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Q5RCY2 (NUDT5_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-sugar pyrophosphatase

EC=3.6.1.-
EC=3.6.1.13
Alternative name(s):
Nucleoside diphosphate-linked moiety X motif 5
Short name=Nudix motif 5
Gene names
Name:NUDT5
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes with similar activities ADP-ribose, ADP-mannose, and ADP-glucose. Can also hydrolyze other nucleotide sugars with low activity By similarity.

Catalytic activity

ADP-ribose + H2O = AMP + D-ribose 5-phosphate.

ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate.

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the Nudix hydrolase family.

Contains 1 nudix hydrolase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216ADP-sugar pyrophosphatase
PRO_0000250702

Regions

Domain57 – 194138Nudix hydrolase
Region46 – 472Substrate binding; shared with dimeric partner By similarity
Motif97 – 11822Nudix box

Sites

Metal binding961Magnesium 1; via carbonyl oxygen By similarity
Metal binding1121Magnesium 2 By similarity
Metal binding1121Magnesium 3 By similarity
Metal binding1161Magnesium 1 By similarity
Metal binding1161Magnesium 3 By similarity
Metal binding1631Magnesium 3 By similarity
Binding site281Substrate By similarity
Binding site511Substrate; shared with dimeric partner By similarity
Binding site841Substrate By similarity
Binding site981Substrate; via amide nitrogen By similarity
Binding site1331Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue91Phosphoserine By similarity
Modified residue101Phosphoserine By similarity
Modified residue421N6-acetyllysine By similarity
Modified residue741Phosphotyrosine By similarity
Modified residue2071N6-acetyllysine By similarity
Modified residue2151N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RCY2 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 9C88CC433D3CC3A9

FASTA21624,070
        10         20         30         40         50         60 
MESQEPTESS QNGKQYIISE ELISEGKWVK LEKTTYMDPT GKTRTWESVK RTTRKEQTAD 

        70         80         90        100        110        120 
GVAVIPVLQR TLHYECIVLV KQFRPPMGGY CIEFPAGLID DGETPEAAAL RELEEETGYK 

       130        140        150        160        170        180 
GDVAECSPAV CMDPGLSNCT VHIVTVTING DDAENARPKP KPEFVEVISL PKNDLLQRLD 

       190        200        210 
ALVAEEHLTV DARVYSYALA LKHANAKPFE VPFLKF 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858136 mRNA. Translation: CAH90375.1.
RefSeqNP_001125182.1. NM_001131710.1.
UniGenePab.13961.

3D structure databases

ProteinModelPortalQ5RCY2.
SMRQ5RCY2. Positions 14-216.
ModBaseSearch...

Proteomic databases

PRIDEQ5RCY2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000002500; ENSPPYP00000002426; ENSPPYG00000002091.
GeneID100172071.
KEGGpon:100172071.

Organism-specific databases

CTD11164.

Phylogenomic databases

HOVERGENHBG052691.

Family and domain databases

InterProIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
Gene3DG3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KOK13987.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSPR00502. NUDIXFAMILY.
SUPFAMSSF55811. NUDIX_hydrolase. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUDT5_PONAB
AccessionPrimary (citable) accession number: Q5RCY2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families