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Protein
Submitted name:

IAG-nucleoside hydrolase

Gene
N/A
Organism
Trypanosoma vivax (Duttonella vivax)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101CalciumCombined sources
Binding sitei10 – 101SubstrateCombined sources
Metal bindingi15 – 151CalciumCombined sources
Binding sitei83 – 831SubstrateCombined sources
Metal bindingi137 – 1371Calcium; via carbonyl oxygenCombined sources
Binding sitei186 – 1861SubstrateCombined sources
Sitei260 – 2601Important for catalytic activityCombined sources
Metal bindingi261 – 2611CalciumCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15858.
BRENDAi3.2.2.1. 6532.
SABIO-RKQ9GPQ4.

Names & Taxonomyi

Protein namesi
Submitted name:
IAG-nucleoside hydrolaseImported
OrganismiTrypanosoma vivax (Duttonella vivax)Imported
Taxonomic identifieri5699 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaDuttonella

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL6134.

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi85 – 85Interchain (with C-248)Combined sources
Disulfide bondi248 – 248Interchain (with C-85)Combined sources

Interactioni

Chemistry

BindingDBiQ9GPQ4.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HOZX-ray1.60A/B2-327[»]
1HP0X-ray2.10A/B2-327[»]
1KICX-ray1.60A/B2-327[»]
1KIEX-ray2.00A/B2-327[»]
1R4FX-ray2.30A/B2-327[»]
2FF1X-ray2.07A/B2-327[»]
2FF2X-ray2.20A/B2-327[»]
3B9GX-ray1.40A/B2-244[»]
A/B258-327[»]
3EPWX-ray1.30A/B2-327[»]
3EPXX-ray1.85A/B2-327[»]
ProteinModelPortaliQ9GPQ4.
SMRiQ9GPQ4. Positions 2-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9GPQ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 296294IU_nuc_hydroInterPro annotationAdd
BLAST

Family and domain databases

Gene3Di3.90.245.10. 1 hit.
InterProiIPR023186. 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.

Sequencei

Sequence statusi: Complete.

Q9GPQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKNVVLDHD GNLDDFVAMV LLASNTEKVR LIGALCTDAD CFVENGFNVT
60 70 80 90 100
GKIMCLMHNN MNLPLFPIGK SAATAVNPFP KEWRCLAKNM DDMPILNIPE
110 120 130 140 150
NVELWDKIKA ENEKYEGQQL LADLVMNSEE KVTICVTGPL SNVAWCIDKY
160 170 180 190 200
GEKFTSKVEE CVIMGGAVDV RGNVFLPSTD GTAEWNIYWD PASAKTVFGC
210 220 230 240 250
PGLRRIMFSL DSTNTVPVRS PYVQRFGEQT NFLLSILVGT MWAMCTHCEL
260 270 280 290 300
LRDGDGYYAW DALTAAYVVD QKVANVDPVP IDVVVDKQPN EGATVRTDAE
310 320
KYPLTFVARN PEAEFFLDML LRSARAC
Length:327
Mass (Da):36,331
Last modified:March 1, 2001 - v1
Checksum:i034F9833FF6C2825
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF311701 mRNA. Translation: AAG38561.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF311701 mRNA. Translation: AAG38561.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HOZX-ray1.60A/B2-327[»]
1HP0X-ray2.10A/B2-327[»]
1KICX-ray1.60A/B2-327[»]
1KIEX-ray2.00A/B2-327[»]
1R4FX-ray2.30A/B2-327[»]
2FF1X-ray2.07A/B2-327[»]
2FF2X-ray2.20A/B2-327[»]
3B9GX-ray1.40A/B2-244[»]
A/B258-327[»]
3EPWX-ray1.30A/B2-327[»]
3EPXX-ray1.85A/B2-327[»]
ProteinModelPortaliQ9GPQ4.
SMRiQ9GPQ4. Positions 2-327.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ9GPQ4.
ChEMBLiCHEMBL6134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15858.
BRENDAi3.2.2.1. 6532.
SABIO-RKQ9GPQ4.

Miscellaneous databases

EvolutionaryTraceiQ9GPQ4.

Family and domain databases

Gene3Di3.90.245.10. 1 hit.
InterProiIPR023186. 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.
ProtoNetiSearch...

Publicationsi

  1. "Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax."
    Versees W., Decanniere K., Pelle R., Depoorter J., Brosens E., Parkin D.W., Steyaert J.
    J. Mol. Biol. 307:1363-1379(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax."
    Versees W., Decanniere K., Van Holsbeke E., Devroede N., Steyaert J.
    J. Biol. Chem. 277:15938-15946(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-327 IN COMPLEX WITH CALCIUM.
  3. "Leaving group activation by aromatic stacking: an alternative to general acid catalysis."
    Versees W., Loverix S., Vandemeulebroucke A., Geerlings P., Steyaert J.
    J. Mol. Biol. 338:1-6(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-327 IN COMPLEX WITH CALCIUM.
  4. "Transition-state complex of the purine-specific nucleoside hydrolase of T. vivax: enzyme conformational changes and implications for catalysis."
    Versees W., Barlow J., Steyaert J.
    J. Mol. Biol. 359:331-346(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 2-327 IN COMPLEX WITH CALCIUM.
  5. "A flexible loop as a functional element in the catalytic mechanism of nucleoside hydrolase from Trypanosoma vivax."
    Vandemeulebroucke A., De Vos S., Van Holsbeke E., Steyaert J., Versees W.
    J. Biol. Chem. 283:22272-22282(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-244 AND 258-327 IN COMPLEX WITH CALCIUM.
  6. "Crystal structures of T. vivax nucleoside hydrolase in complex with new potent and specific inhibitors."
    Versees W., Goeminne A., Berg M., Vandemeulebroucke A., Haemers A., Augustyns K., Steyaert J.
    Biochim. Biophys. Acta 1794:953-960(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-327 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.

Entry informationi

Entry nameiQ9GPQ4_TRYVI
AccessioniPrimary (citable) accession number: Q9GPQ4
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.