977
	10 20 30 40 50 60 MGIGKDGTLP WKLPGDLKFF KDITVTTSDP SKKNAVVMGR KTWESIPLKF RPLPGRLNVI 70 80 90 100 110 120 LTRSGSFDFA TAENVVICGS LDSALQLLAT TPYCLTVEKT FIIGGGEILR QSLNAPACEA 130 140 150 160 170 180 IHLTDIESSI ECDTFIPPID LSMFHPWYSS FPVVENGIKH SFISFVRVTK SIAEANDSSG 190 200 210 220 230 240 KELTGNDSKK VKFEIENFSF LPKMIFERHE EYQYLNLVQD IIRNGAKKND RTGTGTVSKF 250 260 270 280 290 300 GCQMRFNLRR NFPLLTTKRV FWRGVLEELL WFISGSTNAK VLQEKGIHIW DGNASRQYLD 310 320 330 340 350 360 SIGLTQREEG DLGPVYGFQW RHFGAEYTDM HADYVGKGFD QLMDVIDKIK NNPDDRRIIL 370 380 390 400 410 420 SAWNPTDLKK MALPPCHMFA QFYVENGELS CQMYQRSADM GLGVPFNIAS YSLLTCMIAQ 430 440 450 460 470 480 VCDLSPGDFV HVIGDAHVYR THVEALEEQM RKQPKPFPIL KINPVKKDID SFVTSDFKLV 490 RYDPHHKIEM KMAV

References

[1]	"The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications." The rice chromosomes 11 and 12 sequencing consortia BMC Biol. 3:20-20(2005) [PubMed: 16188032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DP000011 Genomic DNA. Translation: ABA98037.2.
3D structure databases
SMR	Q2QRX6. Positions 1-488, 209-494.
ModBase	Search...
Family and domain databases
InterPro	IPR012262. DHFR-TS. IPR017925. Dihydrofolate_reductase_CS. IPR001796. Dihydrofolate_reductase_dom. IPR000398. Thymidylate_synthase. IPR020940. Thymidylate_synthase_AS. [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	PR00108. THYMDSNTHASE.
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_ORYSJ

Accession

Primary (citable) accession number: Q2QRX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 11, 2006
Last modified:	February 9, 2010
This is version 31 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)