[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=TarII; PubMed=1396560 [NCBI, ExPASy, EBI, Israel, Japan] Papadopoulou B., Roy G., Ouellette M.; "A novel antifolate resistance gene on the amplified H circle of Leishmania."; EMBO J. 11:3601-3608(1992).
[2]	FUNCTION. PubMed=7972081 [NCBI, ExPASy, EBI, Israel, Japan] Bello A.R., Nare B., Freedman D., Hardy L.W., Beverley S.M.; "PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major."; Proc. Natl. Acad. Sci. U.S.A. 91:11442-11446(1994).
[3]	X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) IN COMPLEX WITH NADP. DOI=10.1107/S0907444903013131; PubMed=12925782 [NCBI, ExPASy, EBI, Israel, Japan] Zhao H., Bray T., Ouellette M., Zhao M., Ferre R.A., Matthews D., Whiteley J.M., Varughese K.I.; "Structure of pteridine reductase (PTR1) from Leishmania tarentolae."; Acta Crystallogr. D 59:1539-1544(2003).

Comments

FUNCTION: Exhibits a NADPH-dependent biopterin reductase activity. Has good activity with folate and significant activity with dihydrofolate and dihydrobiopterin, but not with quinonoid dihydrobiopterin. Confers resistance to methotrexate (MTX).
CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrobiopterin + 2 NADP⁺ = biopterin + 2 NADPH.
PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from biopterin: step 1/1 .
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z11978; CAA78031.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S25286; S25286.

3D structure databases

PDB

1P33; X-ray; 2.86 A; A/B/C/D=1-289.

[ExPASy / RCSB / EBI]

PDBsum

1P33; -.

ModBase

P42556.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0047040;	Molecular function: pteridine reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0031427;	Biological process: response to methotrexate (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
IPR014058; Pteridine_reductase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

TIGRFAMs

TIGR02685; pter_reduc_Leis; 1.

PROSITE

PS00061; ADH_SHORT; 1.

ProtoNet

P42556.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Methotrexate resistance; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 289`	`289`	`Pteridine reductase 1.`	`PRO_0000054754`
`NP_BIND`	`14 41`	`28`	`NADP.`
`NP_BIND`	`195 199`	`5`	`NADP.`
`ACT_SITE`	`195 195`		`Proton acceptor (By similarity).`
`BINDING`	`176 176`		`Substrate (By similarity).`
`STRAND`	`9 12`	`4`
`TURN`	`13 16`	`4`
`HELIX`	`18 29`	`12`
`STRAND`	`33 40`	`8`
`HELIX`	`42 55`	`14`
`STRAND`	`60 64`	`5`
`STRAND`	`68 70`	`3`
`HELIX`	`86 101`	`16`
`STRAND`	`106 109`	`4`
`HELIX`	`136 148`	`13`
`HELIX`	`150 164`	`15`
`HELIX`	`168 170`	`3`
`STRAND`	`176 180`	`5`
`STRAND`	`185 187`	`3`
`HELIX`	`193 213`	`21`
`TURN`	`214 217`	`4`
`STRAND`	`219 229`	`11`
`HELIX`	`236 243`	`8`
`TURN`	`247 250`	`4`
`HELIX`	`255 266`	`12`
`HELIX`	`268 270`	`3`
`STRAND`	`277 281`	`5`
`HELIX`	`284 286`	`3`

Sequence information

Length: 289 AA [This is the length of the unprocessed precursor]

Molecular weight: 30744 Da [This is the MW of the unprocessed precursor]

CRC64: 1149EE08968D0310 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTSPTAPVA LVTGAAKRLG SSIAEALHAE GYTVCLHYHR SAADASTLAA TLNARRPNSA 

        70         80         90        100        110        120 
ITVQADLSNV ATASFSETDG SVPVTLFSRC SALVDACYMH WGRCDVLVNN ASSFYPTPLL 

       130        140        150        160        170        180 
RKDAGEGGSS VGDKESLEVA AADLFGSNAI APYFLIKAFA QRVADTRAEQ RGTSYSIVNM 

       190        200        210        220        230        240 
VDAMTSQPLL GYTMYTMAKE ALEGLTRSAA LELASLQIRV NGVSPGLSVL PDDMPFSVQE 

       250        260        270        280 
DYRRKVPLYQ RNSSAEEVSD VVIFLCSPKA KYITGTCIKV DGGYSLTRA

P42556 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools