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Reviewed, UniProtKB/Swiss-Prot O46411 (5NTC_BOVIN)

Last modified February 9, 2010. Version 49. 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
    Cytosolic IMP/GMP-specific 5'-nucleotidase
Gene names
Name: NT5C2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length560 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. Ref.1

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.

Subunit structure

Homotetramer 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
   PTMPhosphoprotein
   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 – 560560Cytosolic purine 5'-nucleotidase
PRO_0000310263

Regions

Region202 – 2109Substrate binding Potential
Compositional bias549 – 56012Asp/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

Amino acid modifications

Modified residue5021Phosphoserine By similarity
Modified residue5271Phosphoserine By similarity

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Sequences

Sequence LengthMass (Da)Tools
O46411-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 85E7CC64BF2581A0

FASTA56064,841
        10         20         30         40         50         60 
MTTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY 

        70         80         90        100        110        120 
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV 

       130        140        150        160        170        180 
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS 

       190        200        210        220        230        240 
CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK 

       250        260        270        280        290        300 
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT 

       310        320        330        340        350        360 
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTVCDLLG 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 EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA 

       550        560 
PQEITHCHDE DDDEEEEEEE

« Hide

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References

[1]"Bovine cytosolic IMP/GMP-specific 5'-nucleotidase: cloning and expression of active enzyme in Escherichia coli."
Allegrini S., Pesi R., Tozzi M.G., Fiol C.J., Johnson R.B., Eriksson S.
Biochem. J. 328:483-487(1997) [PubMed: 9371705] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Thymus.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U73690 mRNA. Translation: AAC48784.1.
IPIIPI00716154.
RefSeqNP_776830.1.
UniGeneBt.5382

3D structure databases

HSSPHSSP built from PDB template 2BDE based on UniProtKB Q5ZZB6.
SMRO46411. Positions 3-488.
ModBaseSearch...

Protein-protein interaction databases

STRINGO46411.

Genome annotation databases

EnsemblENSBTAT00000017090; ENSBTAP00000017090; ENSBTAG00000012858; Bos taurus. [Genome view]
GeneID281951.
KEGGbta:281951.

Organism-specific databases

CTD281951.

Phylogenomic databases

eggNOGmaNOG04834.
HOVERGENO46411.
InParanoidO46411.
OMAIGAKGKD.
OrthoDBEOG9HTCBT.
PhylomeDBO46411.

Enzyme and pathway databases

BRENDA3.1.3.5. 251.

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_BOVIN
AccessionPrimary (citable) accession number: O46411
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 1998
Last modified: February 9, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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