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

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P05637 (APAH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

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

Documents (2) |

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 [symmetrical]
EC=3.6.1.41

Alternative name(s):
Ap4A hydrolase
Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase
Diadenosine tetraphosphatase

Gene names

Name:	apaH
Ordered Locus Names:	b0049, JW0048

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. Ref.5
Catalytic activity	P₁,P(4)-bis(5'-adenosyl) tetraphosphate + H₂O = 2 ADP. Ref.5
Enzyme regulation	Co²⁺ is a strong stimulator (100-fold increase in rate of hydrolysis). Mn²⁺, Cd²⁺, Ni²⁺, Mg²⁺ and Ca²⁺ are weak stimulators; the two latter act synergistically with Co²⁺. Ref.5
Subunit structure	Monomer. Ref.5
Sequence similarities	Belongs to the Ap4A hydrolase family.

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleobase-containing small molecule interconversion Inferred from mutant phenotype PubMed 2995325. Source: EcoliWiki
Molecular_function	bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity Inferred from direct assay Ref.5. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 280

280

Bis(5'-nucleosyl)-tetraphosphatase [symmetrical] HAMAP-Rule MF_00199

PRO_0000197988

Experimental info

Sequence conflict

K → L in CAA28416. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P05637 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: BD6560C73446C1BB
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FASTA

280

31,297

        10         20         30         40         50         60 
MATYLIGDVH GCYDELIALL HKVEFTPGKD TLWLTGDLVA RGPGSLDVLR YVKSLGDSVR 

        70         80         90        100        110        120 
LVLGNHDLHL LAVFAGISRN KPKDRLTPLL EAPDADELLN WLRRQPLLQI DEEKKLVMAH 

       130        140        150        160        170        180 
AGITPQWDLQ TAKECARDVE AVLSSDSYPF FLDAMYGDMP NNWSPELRGL GRLRFITNAF 

       190        200        210        220        230        240 
TRMRFCFPNG QLDMYSKESP EEAPAPLKPW FAIPGPVAEE YSIAFGHWAS LEGKGTPEGI 

       250        260        270        280 
YALDTGCCWG GTLTCLRWED KQYFVQPSNR HKDLGEAAAS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene for Escherichia coli diadenosine tetraphosphatase is located immediately clockwise to folA and forms an operon with ksgA." Blanchin-Roland S., Blanquet S., Schmitter J.-M., Fayat G. Mol. Gen. Genet. 205:515-522(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 83 AND 275. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Catabolism of diadenosine 5',5''-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5',5''-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12." Guranowski A., Jakubowski H., Holler E. J. Biol. Chem. 258:14784-14789(1983) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT. Strain: K12.
[6]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04711 Genomic DNA. Translation: CAA28416.1. U00096 Genomic DNA. Translation: AAC73160.1. AP009048 Genomic DNA. Translation: BAB96617.2.
PIR	A64726.
RefSeq	NP_414591.1. NC_000913.2. YP_488355.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P05637.
SMR	P05637. Positions 2-268.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9113N.
IntAct	P05637. 2 interactions.
STRING	511145.b0049.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73160; AAC73160; b0049. BAB96617; BAB96617; BAB96617.
GeneID	12933211. 944770.
KEGG	ecj:Y75_p0049. eco:b0049.
PATRIC	32115197. VBIEscCol129921_0050.
Organism-specific databases
EchoBASE	EB0046.
EcoGene	EG10048. apaH.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000251871.
KO	K01525.
OMA	WLRHQPL.
ProtClustDB	PRK00166.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10048-MONOMER. ECOL316407:JW0048-MONOMER. MetaCyc:EG10048-MONOMER.
Gene expression databases
Genevestigator	P05637.
Family and domain databases
HAMAP	MF_00199. ApaH.
InterPro	IPR004617. ApaH. IPR004843. Metallo_PEstase_dom. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PIRSF	PIRSF000903. B5n-ttraPtase_sm. 1 hit.
TIGRFAMs	TIGR00668. apaH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

APAH_ECOLI

Accession

Primary (citable) accession number: P05637
Secondary accession number(s): P78039

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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

Experimental info

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents