A4HSF7 (A4HSF7_LEIIN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Trypanothione reductase EMBL CAM65344.1
EC=1.8.1.12 EMBL CAM65344.1

Gene names

Name:	TRYR EMBL CAM65344.1
ORF Names:	LINJ_05_0350 EMBL CAM65344.1

Organism

Leishmania infantum [Reference proteome]

Taxonomic identifier

5671 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania › Leishmania › Leishmania donovani species complex

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. RuleBase RU003691

Ontologies

Keywords
Domain	Redox-active center RuleBase RU003691
Ligand	FAD RuleBase RU003691 PDB 2X50 PDB 2JK6 PDB 2W0H Flavoprotein RuleBase RU003691 PDB 2X50 PDB 2JK6 PDB 2W0H NADP PDB 2X50 PDB 2W0H Nucleotide-binding PDB 2X50 PDB 2JK6 PDB 2W0H
Molecular function	Oxidoreductase RuleBase RU003691 EMBL CAM65344.1
Technical term	3D-structure PDB 2X50 PDB 2JK6 PDB 2W0H PDB 4ADW PDB 2YAU Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro trypanothione-disulfide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	14 – 15	2	FAD PDB 2X50 PDB 2JK6 PDB 2W0H
	Nucleotide binding	196 – 202	7	NADP PDB 2X50 PDB 2W0H
	Nucleotide binding	221 – 222	2	NADP PDB 2X50 PDB 2W0H
	Nucleotide binding	284 – 286	3	NADP PDB 2X50 PDB 2W0H
	Nucleotide binding	333 – 335	3	FAD PDB 2X50 PDB 2JK6 PDB 2W0H
Sites
	Binding site	35	1	FAD PDB 2X50 PDB 2JK6 PDB 2W0H
	Binding site	47	1	FAD; via carbonyl oxygen PDB 2X50 PDB 2JK6 PDB 2W0H
	Binding site	51	1	FAD PDB 2X50 PDB 2JK6 PDB 2W0H
	Binding site	56	1	FAD PDB 2X50
	Binding site	60	1	FAD PDB 2X50 PDB 2JK6 PDB 2W0H
	Binding site	127	1	FAD; via amide nitrogen and carbonyl oxygen PDB 2X50 PDB 2JK6 PDB 2W0H
	Binding site	228	1	NADP PDB 2X50 PDB 2W0H
	Binding site	327	1	FAD PDB 2X50 PDB 2JK6 PDB 2W0H
	Binding site	333	1	NADP; via carbonyl oxygen PDB 2X50 PDB 2W0H
	Binding site	365	1	NADP; via carbonyl oxygen PDB 2X50 PDB 2W0H
	Binding site	461	1	FAD; via carbonyl oxygen PDB 2W0H

Sequences

	Sequence		Length	Mass (Da)
	A4HSF7 [UniParc]. Last modified May 1, 2007. Version 1. Checksum: 1E41FDC657DDCF67	FASTA	491	53,026
	10 20 30 40 50 60 MSRAYDLVVL GAGSGGLEAG WNAAVTHKKK VAVVDVQATH GPPLFAALGG TCVNVGCVPK 70 80 90 100 110 120 KLMVTGAQYM DLIRESGGFG WEMDRESLCP NWKTLIAAKN KVVNSINESY KSMFADTEGL 130 140 150 160 170 180 SFHMGFGALQ DAHTVVVRKS EDPHSDVLET LDTEYILIAT GSWPTRLGVP GDEFCITSNE 190 200 210 220 230 240 AFYLEDAPKR MLCVGGGYIA VEFAGIFNGY KPCGGYVDLC YRGDLILRGF DTEVRKSLTK 250 260 270 280 290 300 QLGANGIRVR TNLNPTKITK NEDGSNHVHF NDGTEEDYDQ VMLAIGRVPR SQALQLDKAG 310 320 330 340 350 360 VRTGKNGAVQ VDAYSKTSVD NIYAIGDVTN RVMLTPVAIN EGAAFVETVF GGKPRATDHT 370 380 390 400 410 420 KVACAVFSIP PIGTCGMTEE EAAKNYETVA VYASSFTPLM HNISGSKHKE FMIRIITNES 430 440 450 460 470 480 NGEVLGVHML GDSAPEIIQS VGICMKMGAK ISDFHSTIGV HPTSAEELCS MRTPAYFYES 490 GKRVEKLSSN L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomic analysis of three Leishmania species that cause diverse human disease." Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T., Hance Z. , Jagels K., Moule S., Ormond D., Rutter S., Sqaures R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M. Nat. Genet. 39:839-847(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JPCM5.
[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]	"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).
[4]	"Crystal Structure of Leishmania Infantum Trypanothione Reductase in Complex with Nadph and Trypanothione." Baiocco P., Ilari A., Colotti G., Malatesta F., Fiorillo A. Submitted (JAN-2012) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (3.61 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

FR796437 Genomic DNA. Translation: CAM65344.1.

RefSeq

XP_001462998.1. XM_001462961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

A4HSF7.

SMR

A4HSF7. Positions 2-486.

ModBase

Search...

Protein-protein interaction databases

STRING

5671.LinJ05.0350.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

5066544.

KEGG

lif:LINJ_05_0350.

Phylogenomic databases

eggNOG

COG1249.

KO

K04283.

OMA

ACAVFSI.

ProtClustDB

CLSZ2436777.

Family and domain databases

Gene3D

3.30.390.30. 1 hit.

InterPro

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]

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.
PR00470. TRYPANRDTASE.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.

TIGRFAMs

TIGR01423. trypano_reduc. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1944501.

EvolutionaryTrace

A4HSF7.

Entry information

Entry name

A4HSF7_LEIIN

Accession

Primary (citable) accession number: A4HSF7

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2007
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)