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

Names and origin

Protein names

Recommended 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

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	560 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 560	560	Cytosolic purine 5'-nucleotidase		PRO_0000310263
Regions
	Region	202 – 210	9	Substrate binding Potential
	Compositional bias	549 – 560	12	Asp/Glu-rich (acidic)
Sites
	Active site	52	1	Nucleophile By similarity
	Active site	54	1	Proton donor By similarity
	Metal binding	52	1	Magnesium By similarity
	Metal binding	54	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	351	1	Magnesium By similarity
	Binding site	127	1	Allosteric activator 1 By similarity
	Binding site	154	1	Allosteric activator 2 By similarity
	Binding site	354	1	Allosteric activator 2 By similarity
	Binding site	436	1	Allosteric activator 1; via carbonyl oxygen By similarity
	Binding site	453	1	Allosteric activator 2 By similarity
Amino acid modifications
	Modified residue	502	1	Phosphoserine By similarity
	Modified residue	527	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O46411 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 85E7CC64BF2581A0	FASTA	560	64,841
	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

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U73690 mRNA. Translation: AAC48784.1.
IPI	IPI00716154.
RefSeq	NP_776830.1. NM_174405.2.
UniGene	Bt.5382.
3D structure databases
HSSP	HSSP built from PDB template 2BDE based on UniProtKB Q5ZZB6.
ProteinModelPortal	O46411.
SMR	O46411. Positions 3-488.
ModBase	Search...
Protein-protein interaction databases
STRING	O46411.
Proteomic databases
PRIDE	O46411.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000017090; ENSBTAP00000017090; ENSBTAG00000012858.
GeneID	281951.
KEGG	bta:281951.
Organism-specific databases
CTD	22978.
Phylogenomic databases
eggNOG	maNOG04834.
GeneTree	ENSGT00550000074539.
HOVERGEN	HBG000025.
InParanoid	O46411.
OMA	WERVFRA.
OrthoDB	EOG4MGS72.
PhylomeDB	O46411.
Family and domain databases
InterPro	IPR023214. HAD-like_dom. IPR008380. HAD-SF_hydro_IG_5-nucl. IPR016695. Pur_nucleotidase. [Graphical view]
KO	K01081.
PANTHER	PTHR12103. HAD-SF_hydro_IG_5-nucl. 1 hit.
Pfam	PF05761. 5_nucleotid. 1 hit. [Graphical view]
PIRSF	PIRSF017434. Purine_5'-nucleotidase. 1 hit.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR02244. HAD-IG-Ncltidse. 1 hit.
ProtoNet	Search...

Entry information

Entry name

5NTC_BOVIN

Accession

Primary (citable) accession number: O46411

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	June 1, 1998
Last modified:	November 16, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program