P05637 (APAH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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)

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. HAMAP MF_00199
Catalytic activity	P1,P(4)-bis(5'-adenosyl) tetraphosphate + H2O = 2 ADP. HAMAP MF_00199
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+. HAMAP MF_00199
Subunit structure	Monomer.
Sequence similarities	Belongs to the Ap4A hydrolase family.

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity Inferred from electronic annotation. Source: EC
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 MF_00199		PRO_0000197988
Experimental info
	Sequence conflict	83	1	K → L in CAA28416. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P05637 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: BD6560C73446C1BB	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

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: 3031429] [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: 1630901] [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: 9278503] [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: 16738553] [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: 6317672] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.

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.
3D structure databases
ProteinModelPortal	P05637.
SMR	P05637. Positions 2-268.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9113N.
IntAct	P05637. 2 interactions.
2D gel databases
ECO2DBASE	C031.3. 6TH EDITION.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004303; EBESCP00000004303; EBESCG00000003508. EBESCT00000004304; EBESCP00000004304; EBESCG00000003508. EBESCT00000004305; EBESCP00000004305; EBESCG00000003508. EBESCT00000004306; EBESCP00000004306; EBESCG00000003508. EBESCT00000017189; EBESCP00000016480; EBESCG00000016248.
GeneID	944770.
GenomeReviews	Gene locus JW0048 in contig AP009048_GR. Gene locus b0049 in contig U00096_GR.
KEGG	ecj:JW0048. eco:b0049.
PATRIC	32115197. VBIEscCol129921_0050.
Organism-specific databases
EchoBASE	EB0046.
EcoGene	EG10048. apaH.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	EBGT00050000010576.
HOGENOM	HBG724457.
OMA	LVFGHWA.
PhylomeDB	P05637.
ProtClustDB	PRK00166.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10048-MONOMER. MetaCyc:EG10048-MONOMER.
Gene expression databases
Genevestigator	P05637.
Family and domain databases
HAMAP	MF_00199. ApaH. [Tree]
InterPro	IPR004617. ApaH. IPR004843. Metallo_PEstase_dom. [Graphical view]
KO	K01525.
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:	January 25, 2012
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program