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

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Q9U2M7 (AP4A_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	ndx-4
ORF Names:	Y37H9A.6

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	138 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Ref.1
Catalytic activity	P₁,P(4)-bis(5'-adenosyl) tetraphosphate + H₂O = ATP + AMP.
Cofactor	Divalent ions. Magnesium, cobalt, manganese, zinc or calcium. Ref.1
Subunit structure	Monomer. Ref.4
Domain	Mutagenesis suggests that interactions with P1- and P4-phosphate are minimum indicating the enzyme may have a wide substrate range.
Sequence similarities	Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Ligand	ATP-binding Calcium Cobalt Magnesium Manganese Nucleotide-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	induction of apoptosis Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 138

138

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

PRO_0000057106

Regions

Domain

1 – 132

132

Nudix hydrolase

Motif

37 – 58

Nudix box

Experimental info

Mutagenesis

Y → A: No Effect on substrate binding or catalytic activity.

Mutagenesis

Y → D: Slight increase in substrate binding and no effect on catalytic activity.

Mutagenesis

H → A: Increases substrate binding and reduces catalytic activity.

Mutagenesis

H → V: Increases substrate binding and reduces catalytic activity.

Mutagenesis

K → M: No effect on substrate binding and reduces catalytic activity.

Mutagenesis

H → G: Slight decrease in substrate binding and slight increase in catalytic activity.

Mutagenesis

H → K: Slight decrease in substrate binding and slight increase in catalytic activity.

Mutagenesis

E → Q: No effect on substrate binding and strongly reduces catalytic activity.

Mutagenesis

E → Q: No effect on substrate binding and strongly reduces catalytic activity.

Mutagenesis

Y → A: Increases substrate binding and slightly reduces catalytic activity. Reduces catalytic activity; when associated with A-121.

Mutagenesis

K → M: Slight increase in substrate binding and reduces catalytic activity.

Mutagenesis

K → M: Slight increase in substrate binding and enzyme activity.

Mutagenesis

K → M: Increases substrate binding and reduces catalytic activity.

Mutagenesis

103

E → Q: No effect on substrate binding and reduces catalytic activity.

Mutagenesis

121

Y → A: Increases substrate binding and slightly reduces catalytic activity. Reduces catalytic activity; when associated with A-76.

Secondary structure

138

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9U2M7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5C123085602CE5E5
Show »

FASTA

138

15,889

        10         20         30         40         50         60 
MVVKAAGLVI YRKLAGKIEF LLLQASYPPH HWTPPKGHVD PGEDEWQAAI RETKEEANIT 

        70         80         90        100        110        120 
KEQLTIHEDC HETLFYEAKG KPKSVKYWLA KLNNPDDVQL SHEHQNWKWC ELEDAIKIAD 

       130 
YAEMGSLLRK FSAFLAGF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, characterisation and crystallisation of a diadenosine 5',5''-P(1),P(4)-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans." Abdelghany H.M., Gasmi L., Cartwright J.L., Bailey S., Rafferty J.B., McLennan A.G. Biochim. Biophys. Acta 1550:27-36(2001) [PubMed: 11738085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, COFACTOR. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Analysis of the catalytic and binding residues of the diadenosine tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans by site-directed mutagenesis." Abdelghany H.M., Bailey S., Blackburn G.M., Rafferty J.B., McLennan A.G. J. Biol. Chem. 278:4435-4439(2003) [PubMed: 12475970] [Abstract] Cited for: MUTAGENESIS. Strain: Bristol N2.
[4]	"The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms." Bailey S., Sedelnikova S.E., Blackburn G.M., Abdelghany H.M., Baker P.J., McLennan A.G., Rafferty J.B. Structure 10:589-600(2002) [PubMed: 11937063] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT.
[5]	"Crystallization of a complex of Caenorhabditis elegans diadenosine tetraphosphate hydrolase and a non-hydrolysable substrate analogue, AppCH2ppA." Bailey S., Sedelnikova S.E., Blackburn G.M., Abdelghany H.M., McLennan A.G., Rafferty J.B. Acta Crystallogr. D 58:526-528(2002) [PubMed: 11856844] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL032625 Genomic DNA. Translation: CAB63351.1.

RefSeq

NP_493413.1. NM_061012.3.

UniGene

Cel.16496.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KT9	X-ray	1.98	A	1-138	[»]
1KTG	X-ray	1.80	A/B	1-138	[»]

ProteinModelPortal

Q9U2M7.

SMR

Q9U2M7. Positions 2-138.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24985N.

MINT

MINT-1125473.

STRING

Q9U2M7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

Y37H9A.6.1; Y37H9A.6.1; Y37H9A.6.
Y37H9A.6.2; Y37H9A.6.2; Y37H9A.6.

GeneID

189639.

KEGG

cel:Y37H9A.6.

UCSC

Y37H9A.6.2. c. elegans.

Organism-specific databases

CTD

189639.

WormBase

Y37H9A.6; CE20230; WBGene00003581; ndx-4.

Phylogenomic databases

eggNOG

meNOG18840.

GeneTree

EMGT00050000016984.

HOGENOM

HBG741910.

InParanoid

Q9U2M7.

OMA

RRRLIPK.

PhylomeDB

Q9U2M7.

Gene expression databases

ArrayExpress

Q9U2M7.

Family and domain databases

InterPro

IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]

Gene3D

G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.

K01518.

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

PRINTS

PR01405. TETRPHPHTASE.

SUPFAM

SSF55811. NUDIX_hydrolase. 1 hit.

PROSITE

PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

NextBio

943106.

Entry information

Entry name

AP4A_CAEEL

Accession

Primary (citable) accession number: Q9U2M7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	May 1, 2000
Last modified:	November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents