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UniProtKB/Swiss-Prot entry Q01782


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PTR1_LEIMA
Primary accession number Q01782
Secondary accession numbers Q4QBE7 Q9U1F8
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on May 27, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 63)
Name and origin of the protein
Protein name Pteridine reductase 1
Synonyms EC 1.5.1.33
H region methotrexate resistance protein
Gene name
Name: PTR1
Synonyms: HMTXR
ORFNames: LmjF23.0270, L1063.01
From
Leishmania major [TaxID: 5664] 
Taxonomy Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MHOM/IR/83/Lt252 / CC-1;
PubMed=1339441 [NCBI, ExPASy, EBI, Israel, Japan]
Callahan H.L., Beverley S.M.;
"A member of the aldoketo reductase family confers methotrexate resistance in Leishmania.";
J. Biol. Chem. 267:24165-24168(1992).
[2]
SEQUENCE REVISION TO 162-171.
Callahan H.L., Beverley S.M.;
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MHOM/IL/81/Friedlin;
DOI=10.1126/science.1112680; PubMed=16020728 [NCBI, ExPASy, EBI, Israel, Japan]
Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B.G., Myler P.J.;
"The genome of the kinetoplastid parasite, Leishmania major.";
Science 309:436-442(2005).
[4]
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).
[5]
SUBUNIT.
STRAIN=MHOM/IR/83/Lt252;
DOI=10.1074/jbc.272.21.13883; PubMed=9153248 [NCBI, ExPASy, EBI, Israel, Japan]
Nare B., Hardy L.W., Beverley S.M.;
"The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major.";
J. Biol. Chem. 272:13883-13891(1997).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE.
DOI=10.1038/88584; PubMed=11373620 [NCBI, ExPASy, EBI, Israel, Japan]
Gourley D.G., Schuettelkopf A.W., Leonard G.A., Luba J., Hardy L.W., Beverley S.M., Hunter W.N.;
"Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites.";
Nat. Struct. Biol. 8:521-525(2001).
[7]
PATHWAY.
DOI=10.1021/bi972693a; PubMed=9521731 [NCBI, ExPASy, EBI, Israel, Japan]
Luba J., Nare B., Liang P.-H., Anderson K.S., Beverley S.M., Hardy L.W.;
"Leishmania major pteridine reductase 1 belongs to the short chain dehydrogenase family: stereochemical and kinetic evidence.";
Biochemistry 37:4093-4104(1998).
Comments
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
L01699; AAA29249.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CT005262; CAJ03998.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45168; A45168.
3D structure databases
PDB
1E7W; X-ray; 1.75 A; A/B=1-288.[ExPASy / RCSB / EBI]
1E92; X-ray; 2.20 A; A/B/C/D=1-288.[ExPASy / RCSB / EBI]
1W0C; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-288.[ExPASy / RCSB / EBI]
2BF7; X-ray; 2.40 A; A/B/C/D=1-288.[ExPASy / RCSB / EBI]
2BFA; X-ray; 2.70 A; A/B/C/D=1-288.[ExPASy / RCSB / EBI]
2BFM; X-ray; 2.60 A; A/B/C/D=1-288.[ExPASy / RCSB / EBI]
2BFO; X-ray; 2.60 A; A/B/C/D=1-288.[ExPASy / RCSB / EBI]
2BFP; X-ray; 2.55 A; A/B/C/D=1-288.[ExPASy / RCSB / EBI]
2P8K; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-288.[ExPASy / RCSB / EBI]
2QHX; X-ray; 2.61 A; A/B/C/D=1-288.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E7W; -.
1E92; -.
1W0C; -.
2BF7; -.
2BFA; -.
2BFM; -.
2BFO; -.
2BFP; -.
2P8K; -.
2QHX; -.
ModBase Q01782.
Ontologies
GO
GO:0047040; Molecular function: pteridine reductase activity (inferred from electronic annotation from EC).
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.
BLOCKS Q01782.
Genome annotation databases
KEGG lma:LmjF23.0270; -.
Phylogenomic databases
HOGENOM Q01782; -.
Other
ProtoNet Q01782.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Methotrexate resistance; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   288  288     Pteridine reductase 1. PRO_0000054753
NP_BIND   17    40  24     NADP (By similarity). 
ACT_SITE   194   194        Proton acceptor. 
BINDING   175   175        Substrate. 
CONFLICT   162   162        F -> V (in Ref. 3; CAJ03998). 
STRAND   8    11  4      
HELIX   17    28  12      
STRAND   32    39  8      
HELIX   41    54  14      
STRAND   59    63  5      
STRAND   67    69  3      
HELIX   85   100  16      
STRAND   105   108  4      
HELIX   134   147  14      
HELIX   149   163  15      
HELIX   167   169  3      
STRAND   174   179  6      
TURN   182   185  4      
HELIX   192   212  21      
HELIX   213   215  3      
STRAND   217   227  11      
HELIX   230   232  3      
HELIX   235   242  8      
TURN   246   249  4      
HELIX   254   265  12      
HELIX   267   269  3      
STRAND   276   280  5      
HELIX   283   285  3      
Sequence information
Length: 288 AA [This is the length of the unprocessed precursor] Molecular weight: 30457 Da [This is the MW of the unprocessed precursor] CRC64: B8F6FC23018367E0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTAPTVPVAL VTGAAKRLGR SIAEGLHAEG YAVCLHYHRS AAEANALSAT LNARRPNSAI 

        70         80         90        100        110        120 
TVQADLSNVA TAPVSGADGS APVTLFTRCA ELVAACYTHW GRCDVLVNNA SSFYPTPLLR 

       130        140        150        160        170        180 
NDEDGHEPCV GDREAMETAT ADLFGSNAIA PYFLIKAFAH RFAGTPAKHR GTNYSIINMV 

       190        200        210        220        230        240 
DAMTNQPLLG YTIYTMAKGA LEGLTRSAAL ELAPLQIRVN GVGPGLSVLV DDMPPAVWEG 

       250        260        270        280 
HRSKVPLYQR DSSAAEVSDV VIFLCSSKAK YITGTCVKVD GGYSLTRA 

Q01782 in FASTA format

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