Q8XCG6 (CYSQ_ECO57) Reviewed, UniProtKB/Swiss-Prot

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:	Z5825, ECs5192

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
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 magnesium ion binding Inferred from electronic annotation. Source: InterPro
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_0000142543
Regions
	Region	85 – 88	4	Substrate binding By similarity
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
	Binding site	64	1	Substrate By similarity
	Binding site	205	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XCG6 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 1A2BD090DDAC8AD7	FASTA	246	27,160
	10 20 30 40 50 60 MLDQVCQLAR NAGDAIMQVY DGAKPMDVVS KADNSPVTAA DIAAHTVIMD GLRTLTPDIP 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

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG59412.1. BA000007 Genomic DNA. Translation: BAB38615.1.
PIR	H86118. H91277.
RefSeq	NP_290846.1. NC_002655.2. NP_313219.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8XCG6.
SMR	Q8XCG6. Positions 2-244.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000026983; EBESCP00000025876; EBESCG00000026036. EBESCT00000059919; EBESCP00000057747; EBESCG00000058966.
GeneID	913943. 959907.
GenomeReviews	Gene locus Z5825 in contig AE005174_GR. Gene locus ECs5192 in contig BA000007_GR.
KEGG	ece:Z5825. ecs:ECs5192.
PATRIC	18360017. VBIEscCol44059_5141.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010909.
HOGENOM	HBG730251.
OMA	TYEWDTA.
ProtClustDB	PRK10931.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS5192-MONOMER.
Family and domain databases
InterPro	IPR006240. Bisphos_bac. IPR020583. Inositol_monoP_metal-BS. IPR000760. Inositol_monophosphatase. IPR020550. Inositol_monophosphatase_CS. [Graphical view]
KO	K01082.
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
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_ECO57

Accession

Primary (citable) accession number: Q8XCG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program