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P22255 (CYSQ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3'(2'),5'-bisphosphate nucleotidase CysQ

EC=3.1.3.7
Alternative name(s):
3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
3'-phosphoadenosine 5'-phosphate phosphatase
Short name=PAP phosphatase
DPNPase
Gene names
Name:cysQ
Synonyms:amtA
Ordered Locus Names:b4214, JW4172
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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). Ref.7 Ref.9

Catalytic activity

Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate. Ref.8

Cofactor

Magnesium Probable. Ref.9

Enzyme regulation

Inhibited by lithium and calcium. Ref.9

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Probable.

Induction

Strongly repressed during nitrogen excess. Ref.9

Sequence similarities

Belongs to the inositol monophosphatase family.

Caution

Was originally (Ref.1) thought to be an ammonium transport protein.

Biophysicochemical properties

Kinetic parameters:

KM=1.1 µM for PAP Ref.8

KM=1.2 mM for Ins(1,4)P2

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Cytoplasm
Membrane
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processsulfate assimilation

Inferred from mutant phenotype Ref.2. Source: EcoCyc

   Cellular componentcytoplasm

Inferred by curator. Source: EcoliWiki

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3'(2'),5'-bisphosphate nucleotidase activity

Inferred from direct assay Ref.9. Source: EcoCyc

magnesium ion binding

Inferred from direct assay Ref.9. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2462463'(2'),5'-bisphosphate nucleotidase CysQ
PRO_0000142541

Regions

Region85 – 884Substrate binding By similarity

Sites

Metal binding641Magnesium 1 By similarity
Metal binding831Magnesium 1 By similarity
Metal binding831Magnesium 2 By similarity
Metal binding851Magnesium 1; via carbonyl oxygen By similarity
Metal binding861Magnesium 2 By similarity
Metal binding2051Magnesium 2 By similarity
Binding site641Substrate By similarity
Binding site2051Substrate By similarity

Experimental info

Sequence conflict193 – 1942QL → HV Ref.1
Sequence conflict193 – 1942QL → HV Ref.2

Sequences

Sequence LengthMass (Da)Tools
P22255 [UniParc].

Last modified June 20, 2003. Version 2.
Checksum: F0CBDFAA98DDAF85

FASTA24627,176
        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 

« Hide

References

« Hide 'large scale' references
[1]"Ammonium transport in Escherichia coli: localization and nucleotide sequence of the amtA gene."
Fabiny J.M., Jayakumar A., Chinault A.C., Barnes E.M. Jr.
J. Gen. Microbiol. 137:983-989(1991) [PubMed: 1856684] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"cysQ, a gene needed for cysteine synthesis in Escherichia coli K-12 only during aerobic growth."
Neuwald A.F., Krishnan B.R., Brikun I., Kulakauskas S., Suziedelis K., Tomcsanyi T., Leyh T.S., Berg D.E.
J. Bacteriol. 174:415-425(1992) [PubMed: 1729235] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"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].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"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."
Liu J., Beacham I.R.
Mol. Gen. Genet. 222:161-165(1990) [PubMed: 2172762] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
Strain: K12.
[7]"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."
Peng Z., Verma D.P.S.
J. Biol. Chem. 270:29105-29110(1995) [PubMed: 7493934] [Abstract]
Cited for: FUNCTION.
[8]"Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate."
Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.
J. Biol. Chem. 274:13619-13628(1999) [PubMed: 10224133] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[9]"Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells."
Mechold U., Ogryzko V., Ngo S., Danchin A.
Nucleic Acids Res. 34:2364-2373(2006) [PubMed: 16682444] [Abstract]
Cited for: FUNCTION, COFACTOR, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55170 Genomic DNA. Translation: AAA23444.1.
M80795 Genomic DNA. Translation: AAA23657.1.
U14003 Genomic DNA. Translation: AAA97110.1.
U00096 Genomic DNA. Translation: AAC77171.1.
AP009048 Genomic DNA. Translation: BAE78215.1.
X54008 Genomic DNA. Translation: CAA37953.1.
PIRS56439.
RefSeqNP_418635.1. NC_000913.2.

3D structure databases

ProteinModelPortalP22255.
SMRP22255. Positions 2-244.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9385N.
IntActP22255. 6 interactions.
MINTMINT-1300047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000004948; EBESCP00000004948; EBESCG00000004039.
EBESCT00000015756; EBESCP00000015047; EBESCG00000014816.
GeneID948728.
GenomeReviewsGene locus JW4172 in contig AP009048_GR.
Gene locus b4214 in contig U00096_GR.
KEGGecj:JW4172.
eco:b4214.
PATRIC32124003. VBIEscCol129921_4346.

Organism-specific databases

EchoBASEEB0041.
EcoGeneEG10043. cysQ.

Phylogenomic databases

eggNOGCOG1218.
GeneTreeEBGT00050000010909.
HOGENOMHBG730251.
OMATYEWDTA.
PhylomeDBP22255.
ProtClustDBPRK10931.

Enzyme and pathway databases

BioCycEcoCyc:EG10043-MONOMER.
MetaCyc:EG10043-MONOMER.

Gene expression databases

GenevestigatorP22255.

Family and domain databases

InterProIPR006240. Bisphos_bac.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
KOK01082.
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
TIGRFAMsTIGR01331. Bisphos_cysQ. 1 hit.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSQ_ECOLI
AccessionPrimary (citable) accession number: P22255
Secondary accession number(s): Q2M691
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 20, 2003
Last modified: January 25, 2012
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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