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Protein

Inosine-uridine preferring nucleoside hydrolase

Gene

NSNH

Organism
Leishmania major
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates.1 Publication

Catalytic activityi

A purine nucleoside + H2O = D-ribose + a purine base.1 Publication

Cofactori

Ca2+1 Publication

Pathwayi: purine nucleoside salvage

This protein is involved in the pathway purine nucleoside salvage, which is part of Purine metabolism.
View all proteins of this organism that are known to be involved in the pathway purine nucleoside salvage and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101Calcium
Binding sitei14 – 141SubstrateBy similarity
Metal bindingi15 – 151Calcium
Metal bindingi126 – 1261Calcium
Binding sitei160 – 1601SubstrateBy similarity
Binding sitei166 – 1661SubstrateBy similarity
Binding sitei168 – 1681SubstrateBy similarity
Active sitei240 – 2401By similarity
Metal bindingi241 – 2411Calcium

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • inosine nucleosidase activity Source: UniProtKB
  • purine nucleosidase activity Source: UniProtKB
  • uridine nucleosidase activity Source: UniProtKB

GO - Biological processi

  • nucleotide metabolic process Source: UniProtKB-KW
  • purine-containing compound salvage Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00606.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-uridine preferring nucleoside hydrolase (EC:3.2.2.-)
Short name:
IU-NH
Short name:
IU-nucleoside hydrolase
Alternative name(s):
Non-specific nucleoside hydrolase
Purine nucleosidase
Gene namesi
Name:NSNH
OrganismiLeishmania major
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 314313Inosine-uridine preferring nucleoside hydrolasePRO_0000206811Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi5664.LmjF.18.1580.

Structurei

Secondary structure

1
314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi13 – 2412Combined sources
Beta strandi28 – 358Combined sources
Helixi42 – 5514Combined sources
Beta strandi63 – 653Combined sources
Beta strandi71 – 733Combined sources
Beta strandi85 – 873Combined sources
Helixi105 – 11511Combined sources
Beta strandi121 – 1255Combined sources
Helixi130 – 1389Combined sources
Helixi142 – 1454Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi160 – 1645Combined sources
Helixi167 – 1704Combined sources
Helixi173 – 1808Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi186 – 1894Combined sources
Helixi191 – 1944Combined sources
Helixi201 – 21010Combined sources
Helixi213 – 22816Combined sources
Helixi230 – 2323Combined sources
Beta strandi233 – 2353Combined sources
Helixi242 – 2498Combined sources
Helixi251 – 2533Combined sources
Beta strandi254 – 2574Combined sources
Beta strandi261 – 2633Combined sources
Turni268 – 2725Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi287 – 2948Combined sources
Helixi296 – 31015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZRX-ray2.50A/B/C/D1-314[»]
ProteinModelPortaliP83851.
SMRiP83851. Positions 2-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83851.

Family & Domainsi

Sequence similaritiesi

Belongs to the IUNH family.1 Publication

Phylogenomic databases

eggNOGiKOG2938. Eukaryota.
COG1957. LUCA.

Family and domain databases

Gene3Di3.90.245.10. 1 hit.
InterProiIPR015910. I/U_nuclsd_hydro_CS.
IPR023186. Inosine/uridine_hydrolase.
IPR001910. Inosine/uridine_hydrolase_dom.
[Graphical view]
PANTHERiPTHR12304. PTHR12304. 1 hit.
PfamiPF01156. IU_nuc_hydro. 1 hit.
[Graphical view]
SUPFAMiSSF53590. SSF53590. 1 hit.
PROSITEiPS01247. IUNH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83851-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRKIILDCD PGIDDAVAIF LAHGNPEIEL LAITTVVGNQ SLEKVTQNAR
60 70 80 90 100
LVADVAGIVG VPVAAGCTKP LVRGVRNASH IHGETGMGNV SYPPEFKTKL
110 120 130 140 150
DGRHAVQLII DLIMSHEPKT ITLVPTGGLT NIAMAVRLEP RIVDRVKEVV
160 170 180 190 200
LMGGGYHTGN ASPVAEFNVF IDPEAAHIVF NESWNVTMVG LDLTHQALAT
210 220 230 240 250
PAVQKRVREV GTKPAAFMLQ ILDFYTKVYE KEHDTYGKVH DPCAVAYVID
260 270 280 290 300
PTVMTTERVP VDIELNGALT TGMTVVDFRY PRPKNCRTQV AVKLDFDKFW
310
CLVIDALERI GDPQ
Length:314
Mass (Da):34,310
Last modified:January 23, 2007 - v3
Checksum:i947D924C65FD0723
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961Q → L (PubMed:10409664).Curated
Sequence conflicti276 – 2761V → A (PubMed:10409664).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY533501 Genomic DNA. Translation: AAS48367.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY533501 Genomic DNA. Translation: AAS48367.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZRX-ray2.50A/B/C/D1-314[»]
ProteinModelPortaliP83851.
SMRiP83851. Positions 2-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5664.LmjF.18.1580.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2938. Eukaryota.
COG1957. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00606.

Miscellaneous databases

EvolutionaryTraceiP83851.

Family and domain databases

Gene3Di3.90.245.10. 1 hit.
InterProiIPR015910. I/U_nuclsd_hydro_CS.
IPR023186. Inosine/uridine_hydrolase.
IPR001910. Inosine/uridine_hydrolase_dom.
[Graphical view]
PANTHERiPTHR12304. PTHR12304. 1 hit.
PfamiPF01156. IU_nuc_hydro. 1 hit.
[Graphical view]
SUPFAMiSSF53590. SSF53590. 1 hit.
PROSITEiPS01247. IUNH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and sequencing of nonspecific nucleoside hydrolase (nsnh) from Leishmania."
    Banuls A.L., Hide M.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MHOM/SU/73/5ASKHImported.
  2. "Nucleoside hydrolase from Leishmania major. Cloning, expression, catalytic properties, transition state inhibitors, and the 2.5-A crystal structure."
    Shi W., Schramm V.L., Almo S.C.
    J. Biol. Chem. 274:21114-21120(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiIUNH_LEIMA
AccessioniPrimary (citable) accession number: P83851
Secondary accession number(s): Q6QMH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 23, 2007
Last modified: November 11, 2015
This is version 53 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.