Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]

Gene

ndx-4

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Asymmetrically hydrolyzes Ap4A to yield AMP and ATP.1 Publication

Catalytic activityi

P1,P4-bis(5'-adenosyl) tetraphosphate + H2O = ATP + AMP.

Cofactori

Mg2+1 Publication, Co2+1 Publication, Mn2+1 Publication, Zn2+1 Publication, Ca2+1 PublicationNote: Divalent metal ions. Mg2+, Co2+, Mn2+, Zn2+ or Ca2+.1 Publication

GO - Molecular functioni

  • 5-phosphoribosyl 1-pyrophosphate pyrophosphatase activity Source: WormBase
  • ATP binding Source: UniProtKB-KW
  • bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Source: UniProtKB

GO - Biological processi

  • ADP biosynthetic process Source: WormBase
  • AMP biosynthetic process Source: WormBase
  • apoptotic process Source: UniProtKB
  • ATP biosynthetic process Source: WormBase
  • diadenosine tetraphosphate catabolic process Source: WormBase
  • ribose phosphate metabolic process Source: WormBase

Keywordsi

Molecular functionHydrolase
LigandATP-binding, Calcium, Cobalt, Magnesium, Manganese, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi3.6.1.17. 1045.
ReactomeiR-CEL-3299685. Detoxification of Reactive Oxygen Species.
SABIO-RKiQ9U2M7.

Names & Taxonomyi

Protein namesi
Recommended name:
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (EC:3.6.1.-)
Alternative name(s):
Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
Short name:
Ap4A hydrolase
Short name:
Ap4Aase
Short name:
Diadenosine tetraphosphatase
Nudix hydrolase 4
Gene namesi
Name:ndx-4
ORF Names:Y37H9A.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiY37H9A.6; CE20230; WBGene00003581; ndx-4.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27Y → A: No Effect on substrate binding or catalytic activity. 1 Publication1
Mutagenesisi27Y → D: Slight increase in substrate binding and no effect on catalytic activity. 1 Publication1
Mutagenesisi31H → A: Increases substrate binding and reduces catalytic activity. 1 Publication1
Mutagenesisi31H → V: Increases substrate binding and reduces catalytic activity. 1 Publication1
Mutagenesisi36K → M: No effect on substrate binding and reduces catalytic activity. 1 Publication1
Mutagenesisi38H → G: Slight decrease in substrate binding and slight increase in catalytic activity. 1 Publication1
Mutagenesisi38H → K: Slight decrease in substrate binding and slight increase in catalytic activity. 1 Publication1
Mutagenesisi52E → Q: No effect on substrate binding and strongly reduces catalytic activity. 1 Publication1
Mutagenesisi56E → Q: No effect on substrate binding and strongly reduces catalytic activity. 1 Publication1
Mutagenesisi76Y → A: Increases substrate binding and slightly reduces catalytic activity. Reduces catalytic activity; when associated with A-121. 1 Publication1
Mutagenesisi79K → M: Slight increase in substrate binding and reduces catalytic activity. 1 Publication1
Mutagenesisi81K → M: Slight increase in substrate binding and enzyme activity. 1 Publication1
Mutagenesisi83K → M: Increases substrate binding and reduces catalytic activity. 1 Publication1
Mutagenesisi103E → Q: No effect on substrate binding and reduces catalytic activity. 1 Publication1
Mutagenesisi121Y → A: Increases substrate binding and slightly reduces catalytic activity. Reduces catalytic activity; when associated with A-76. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000571061 – 138Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]Add BLAST138

Proteomic databases

EPDiQ9U2M7.
PaxDbiQ9U2M7.
PeptideAtlasiQ9U2M7.
PRIDEiQ9U2M7.

Expressioni

Gene expression databases

BgeeiWBGene00003581.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi54272. 1 interactor.
DIPiDIP-24985N.
MINTiMINT-1125473.
STRINGi6239.Y37H9A.6.1.

Structurei

Secondary structure

1138
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 14Combined sources12
Beta strandi17 – 27Combined sources11
Beta strandi32 – 38Combined sources7
Helixi45 – 57Combined sources13
Helixi61 – 63Combined sources3
Beta strandi64 – 78Combined sources15
Beta strandi81 – 92Combined sources12
Beta strandi104 – 110Combined sources7
Helixi112 – 119Combined sources8
Helixi122 – 137Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KT9X-ray1.98A1-138[»]
1KTGX-ray1.80A/B1-138[»]
ProteinModelPortaliQ9U2M7.
SMRiQ9U2M7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9U2M7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 132Nudix hydrolasePROSITE-ProRule annotationAdd BLAST132

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi37 – 58Nudix boxAdd BLAST22

Domaini

Mutagenesis suggests that interactions with P1- and P4-phosphate are minimum indicating the enzyme may have a wide substrate range.

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated

Phylogenomic databases

eggNOGiKOG2839. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000002416.
HOGENOMiHOG000261976.
InParanoidiQ9U2M7.
KOiK01518.
OMAiLFRDTRG.
OrthoDBiEOG091G0S47.
PhylomeDBiQ9U2M7.

Family and domain databases

InterProiView protein in InterPro
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
PfamiView protein in Pfam
PF00293. NUDIX. 1 hit.
PRINTSiPR01405. TETRPHPHTASE.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiView protein in PROSITE
PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9U2M7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVKAAGLVI YRKLAGKIEF LLLQASYPPH HWTPPKGHVD PGEDEWQAAI
60 70 80 90 100
RETKEEANIT KEQLTIHEDC HETLFYEAKG KPKSVKYWLA KLNNPDDVQL
110 120 130
SHEHQNWKWC ELEDAIKIAD YAEMGSLLRK FSAFLAGF
Length:138
Mass (Da):15,889
Last modified:May 1, 2000 - v1
Checksum:i5C123085602CE5E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL032625 Genomic DNA. Translation: CAB63351.1.
RefSeqiNP_493413.1. NM_061012.4.
UniGeneiCel.16496.

Genome annotation databases

EnsemblMetazoaiY37H9A.6; Y37H9A.6; WBGene00003581.
GeneIDi189639.
KEGGicel:CELE_Y37H9A.6.
UCSCiY37H9A.6.2. c. elegans.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiAP4A_CAEEL
AccessioniPrimary (citable) accession number: Q9U2M7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: May 1, 2000
Last modified: June 7, 2017
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families