ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05637

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name APAH_ECOLI
Primary accession number P05637
Secondary accession number P78039
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 80)
Name and origin of the protein
Protein name Bis(5'-nucleosyl)-tetraphosphatase [symmetrical]
Synonyms EC 3.6.1.41
Diadenosine tetraphosphatase
Ap4A hydrolase
Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase
Gene name
Name: apaH
OrderedLocusNames: b0049, JW0048
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00338091; PubMed=3031429 [NCBI, ExPASy, EBI, Israel, Japan]
Blanchin-Roland S., Blanquet S., Schmitter J.-M., Fayat G.;
"The gene for Escherichia coli diadenosine tetraphosphatase is located immediately clockwise to folA and forms an operon with ksgA.";
Mol. Gen. Genet. 205:515-522(1986).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/20.13.3305; PubMed=1630901 [NCBI, ExPASy, EBI, Israel, Japan]
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 83 AND 275.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
 CHARACTERIZATION.
STRAIN=K12;
PubMed=6317672 [NCBI, ExPASy, EBI, Israel, Japan]
Guranowski A., Jakubowski H., Holler E.;
"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.";
J. Biol. Chem. 258:14784-14789(1983).
Comments
  • FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
  • CATALYTIC ACTIVITY: P1,P4-bis(5'-adenosyl) tetraphosphate + H2O = 2 ADP.
  • ENZYME REGULATION: Co(2+) is a strong stimulator (100-fold increase in rate of hydrolysis). Mn(2+), Cd(2+), Ni(2+), Mg(2+) and Ca(2+) are weak stimulators; the two latter act synergistically with Co(2+).
  • SUBUNIT: Monomer.
  • SIMILARITY: Belongs to the Ap4A hydrolase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04711; CAA28416.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73160.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAB96617.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A64726; A64726.
RefSeq AP_000713.1; -.
NP_414591.1; -.
3D structure databases
SMR P05637; 2-268.
ModBase P05637.
Enzyme and pathway databases
BioCyc EcoCyc:EG10048-MON; -.
MetaCyc:EG10048-MON; -.
2D gel databases
ECO2DBASE C031.3; 6TH EDITION.
Organism-specific databases
EchoBASE EB0046; -.
EcoGene EG10048; apaH.
Ontologies
GO
GO:0008803; Molecular function: bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00199; -; 1.
PBIL [Tree]
InterPro IPR004617; ApaH.
IPR004843; M-pesterase.
Graphical view of domain structure.
Pfam PF00149; Metallophos; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000903; B5n-ttraPtase_sm; 1.
TIGRFAMs TIGR00668; apaH; 1.
BLOCKS P05637.
ProtoNet P05637.
Genome annotation databases
GeneID 944770; -.
GenomeReviews U00096_GR; b0049.
AP009048_GR; JW0048.
KEGG ecj:JW0048; -.
eco:b0049; -.
Phylogenomic databases
HOGENOM P05637; -.
Genome annotation databases
CMR P05637; b0049.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   280  280     Bis(5'-nucleosyl)-tetraphosphatase [symmetrical]. PRO_0000197988
CONFLICT   83    83        K -> L (in Ref. 1). 
Sequence information
Length: 280 AA [This is the length of the unprocessed precursor] Molecular weight: 31297 Da [This is the MW of the unprocessed precursor] CRC64: BD6560C73446C1BB [This is a checksum on the sequence] 
        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
P05637 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!