Reviewed, UniProtKB/Swiss-Prot P59735 (CYSQ_SHIFL)

Names and origin

Protein names

Recommended 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

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Inferred from electronic annotation. Source: EC inositol or phosphatidylinositol phosphatase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 246	246	3'(2'),5'-bisphosphate nucleotidase cysQ		PRO_0000142546
Sites
	Metal binding	64	1	Magnesium 1 By similarity
	Metal binding	83	1	Magnesium 1 By similarity
	Metal binding	83	1	Magnesium 2 By similarity
	Metal binding	85	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	86	1	Magnesium 2 By similarity
	Metal binding	205	1	Magnesium 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59735-1 [UniParc]. Last modified June 20, 2003. Version 1. Checksum: D41151F8EDE4F6EC	FASTA	246	27,145
	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

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. , 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
EMBLGenBankDDBJ	AE005674 Genomic DNA. Translation: AAN45690.1. AE014073 Genomic DNA. Translation: AAP19476.1.
RefSeq	NP_709983.1. NP_839664.1.
3D structure databases
HSSP	HSSP built from PDB template 1KA1 based on UniProtKB P32179.
ModBase	Search...
Genome annotation databases
GeneID	1026559. 1080744.
GenomeReviews	Gene locus SF4272 in contig AE005674_GR. Gene locus S4537 in contig AE014073_GR.
KEGG	sfl:SF4272. sfx:S4537.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P59735.
OMA	P59735. KPDILNP.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN45690.1-MON.
Family and domain databases
InterPro	IPR006240. Bisphos_bac. IPR000760. Inositol_P. [Graphical view]
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PRINTS	PR00378. INOSPHPHTASE.
ProDom	PD023420. Inositol_P. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01331. bisphos_cysQ. 1 hit.
PROSITE	PS00629. IMP_1. 1 hit. PS00630. IMP_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSQ_SHIFL

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)