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Reviewed, UniProtKB/Swiss-Prot Q6DKB0 (5NTC_XENLA)

Last modified February 9, 2010. Version 33. 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

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Names and origin

Protein namesRecommended name:
    Cytosolic purine 5'-nucleotidase
    EC=3.1.3.5
Alternative name(s):
    Cytosolic 5'-nucleotidase II
Gene names
Name: nt5c2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 569569Cytosolic purine 5'-nucleotidase
PRO_0000310267

Regions

Region202 – 2109Substrate binding Potential
Compositional bias549 – 56921Asp/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

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Sequences

Sequence LengthMass (Da)Tools
Q6DKB0-1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: E181B6EAF7455227

FASTA56966,180
        10         20         30         40         50         60 
MTTSWSDRLQ NAADLPANMD RHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY 

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

       130        140        150        160        170        180 
CAHGFNFMRG LETREQYPNK FIQRDDTDRF YILNTLFNLP ETYLLACLVD FFTNCDRYSS 

       190        200        210        220        230        240 
CETGFKDGDL FMSFRSMFQD VRDAVDWVHY KGSLKEKTVE NLPKYVVKDS KLPLLLSRMN 

       250        260        270        280        290        300 
EVGKVFLVTN SDYKYTHKIM TYLFDLPHGP KPDSSHRVWQ SYFDLILVDA RKPLFFGEGT 

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

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

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

       490        500        510        520        530        540 
HVLMPHESTV EHAHVDIHES ESPMATRNRC SLDFKDSEFK RHHLTRSISE IKPPNLFPQK 

       550        560 
PREITHCHDE DDDEEEEEEE EEEEEEEEE

« Hide

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References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC074446 mRNA. Translation: AAH74446.1.
RefSeqNP_001086300.1.
UniGeneXl.9923

3D structure databases

HSSPHSSP built from PDB template 2BDE based on UniProtKB Q5ZZB6.
SMRQ6DKB0. Positions 3-488.
ModBaseSearch...

Genome annotation databases

GeneID444729.
KEGGxla:444729.

Organism-specific databases

XenbaseXB-FEAT-988874. nt5c2.

Phylogenomic databases

HOVERGENQ6DKB0.

Enzyme and pathway databases

BRENDA3.1.3.5. 648.

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...

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Entry information

Entry name5NTC_XENLA
AccessionPrimary (citable) accession number: Q6DKB0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: August 16, 2004
Last modified: February 9, 2010
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

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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