[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; PubMed=1856684 [NCBI, ExPASy, EBI, Israel, Japan] Fabiny J.M., Jayakumar A., Chinault A.C., Barnes E.M. Jr.; "Ammonium transport in Escherichia coli: localization and nucleotide sequence of the amtA gene."; J. Gen. Microbiol. 137:983-989(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1729235 [NCBI, ExPASy, EBI, Israel, Japan] Neuwald A.F., Krishnan B.R., Brikun I., Kulakauskas S., Suziedelis K., Tomcsanyi T., Leyh T.S., Berg D.E.; "cysQ, a gene needed for cysteine synthesis in Escherichia coli K-12 only during aerobic growth."; J. Bacteriol. 174:415-425(1992).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan] Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."; Nucleic Acids Res. 23:2105-2119(1995).
[4]	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).
[5]	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).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98. STRAIN=K12; PubMed=2172762 [NCBI, ExPASy, EBI, Israel, Japan] Liu J., Beacham I.R.; "Transcription and regulation of the cpdB gene in Escherichia coli K12 and Salmonella typhimurium LT2: evidence for modulation of constitutive promoters by cyclic AMP-CRP complex."; Mol. Gen. Genet. 222:161-165(1990).
[7]	FUNCTION. DOI=10.1074/jbc.270.49.29105; PubMed=7493934 [NCBI, ExPASy, EBI, Israel, Japan] Peng Z., Verma D.P.S.; "A rice HAL2-like gene encodes a Ca(2+)-sensitive 3'(2'),5'-diphosphonucleoside 3'(2')-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations."; J. Biol. Chem. 270:29105-29110(1995).
[8]	CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. DOI=10.1074/jbc.274.19.13619; PubMed=10224133 [NCBI, ExPASy, EBI, Israel, Japan] Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.; "Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate."; J. Biol. Chem. 274:13619-13628(1999).
[9]	FUNCTION, COFACTOR, AND ENZYME REGULATION. DOI=10.1093/nar/gkl247; PubMed=16682444 [NCBI, ExPASy, EBI, Israel, Japan] Mechold U., Ogryzko V., Ngo S., Danchin A.; "Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells."; Nucleic Acids Res. 34:2364-2373(2006).

Comments

FUNCTION: Converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP. May also convert adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS). Has 10000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2).
CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H₂O = adenosine 5'-phosphate + phosphate.
COFACTOR: Magnesium (Probable).
ENZYME REGULATION: Inhibited by lithium and calcium.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=1.1 µM for PAP;
K_M=1.2 mM for Ins(1,4)P2;
SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (Probable).
INDUCTION: Strongly repressed during nitrogen excess.
SIMILARITY: Belongs to the inositol monophosphatase family.
CAUTION: Was originally (PubMed:1856684) thought to be an ammonium transport protein.

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

M55170; AAA23444.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M80795; AAA23657.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97110.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77171.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78215.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X54008; CAA37953.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S56439; S56439.

RefSeq

AP_004714.1; -.
NP_418635.1; -.

3D structure databases

HSSP

P32179; 1KA1. [HSSP ENTRY / PDB]

ModBase

P22255.

Protein-protein interaction databases

DIP

DIP:9385N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10043-MON; -.

Organism-specific databases

EchoBASE

EB0041; -.

EcoGene

EG10043; cysQ.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008441;	Molecular function: 3'(2'),5'-bisphosphate nucleotidase activity (inferred from electronic annotation from EC).
GO:0004437;	Molecular function: inositol or phosphatidylinositol phosphatase activity (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006240; Bisphos_bac.
IPR000760; Inositol_P.
Graphical view of domain structure.

PANTHER

PTHR20854; Inositol_P; 1.

Pfam

PF00459; Inositol_P; 1.
Pfam graphical view of domain structure.

PRINTS

PR00378; INOSPHPHTASE.

ProDom

PD023420; Inositol_P; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01331; bisphos_cysQ; 1.

PROSITE

PS00629; IMP_1; 1.
PS00630; IMP_2; 1.

ProtoNet

P22255.

Genome annotation databases

GeneID

948728; -.

GenomeReviews

U00096_GR; b4214.
AP009048_GR; JW4172.

KEGG

ecj:JW4172; -.
eco:b4214; -.

Phylogenomic databases

HOGENOM

P22255; -.

Genome annotation databases

CMR

P22255; b4214.

Other

UniRef

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

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Membrane; Metal-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 246`	`246`	`3'(2'),5'-bisphosphate nucleotidase cysQ.`	`PRO_0000142541`
`METAL`	`64 64`		`Magnesium 1 (By similarity).`
`METAL`	`83 83`		`Magnesium 1 (By similarity).`
`METAL`	`83 83`		`Magnesium 2 (By similarity).`
`METAL`	`85 85`		`Magnesium 1; via carbonyl oxygen (By similarity).`
`METAL`	`86 86`		`Magnesium 2 (By similarity).`
`METAL`	`205 205`		`Magnesium 2 (By similarity).`
`CONFLICT`	`193 194`		`QL -> HV (in Ref. 1 and 2).`

Sequence information

Length: 246 AA [This is the length of the unprocessed precursor]

Molecular weight: 27176 Da [This is the MW of the unprocessed precursor]

CRC64: F0CBDFAA98DDAF85 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLDQVCQLAR NAGDAIMQVY DGTKPMDVVS KADNSPVTAA DIAAHTVIMD GLRTLTPDVP 

        70         80         90        100        110        120 
VLSEEDPPGW EVRQHWQRYW LVDPLDGTKE FIKRNGEFTV NIALIDHGKP ILGVVYAPVM 

       130        140        150        160        170        180 
NVMYSAAEGK AWKEECGVRK QIQVRDARPP LVVISRSHAD AELKEYLQQL GEHQTTSIGS 

       190        200        210        220        230        240 
SLKFCLVAEG QAQLYPRFGP TNIWDTAAGH AVAAAAGAHV HDWQGKPLDY TPRESFLNPG 


FRVSIY

P22255 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