Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A4HSF7

- A4HSF7_LEIIN

UniProt

A4HSF7 - A4HSF7_LEIIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Submitted name:

Trypanothione reductase

Gene

TRYR

Organism
Leishmania infantum
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101FADImported
Binding sitei51 – 511FADImported
Binding sitei56 – 561FADImported
Binding sitei60 – 601FADImported
Binding sitei127 – 1271FAD; via amide nitrogen and carbonyl oxygenImported
Binding sitei159 – 1591FAD; via carbonyl oxygenImported
Binding sitei228 – 2281NADPImported
Binding sitei228 – 2281Sulfate 3
Binding sitei228 – 2281Sulfate 4
Binding sitei327 – 3271FADImported
Binding sitei333 – 3331NADP; via carbonyl oxygenImported
Binding sitei365 – 3651NADP; via carbonyl oxygenImported
Binding sitei461 – 4611FAD; via carbonyl oxygenImported

Regions

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

GO - Molecular functioni

  1. disulfide oxidoreductase activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. trypanothione-disulfide reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Ligandi

FADUniRule annotationImported, Flavoprotein, NADPImported, Nucleotide-bindingImported

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: Chromosome 5

Interactioni

Protein-protein interaction databases

STRINGi5671.LinJ05.0350.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 2222Sulfate 3 binding
Regioni221 – 2222Sulfate 4 binding
Regioni284 – 2863Sulfate 2 binding
Regioni284 – 2863Sulfate 3 binding

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.
OMAiDAKNYGW.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
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]
PRINTSiPR00368. FADPNR.
PR00470. 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
FR796437 Genomic DNA. Translation: CAM65344.1 .
RefSeqi XP_001462998.1. XM_001462961.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JK6 X-ray 2.95 A/B 1-491 [» ]
2W0H X-ray 3.00 A/B 1-491 [» ]
2X50 X-ray 3.30 A/B 1-490 [» ]
2YAU X-ray 3.50 A/B 1-491 [» ]
4ADW X-ray 3.61 A/B 1-491 [» ]
4APN X-ray 3.20 A/B 1-491 [» ]
ProteinModelPortali A4HSF7.
SMRi A4HSF7. Positions 2-486.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5671.LinJ05.0350.

Chemistry

ChEMBLi CHEMBL1944501.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5066544.
KEGGi lif:LINJ_05_0350.

Phylogenomic databases

eggNOGi COG1249.
InParanoidi A4HSF7.
KOi K04283.
OMAi DAKNYGW.

Miscellaneous databases

EvolutionaryTracei A4HSF7.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
PR00470. TRYPANRDTASE.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01423. trypano_reduc. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
  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.
  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: October 29, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3