[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-29. STRAIN=K12; PubMed=2168385 [NCBI, ExPASy, EBI, Israel, Japan] Dassa J., Marck C., Boquet P.L.; "The complete nucleotide sequence of the Escherichia coli gene appA reveals significant homology between pH 2.5 acid phosphatase and glucose-1-phosphatase."; J. Bacteriol. 172:5497-5500(1990).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan] Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.; "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."; DNA Res. 3:137-155(1996).
[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]. 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]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112. DOI=10.1016/0300-9084(87)90045-9; PubMed=3038201 [NCBI, ExPASy, EBI, Israel, Japan] Touati E., Danchin A.; "The structure of the promoter and amino terminal region of the pH 2.5 acid phosphatase structural gene (appA) of E. coli: a negative control of transcription mediated by cyclic AMP."; Biochimie 69:215-221(1987).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17. STRAIN=K12; DOI=10.1007/BF00267454; PubMed=1658595 [NCBI, ExPASy, EBI, Israel, Japan] Dassa J., Fsihi H., Marck C., Dion M., Kieffer-Bontemps M., Boquet P.L.; "A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA)."; Mol. Gen. Genet. 229:341-352(1991).
[7]	CHARACTERIZATION, AND PROTEIN SEQUENCE OF 23-34. Greiner R., Jany K.-D.; "Characterization of a phytase from Escherichia coli."; Biol. Chem. Hoppe-Seyler 372:664-665(1991).
[8]	CHARACTERIZATION, AND PROTEIN SEQUENCE OF 23-35. DOI=10.1006/abbi.1993.1261; PubMed=8387749 [NCBI, ExPASy, EBI, Israel, Japan] Greiner R., Konietzny U., Jany K.-D.; "Purification and characterization of two phytases from Escherichia coli."; Arch. Biochem. Biophys. 303:107-113(1993).
[9]	CHARACTERIZATION. DOI=10.1139/cjm-46-1-59; PubMed=10696472 [NCBI, ExPASy, EBI, Israel, Japan] Golovan S., Wang G., Zhang J., Forsberg C.W.; "Characterization and overproduction of the Escherichia coli appA encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities."; Can. J. Microbiol. 46:59-71(2000).
[10]	MUTAGENESIS. PubMed=1429631 [NCBI, ExPASy, EBI, Israel, Japan] Ostanin K., Harms E.H., Stevis P.E., Kuciel R., Zhou M.-M., van Etten R.L.; "Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase."; J. Biol. Chem. 267:22830-22836(1992).
[11]	X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). DOI=10.1038/72371; PubMed=10655611 [NCBI, ExPASy, EBI, Israel, Japan] Lim D., Golovan S., Forsberg C.W., Jia Z.; "Crystal structures of Escherichia coli phytase and its complex with phytate."; Nat. Struct. Biol. 7:108-113(2000).

Comments

CATALYTIC ACTIVITY: A phosphate monoester + H₂O = an alcohol + phosphate.
CATALYTIC ACTIVITY: Myo-inositol hexakisphosphate + H₂O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Periplasm.
INDUCTION: In addition to cAMP-mediated control, this enzyme is induced when bacterial cultures reach stationary phase; its synthesis is triggered by phosphate starvation or a shift from aerobic to anaerobic conditions.
SIMILARITY: Belongs to the histidine acid phosphatase 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

M58708; AAA72086.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74065.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35745.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05471; CAA29031.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S63811; AAB20286.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B36733; B36733.

RefSeq

AP_001609.1; -.
NP_415500.1; -.

3D structure databases

PDB

1DKL; X-ray; 2.30 A; A/B=23-432.	[ExPASy / RCSB / EBI]
1DKM; X-ray; 2.25 A; A=23-432.	[ExPASy / RCSB / EBI]
1DKN; X-ray; 2.40 A; A=23-432.	[ExPASy / RCSB / EBI]
1DKO; X-ray; 2.38 A; A=23-432.	[ExPASy / RCSB / EBI]
1DKP; X-ray; 2.28 A; A=23-432.	[ExPASy / RCSB / EBI]
1DKQ; X-ray; 2.05 A; A=23-432.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DKL; -.
1DKM; -.
1DKN; -.
1DKO; -.
1DKP; -.
1DKQ; -.

ModBase

P07102.

Enzyme and pathway databases

BioCyc

EcoCyc:APPA-MON; -.
MetaCyc:APPA-MON; -.

2D gel databases

SWISS-2DPAGE

P07102; -.

Organism-specific databases

EchoBASE

EB0047; -.

EcoGene

EG10049; appA.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0008707;	Molecular function: 4-phytase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR000560; Histidine_acid_Pase.
Graphical view of domain structure.

Pfam

PF00328; Acid_phosphat_A; 1.
Pfam graphical view of domain structure.

PROSITE

PS00616; HIS_ACID_PHOSPHAT_1; 1.
PS00778; HIS_ACID_PHOSPHAT_2; 1.

Genome annotation databases

GeneID

946206; -.

GenomeReviews

U00096_GR; b0980.
AP009048_GR; JW0963.

KEGG

ecj:JW0963; -.
eco:b0980; -.

Phylogenomic databases

HOGENOM

P07102; -.

Other

LinkHub

P07102; -.

Genome annotation databases

CMR

P07102; b0980.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; Multifunctional enzyme; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`
`CHAIN`	`23 432`	`410`	`Periplasmic appA protein.`	`PRO_0000023947`
`ACT_SITE`	`39 39`		`Nucleophile.`
`ACT_SITE`	`326 326`		`Proton donor.`
`DISULFID`	`99 130`
`DISULFID`	`155 430`
`DISULFID`	`200 210`
`DISULFID`	`404 413`
`CONFLICT`	`51 66`		`MQDVTPDAWPTWPVKL -> NAGCHPRRMANLAGKT (in Ref. 5; CAA29031).`
`CONFLICT`	`75 76`		`EL -> DV (in Ref. 5; CAA29031).`
`CONFLICT`	`112 112`		`D -> S (in Ref. 5; CAA29031).`
`STRAND`	`28 38`	`11`
`HELIX`	`49 53`	`5`
`HELIX`	`71 90`	`20`
`STRAND`	`96 98`	`3`
`TURN`	`102 104`	`3`
`STRAND`	`105 109`	`5`
`HELIX`	`113 126`	`14`
`HELIX`	`145 147`	`3`
`TURN`	`149 153`	`5`
`HELIX`	`159 169`	`11`
`HELIX`	`174 179`	`6`
`HELIX`	`182 192`	`11`
`HELIX`	`194 196`	`3`
`HELIX`	`198 201`	`4`
`HELIX`	`212 215`	`4`
`STRAND`	`220 223`	`4`
`STRAND`	`226 229`	`4`
`HELIX`	`231 249`	`19`
`HELIX`	`254 257`	`4`
`HELIX`	`262 279`	`18`
`HELIX`	`283 301`	`19`
`HELIX`	`310 312`	`3`
`STRAND`	`314 316`	`3`
`STRAND`	`318 324`	`7`
`HELIX`	`326 336`	`11`
`STRAND`	`354 362`	`9`
`TURN`	`363 365`	`3`
`STRAND`	`368 376`	`9`
`HELIX`	`379 383`	`5`
`STRAND`	`390 392`	`3`
`STRAND`	`395 398`	`4`
`HELIX`	`415 425`	`11`
`HELIX`	`428 430`	`3`

Sequence information

Length: 432 AA [This is the length of the unprocessed precursor]

Molecular weight: 47057 Da [This is the MW of the unprocessed precursor]

CRC64: 6510C6C579177F11 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAILIPFLS LLIPLTPQSA FAQSEPELKL ESVVIVSRHG VRAPTKATQL MQDVTPDAWP 

        70         80         90        100        110        120 
TWPVKLGWLT PRGGELIAYL GHYQRQRLVA DGLLAKKGCP QSGQVAIIAD VDERTRKTGE 

       130        140        150        160        170        180 
AFAAGLAPDC AITVHTQADT SSPDPLFNPL KTGVCQLDNA NVTDAILSRA GGSIADFTGH 

       190        200        210        220        230        240 
RQTAFRELER VLNFPQSNLC LKREKQDESC SLTQALPSEL KVSADNVSLT GAVSLASMLT 

       250        260        270        280        290        300 
EIFLLQQAQG MPEPGWGRIT DSHQWNTLLS LHNAQFYLLQ RTPEVARSRA TPLLDLIKTA 

       310        320        330        340        350        360 
LTPHPPQKQA YGVTLPTSVL FIAGHDTNLA NLGGALELNW TLPGQPDNTP PGGELVFERW 

       370        380        390        400        410        420 
RRLSDNSQWI QVSLVFQTLQ QMRDKTPLSL NTPPGEVKLT LAGCEERNAQ GMCSLAGFTQ 

       430 
IVNEARIPAC SL

P07102 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools