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Q27546 (IUNH_CRIFA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-uridine preferring nucleoside hydrolase

Short name=IU-NH
Short name=IU-nucleoside hydrolase
EC=3.2.2.-
Alternative name(s):
Non-specific nucleoside hydrolase
Purine nucleosidase
Gene names
Name:IUNH
OrganismCrithidia fasciculata
Taxonomic identifier5656 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Calcium.

Pathway

Purine metabolism; purine nucleoside salvage.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the IUNH family.

Mass spectrometry

Molecular mass is 34194±4 Da from positions 2 - 315. Determined by ESI. Ref.1

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 315314Inosine-uridine preferring nucleoside hydrolase
PRO_0000206810

Sites

Active site2411
Metal binding101Calcium
Metal binding151Calcium
Metal binding1261Calcium
Metal binding2421Calcium
Binding site141Substrate
Binding site1601Substrate
Binding site1661Substrate
Binding site1681Substrate

Experimental info

Mutagenesis2411H → A: Loss of activity.

Secondary structure

............................................................. 315
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q27546 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B88CF9DA41B53F43

FASTA31534,326
        10         20         30         40         50         60 
MPKKIILDCD PGLDDAVAIL LAHGNPEIEL LAITTVVGNQ TLAKVTRNAQ LVADIAGITG 

        70         80         90        100        110        120 
VPIAAGCDKP LVRKIMTAGH IHGESGMGTV AYPAEFKNKV DERHAVNLII DLVMSHEPKT 

       130        140        150        160        170        180 
ITLVPTGGLT NIAMAARLEP RIVDRVKEVV LMGGGYHEGN ATSVAEFNII IDPEAAHIVF 

       190        200        210        220        230        240 
NESWQVTMVG LDLTHQALAT PPILQRVKEV DTNPARFMLE IMDYYTKIYQ SNRYMAAAAV 

       250        260        270        280        290        300 
HDPCAVAYVI DPSVMTTERV PVDIELTGKL TLGMTVADFR NPRPEHCHTQ VAVKLDFEKF 

       310 
WGLVLDALER IGDPQ 

« Hide

References

[1]"Inosine-uridine nucleoside hydrolase from Crithidia fasciculata. Genetic characterization, crystallization, and identification of histidine 241 as a catalytic site residue."
Gopaul D.N., Meyer S.L., Degano M., Sacchettini J.C., Schramm V.L.
Biochemistry 35:5963-5970(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, MUTAGENESIS.
[2]"Three-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata."
Degano M., Gopaul D.N., Scapin G., Schramm V.L., Sacchettini J.C.
Biochemistry 35:5971-5981(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND CALCIUM IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43371 Genomic DNA. Translation: AAC47119.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MASX-ray2.50A/B3-315[»]
2MASX-ray2.30A/B/C/D3-314[»]
ProteinModelPortalQ27546.
SMRQ27546. Positions 3-314.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00606.

Family and domain databases

Gene3D3.90.245.10. 1 hit.
InterProIPR015910. I/U_nuclsd_hydro_CS.
IPR023186. Inosine/uridine_hydrolase.
IPR001910. Inosine/uridine_hydrolase_dom.
[Graphical view]
PANTHERPTHR12304. PTHR12304. 1 hit.
PfamPF01156. IU_nuc_hydro. 1 hit.
[Graphical view]
SUPFAMSSF53590. SSF53590. 1 hit.
PROSITEPS01247. IUNH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ27546.

Entry information

Entry nameIUNH_CRIFA
AccessionPrimary (citable) accession number: Q27546
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways