SubmitCancel

Skip Header

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

Q27546

- IUNH_CRIFA

UniProt

Q27546 - IUNH_CRIFA

(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
Inosine-uridine preferring nucleoside hydrolase
Gene
IUNH
Organism
Crithidia fasciculata
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Calcium.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101Calcium
Binding sitei14 – 141Substrate
Metal bindingi15 – 151Calcium
Metal bindingi126 – 1261Calcium
Binding sitei160 – 1601Substrate
Binding sitei166 – 1661Substrate
Binding sitei168 – 1681Substrate
Active sitei241 – 2411
Metal bindingi242 – 2421Calcium

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing N-glycosyl compounds Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. nucleotide metabolic process Source: UniProtKB-KW
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:IUNH
OrganismiCrithidia fasciculata
Taxonomic identifieri5656 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi241 – 2411H → A: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 315314Inosine-uridine preferring nucleoside hydrolase
PRO_0000206810Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97
Helixi13 – 2412
Beta strandi28 – 358
Beta strandi37 – 404
Helixi42 – 5514
Beta strandi63 – 653
Beta strandi71 – 733
Helixi79 – 824
Beta strandi84 – 874
Helixi105 – 11511
Beta strandi121 – 1255
Helixi130 – 1389
Helixi142 – 1454
Beta strandi148 – 1525
Beta strandi160 – 1645
Helixi167 – 1704
Helixi173 – 1819
Beta strandi182 – 1843
Beta strandi186 – 1894
Helixi191 – 1944
Helixi201 – 2088
Helixi213 – 23018
Beta strandi236 – 2394
Helixi242 – 2509
Helixi252 – 2543
Beta strandi255 – 2595
Beta strandi262 – 2643
Turni269 – 2735
Beta strandi275 – 2773
Beta strandi288 – 2958
Helixi297 – 31115

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MASX-ray2.50A/B3-315[»]
2MASX-ray2.30A/B/C/D3-315[»]
ProteinModelPortaliQ27546.
SMRiQ27546. Positions 3-314.

Miscellaneous databases

EvolutionaryTraceiQ27546.

Family & Domainsi

Sequence similaritiesi

Belongs to the IUNH family.

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.

Q27546-1 [UniParc]FASTAAdd to Basket

« Hide

MPKKIILDCD PGLDDAVAIL LAHGNPEIEL LAITTVVGNQ TLAKVTRNAQ    50
LVADIAGITG VPIAAGCDKP LVRKIMTAGH IHGESGMGTV AYPAEFKNKV 100
DERHAVNLII DLVMSHEPKT ITLVPTGGLT NIAMAARLEP RIVDRVKEVV 150
LMGGGYHEGN ATSVAEFNII IDPEAAHIVF NESWQVTMVG LDLTHQALAT 200
PPILQRVKEV DTNPARFMLE IMDYYTKIYQ SNRYMAAAAV HDPCAVAYVI 250
DPSVMTTERV PVDIELTGKL TLGMTVADFR NPRPEHCHTQ VAVKLDFEKF 300
WGLVLDALER IGDPQ 315
Length:315
Mass (Da):34,326
Last modified:January 23, 2007 - v3
Checksum:iB88CF9DA41B53F43
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43371 Genomic DNA. Translation: AAC47119.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43371 Genomic DNA. Translation: AAC47119.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MAS X-ray 2.50 A/B 3-315 [» ]
2MAS X-ray 2.30 A/B/C/D 3-315 [» ]
ProteinModelPortali Q27546.
SMRi Q27546. Positions 3-314.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00606 .

Miscellaneous databases

EvolutionaryTracei Q27546.

Family and domain databases

Gene3Di 3.90.245.10. 1 hit.
InterProi IPR015910. I/U_nuclsd_hydro_CS.
IPR023186. Inosine/uridine_hydrolase.
IPR001910. Inosine/uridine_hydrolase_dom.
[Graphical view ]
PANTHERi PTHR12304. PTHR12304. 1 hit.
Pfami PF01156. IU_nuc_hydro. 1 hit.
[Graphical view ]
SUPFAMi SSF53590. SSF53590. 1 hit.
PROSITEi PS01247. IUNH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiIUNH_CRIFA
AccessioniPrimary (citable) accession number: Q27546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

External Data

Dasty 3

Similar proteinsi