Reviewed, UniProtKB/Swiss-Prot P36591 (DYR_SCHPO)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:	dfr1
ORF Names:	SPCC1223.08c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-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	Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide 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
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NADP or NADPH binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activity Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	Dihydrofolate reductase		PRO_0000186377
Regions
	Domain	233 – 447	215	DHFR
	Nucleotide binding	275 – 282	8	ATP Potential
Experimental info
	Sequence conflict	126 – 127	2	QP → HA in AAA57051. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36591-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: F6A3695F537A03C9	FASTA	461	51,523
	10 20 30 40 50 60 MSKPLKVLCL HGWIQSGPVF SKKMGSVQKY LSKYAELHFP TGPVVADEEA DPNDEEEKKR 70 80 90 100 110 120 LAALGGEQNG GKFGWFEVED FKNTYGSWDE SLECINQYMQ EKGPFDGLIG FSQGAGIGAM 130 140 150 160 170 180 LAQMLQPGQP PNPYVQHPPF KFVVFVGGFR AEKPEFDHFY NPKLTTPSLH IAGTSDTLVP 190 200 210 220 230 240 LARSKQLVER CENAHVLLHP GQHIVPQQAV YKTGIRDFMF SAPTKEPTKH PRDLTMIVAV 250 260 270 280 290 300 SSPNLGIGKK NSMPWHIKQE MAYFANVTSS TESSGQLEEG KSKIMNVVIM GRSCYDSLPK 310 320 330 340 350 360 KNRPLKDRIN IVITRNSNYN FGLTKKEKMP ENLYAADCID SALDLVAEKY GADSDIQVGK 370 380 390 400 410 420 VFIIGGSFLY GSALYHPLTK NLLFTRIHKE YPCDSFFPFE PAESSDWVRK AHPELEKFVG 430 440 450 460 IPVEEGRLKA ASSNKEEVEI EFELYGKNDD VNVALEKLSI C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The isolation and characterization of the gene (dfr1) encoding dihydrofolate reductase (DHFR) in Schizosaccharomyces pombe." Bertani L.E., Campbell J.L. Gene 147:131-135(1994) [PubMed: 8088538] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L13703 mRNA. Translation: AAA57051.1. CU329672 Genomic DNA. Translation: CAA20877.1.
PIR	T43248.
RefSeq	NP_588353.1.
3D structure databases
HSSP	HSSP built from PDB template 1DYR based on UniProtKB P16184.
ModBase	Search...
Protein-protein interaction databases
STRING	P36591.
Genome annotation databases
GeneID	2539048.
GenomeReviews	Gene locus dfr1 in contig CU329672_GR.
KEGG	spo:SPCC1223.08c.
NMPDR	fig|4896.1.peg.691.
Organism-specific databases
GeneDB_Spombe	SPCC1223.08c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000273-MON.
BRENDA	1.5.1.3. 653.
Gene expression databases
ArrayExpress	P36591.
Family and domain databases
InterPro	IPR012259. DHFR. IPR001796. DHFR_reg. IPR017925. Dihydrofolate_reductase_CS. IPR005645. DUF341. [Graphical view]
Pfam	PF00186. DHFR_1. 1 hit. PF03959. FSH1. 1 hit. [Graphical view]
PRINTS	PR00070. DHFR.
PROSITE	PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DYR_SCHPO

Accession

Primary (citable) accession number: P36591
Secondary accession number(s): O74408

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	May 30, 2000
Last modified:	September 22, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)