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Reviewed, UniProtKB/Swiss-Prot Q5ZIZ4 (5NTC_CHICK)

Last modified September 1, 2009. Version 28. 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
ORF Names: RCJMB04_22h21
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length569 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 – 569569Cytosolic purine 5'-nucleotidase
PRO_0000310266

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

Sequences

Sequence LengthMass (Da)Tools
Q5ZIZ4-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: C8FD122625879CB6

FASTA56965,894
        10         20         30         40         50         60 
MTTSWSDRLQ NAADLPANMD GHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY 

        70         80         90        100        110        120 
KSPEYESLGF DLTVERLVSI GYPHELLNFV YDPAFPTRGL VFDTHYGNLL KVDAYGNLLV 

       130        140        150        160        170        180 
CAHGFNFLRG PETRDQYPNK FIQRDDTDRF YILNTLFNLP ETYLLACLVD FFTNCDRYTS 

       190        200        210        220        230        240 
CETGFKDGDL FMSFRSMFQD VRDAVDWVHY KGSLKEKTLE NLEKYVVKDG KLPLLLSRMN 

       250        260        270        280        290        300 
EVGKVFLVTN SDYKYTDKIM TYLFDFPHGP KPGSAHRPWQ SYFDLILVDA RKPLFFGEGT 

       310        320        330        340        350        360 
VLRQVDTVTG KLKIGTYTGP LQHGIVYSGG SSDTVCDLLG AKGKDILYIG DHIFGDILKS 

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

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

       490        500        510        520        530        540 
HVLMPHESTV EHTHVDINEK ESPMATRNRT SVDFKDSDYK RHQLTRSISE IKPPNLFPQA 

       550        560 
PQEITHCHDE DDDEEEEEEE VEEEEEEEE 

« Hide

References

[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005) [PubMed: 15642098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Cross-references

Sequence databases

AJ720640 mRNA. Translation: CAG32299.1.
IPIIPI00583285.
RefSeqNP_001026405.1.
UniGeneGga.22448

3D structure databases

SMRQ5ZIZ4. Positions 3-488.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5ZIZ4.

Genome annotation databases

EnsemblENSGALT00000013309; ENSGALP00000013294; ENSGALG00000008179; Gallus gallus. [Genome view]
GeneID423871.
KEGGgga:423871.

Organism-specific databases

CTD423871.

Phylogenomic databases

HOGENOMQ5ZIZ4.
HOVERGENQ5ZIZ4.

Enzyme and pathway databases

BRENDA3.1.3.5. 4.

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_CHICK
AccessionPrimary (citable) accession number: Q5ZIZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 23, 2004
Last modified: September 1, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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