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Reviewed, UniProtKB/Swiss-Prot P59735 (CYSQ_SHIFL)

Last modified June 16, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
Ordered Locus Names: SF4272, S4537
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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) By similarity.

Catalytic activity

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

Cofactor

Magnesium By similarity.

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity.

Sequence similarities

Belongs to the inositol monophosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2462463'(2'),5'-bisphosphate nucleotidase cysQ
PRO_0000142546

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

Sequences

Sequence LengthMass (Da)Tools
P59735-1 [UniParc].

Last modified June 20, 2003. Version 1.
Checksum: D41151F8EDE4F6EC

FASTA24627,145
        10         20         30         40         50         60 
MLDQVCQLAR NAGDAIMQVY DGTKPMDVVS KADNSPVTAA DIAAHTVIMD GLRTLAPDIP 

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

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

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


FRVSIY 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

AE005674 Genomic DNA. Translation: AAN45690.1.
AE014073 Genomic DNA. Translation: AAP19476.1.
RefSeqNP_709983.1.
NP_839664.1.

3D structure databases

HSSPHSSP built from PDB template 1KA1 based on UniProtKB P32179.
ModBaseSearch...

Genome annotation databases

GeneID1026559.
1080744.
GenomeReviewsGene locus SF4272 in contig AE005674_GR.
Gene locus S4537 in contig AE014073_GR.
KEGGsfl:SF4272.
sfx:S4537.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP59735.
OMAP59735. KPDILNP.

Enzyme and pathway databases

BioCycSFLE198214:AAN45690.1-MON.

Family and domain databases

InterProIPR006240. Bisphos_bac.
IPR000760. Inositol_P.
[Graphical view]
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00378. INOSPHPHTASE.
ProDomPD023420. Inositol_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01331. bisphos_cysQ. 1 hit.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSQ_SHIFL
AccessionPrimary (citable) accession number: P59735
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents