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Protein
Submitted name:

Trypanothione reductase

Gene

TRYR

Organism
Leishmania infantum
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101FADCombined sources
Binding sitei51 – 511FAD
Binding sitei56 – 561FAD
Binding sitei60 – 601FAD
Binding sitei127 – 1271FAD; via amide nitrogen and carbonyl oxygen
Binding sitei159 – 1591FAD; via carbonyl oxygenCombined sources
Binding sitei228 – 2281NADPCombined sources
Binding sitei327 – 3271FAD
Binding sitei333 – 3331NADP; via carbonyl oxygenCombined sources
Binding sitei365 – 3651NADP; via carbonyl oxygenCombined sources
Binding sitei461 – 4611FAD; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 152FAD
Nucleotide bindingi34 – 352FAD
Nucleotide bindingi46 – 472FAD
Nucleotide bindingi196 – 2027NADPCombined sources
Nucleotide bindingi221 – 2222NADPCombined sources
Nucleotide bindingi284 – 2863NADPCombined sources
Nucleotide bindingi333 – 3353FAD

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Ligandi

FADUniRule annotation, Flavoprotein, NADPCombined sources, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.8.1.12. 2949.

Names & Taxonomyi

Protein namesi
Submitted name:
Trypanothione reductaseImported (EC:1.8.1.12Imported)
Gene namesi
Name:TRYRImported
ORF Names:LINJ_05_0350Imported
OrganismiLeishmania infantumImported
Taxonomic identifieri5671 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
ProteomesiUP000008153 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 57
Disulfide bondi89 ↔ 213Combined sources

Interactioni

Protein-protein interaction databases

STRINGi435258.XP_001462998.1.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JK6X-ray2.95A/B1-491[»]
2W0HX-ray3.00A/B1-491[»]
2X50X-ray3.30A/B1-490[»]
2YAUX-ray3.50A/B1-491[»]
4ADWX-ray3.61A/B1-491[»]
4APNX-ray3.20A/B1-491[»]
ProteinModelPortaliA4HSF7.
SMRiA4HSF7. Positions 2-486.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA4HSF7.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.UniRule annotation

Keywords - Domaini

Redox-active centerUniRule annotation

Phylogenomic databases

eggNOGiCOG1249.
InParanoidiA4HSF7.
KOiK04283.
OMAiVIGASMC.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR001864. Trypnth_redctse.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00470. TRYPANRDTASE.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01423. trypano_reduc. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4HSF7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRAYDLVVL GAGSGGLEAG WNAAVTHKKK VAVVDVQATH GPPLFAALGG
60 70 80 90 100
TCVNVGCVPK KLMVTGAQYM DLIRESGGFG WEMDRESLCP NWKTLIAAKN
110 120 130 140 150
KVVNSINESY KSMFADTEGL SFHMGFGALQ DAHTVVVRKS EDPHSDVLET
160 170 180 190 200
LDTEYILIAT GSWPTRLGVP GDEFCITSNE AFYLEDAPKR MLCVGGGYIA
210 220 230 240 250
VEFAGIFNGY KPCGGYVDLC YRGDLILRGF DTEVRKSLTK QLGANGIRVR
260 270 280 290 300
TNLNPTKITK NEDGSNHVHF NDGTEEDYDQ VMLAIGRVPR SQALQLDKAG
310 320 330 340 350
VRTGKNGAVQ VDAYSKTSVD NIYAIGDVTN RVMLTPVAIN EGAAFVETVF
360 370 380 390 400
GGKPRATDHT KVACAVFSIP PIGTCGMTEE EAAKNYETVA VYASSFTPLM
410 420 430 440 450
HNISGSKHKE FMIRIITNES NGEVLGVHML GDSAPEIIQS VGICMKMGAK
460 470 480 490
ISDFHSTIGV HPTSAEELCS MRTPAYFYES GKRVEKLSSN L
Length:491
Mass (Da):53,026
Last modified:May 1, 2007 - v1
Checksum:i1E41FDC657DDCF67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796437 Genomic DNA. Translation: CAM65344.1.
RefSeqiXP_001462998.1. XM_001462961.1.

Genome annotation databases

GeneIDi5066544.
KEGGilif:LINJ_05_0350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796437 Genomic DNA. Translation: CAM65344.1.
RefSeqiXP_001462998.1. XM_001462961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JK6X-ray2.95A/B1-491[»]
2W0HX-ray3.00A/B1-491[»]
2X50X-ray3.30A/B1-490[»]
2YAUX-ray3.50A/B1-491[»]
4ADWX-ray3.61A/B1-491[»]
4APNX-ray3.20A/B1-491[»]
ProteinModelPortaliA4HSF7.
SMRiA4HSF7. Positions 2-486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi435258.XP_001462998.1.

Chemistry

BindingDBiA4HSF7.
ChEMBLiCHEMBL1944501.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5066544.
KEGGilif:LINJ_05_0350.

Phylogenomic databases

eggNOGiCOG1249.
InParanoidiA4HSF7.
KOiK04283.
OMAiVIGASMC.

Enzyme and pathway databases

BRENDAi1.8.1.12. 2949.

Miscellaneous databases

EvolutionaryTraceiA4HSF7.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR001864. Trypnth_redctse.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00470. TRYPANRDTASE.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01423. trypano_reduc. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JPCM5Imported.
  2. "Molecular basis of antimony treatment in leishmaniasis."
    Baiocco P., Colotti G., Franceschini S., Ilari A.
    J. Med. Chem. 52:2603-2612(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH FAD AND NADP, DISULFIDE BONDS.
  3. "Inhibitory Effect of Silver Nanoparticles on Trypanothione Reductase Activity and Leishmania infantum Proliferation."
    Baiocco P., Ilari A., Ceci P., Orsini S., Gramiccia M., Di Muccio T., Colotti G.
    ACS Med. Chem. Lett. 2:230-233(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-490 IN COMPLEX WITH FAD AND NADP.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JPCM5Imported.
  5. "A gold-containing drug against parasitic polyamine metabolism: the X-ray structure of trypanothione reductase from Leishmania infantum in complex with auranofin reveals a dual mechanism of enzyme inhibition."
    Ilari A., Baiocco P., Messori L., Fiorillo A., Boffi A., Gramiccia M., Di Muccio T., Colotti G.
    Amino Acids 42:803-811(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH FAD AND NADP, DISULFIDE BONDS.
  6. "Inhibition of Leishmania infantum trypanothione reductase by azole-based compounds: a comparative analysis with its physiological substrate by X-ray crystallography."
    Baiocco P., Poce G., Alfonso S., Cocozza M., Porretta G.C., Colotti G., Biava M., Moraca F., Botta M., Yardley V., Fiorillo A., Lantella A., Malatesta F., Ilari A.
    ChemMedChem 8:1175-1183(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH FAD AND NADP.

Entry informationi

Entry nameiA4HSF7_LEIIN
AccessioniPrimary (citable) accession number: A4HSF7
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: July 22, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.