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Reviewed, UniProtKB/Swiss-Prot Q5EBF1 (5NTC_XENTR)

Last modified June 16, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytosolic purine 5'-nucleotidase
    EC=3.1.3.5
Alternative name(s):
    5'-nucleotidase cytosolic II
Gene names
Name: nt5c2
OrganismXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifier8364 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusSilurana

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides By similarity.

Catalytic activity

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Enzyme regulation

Allosterically activated by various compounds, including ATP By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 5'(3')-deoxyribonucleotidase family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological processnucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function5'-nucleotidase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 568568Cytosolic purine 5'-nucleotidase
PRO_0000310268

Regions

Region202 – 2109Substrate binding Potential
Compositional bias549 – 56820Asp/Glu-rich (acidic)

Sites

Active site521Nucleophile By similarity
Active site541Proton donor By similarity
Metal binding521Magnesium By similarity
Metal binding541Magnesium; via carbonyl oxygen By similarity
Metal binding3511Magnesium By similarity
Binding site1271Allosteric activator 1 By similarity
Binding site1541Allosteric activator 2 By similarity
Binding site3541Allosteric activator 2 By similarity
Binding site4361Allosteric activator 1; via carbonyl oxygen By similarity
Binding site4531Allosteric activator 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5EBF1-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: E5FB912D35AD64DD

FASTA56865,965
        10         20         30         40         50         60 
MTTSWSDRLQ NAADLPANMD GHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY 

        70         80         90        100        110        120 
KSPEYESLGF DLTVERLVSI GYPQELLNFV YDPTFPTRGL VFDSTYGNLL KVDAYGNILV 

       130        140        150        160        170        180 
CAHGFNFMRG PEIREQYPNK FIQRDDTDRF YILNTLFNLP ETYLLACLVD FFTNCDRYTS 

       190        200        210        220        230        240 
CEMGFKDGDL FMSFRSMFQD VRDAVDWVHY KGSLKEKTVE NLPKYVVKDP KLPLLLSRMN 

       250        260        270        280        290        300 
EVGKVFLVTN SDYKYTHKIM TYLFDLPHGP KPGSSHRLWQ TYFDLILVDA RKPLFFGEGT 

       310        320        330        340        350        360 
VLRQVDTNTG KLKIGTYTGP LQHGIVYSGG SSDIVCDLLG AKGKDILYIG DHIFGDILKS 

       370        380        390        400        410        420 
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ 

       430        440        450        460        470        480 
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA 

       490        500        510        520        530        540 
HVLMPHESTV EHTHVDIHET ESPMATRNRC SLDFKDSDFK RHQLTRSISE IKPPNLFPQK 

       550        560 
PQEITHCHDE DDDEEEEEEE EEEEEEEE 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

BC089713 mRNA. Translation: AAH89713.1.
RefSeqNP_001015773.1.
UniGeneStr.5805

3D structure databases

SMRQ5EBF1. Positions 3-488.
ModBaseSearch...

Genome annotation databases

GeneID548490.
KEGGxtr:548490.

Organism-specific databases

XenbaseXB-FEAT-988874. nt5c2.

Phylogenomic databases

HOVERGENQ5EBF1.

Enzyme and pathway databases

BRENDA3.1.3.5. 279072.

Family and domain databases

InterProIPR008380. HAD-SF_hydro_IG_5-nucl.
IPR016695. Pur_nucleotidase.
[Graphical view]
PANTHERPTHR12103. HAD-SF_hydro_IG_5-nucl. 1 hit.
PfamPF05761. 5_nucleotid. 1 hit.
[Graphical view]
PIRSFPIRSF017434. Purine_5'-nucleotidase. 1 hit.
TIGRFAMsTIGR02244. HAD-IG-Ncltidse. 1 hit.
ProtoNetSearch...

Entry information

Entry name5NTC_XENTR
AccessionPrimary (citable) accession number: Q5EBF1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 15, 2005
Last modified: June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents