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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,P(4)-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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-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-RKQ9U2M7.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271Y → A: No Effect on substrate binding or catalytic activity. 1 Publication
Mutagenesisi27 – 271Y → D: Slight increase in substrate binding and no effect on catalytic activity. 1 Publication
Mutagenesisi31 – 311H → A: Increases substrate binding and reduces catalytic activity. 1 Publication
Mutagenesisi31 – 311H → V: Increases substrate binding and reduces catalytic activity. 1 Publication
Mutagenesisi36 – 361K → M: No effect on substrate binding and reduces catalytic activity. 1 Publication
Mutagenesisi38 – 381H → G: Slight decrease in substrate binding and slight increase in catalytic activity. 1 Publication
Mutagenesisi38 – 381H → K: Slight decrease in substrate binding and slight increase in catalytic activity. 1 Publication
Mutagenesisi52 – 521E → Q: No effect on substrate binding and strongly reduces catalytic activity. 1 Publication
Mutagenesisi56 – 561E → Q: No effect on substrate binding and strongly reduces catalytic activity. 1 Publication
Mutagenesisi76 – 761Y → A: Increases substrate binding and slightly reduces catalytic activity. Reduces catalytic activity; when associated with A-121. 1 Publication
Mutagenesisi79 – 791K → M: Slight increase in substrate binding and reduces catalytic activity. 1 Publication
Mutagenesisi81 – 811K → M: Slight increase in substrate binding and enzyme activity. 1 Publication
Mutagenesisi83 – 831K → M: Increases substrate binding and reduces catalytic activity. 1 Publication
Mutagenesisi103 – 1031E → Q: No effect on substrate binding and reduces catalytic activity. 1 Publication
Mutagenesisi121 – 1211Y → A: Increases substrate binding and slightly reduces catalytic activity. Reduces catalytic activity; when associated with A-76. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 138138Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]PRO_0000057106Add
BLAST

Proteomic databases

EPDiQ9U2M7.
PaxDbiQ9U2M7.

Expressioni

Gene expression databases

BgeeiWBGene00003581.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

1
138
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1412Combined sources
Beta strandi17 – 2711Combined sources
Beta strandi32 – 387Combined sources
Helixi45 – 5713Combined sources
Helixi61 – 633Combined sources
Beta strandi64 – 7815Combined sources
Beta strandi81 – 9212Combined sources
Beta strandi104 – 1107Combined sources
Helixi112 – 1198Combined sources
Helixi122 – 13716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KT9X-ray1.98A1-138[»]
1KTGX-ray1.80A/B1-138[»]
ProteinModelPortaliQ9U2M7.
SMRiQ9U2M7. Positions 2-138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9U2M7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 132132Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 5822Nudix boxAdd
BLAST

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
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

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

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01405. TETRPHPHTASE.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KT9X-ray1.98A1-138[»]
1KTGX-ray1.80A/B1-138[»]
ProteinModelPortaliQ9U2M7.
SMRiQ9U2M7. Positions 2-138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiQ9U2M7.
PaxDbiQ9U2M7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi189639.
WormBaseiY37H9A.6; CE20230; WBGene00003581; ndx-4.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.6.1.17. 1045.
ReactomeiR-CEL-3299685. Detoxification of Reactive Oxygen Species.
SABIO-RKQ9U2M7.

Miscellaneous databases

EvolutionaryTraceiQ9U2M7.
PROiQ9U2M7.

Gene expression databases

BgeeiWBGene00003581.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01405. TETRPHPHTASE.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAP4A_CAEEL
AccessioniPrimary (citable) accession number: Q9U2M7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 106 of the entry and version 1 of the sequence. [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

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.