Reviewed, UniProtKB/Swiss-Prot P22255 (CYSQ_ECOLI)

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
Synonyms:	amtA
Ordered Locus Names:	b4214, JW4172

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.
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 KM=1.2 mM for Ins(1,4)P2

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_0000142541
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
Experimental info
	Sequence conflict	193 – 194	2	QL → HV Ref.1
	Sequence conflict	193 – 194	2	QL → HV Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P22255-1 [UniParc]. Last modified June 20, 2003. Version 2. Checksum: F0CBDFAA98DDAF85	FASTA	246	27,176
	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

References

	« Hide 'large scale' referencesShow '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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	S56439.
RefSeq	AP_004714.1. NP_418635.1.
3D structure databases
HSSP	HSSP built from PDB template 1KA1 based on UniProtKB P32179.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9385N.
Genome annotation databases
GeneID	948728.
GenomeReviews	Gene locus JW4172 in contig AP009048_GR. Gene locus b4214 in contig U00096_GR.
KEGG	ecj:JW4172. eco:b4214.
Organism-specific databases
EchoBASE	EB0041.
EcoGene	EG10043. cysQ.
CMR	Search...
Phylogenomic databases
HOGENOM	P22255.
OMA	P22255. KPDILNP.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10043-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_ECOLI

Accession

Primary (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:	June 16, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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