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P70714 (CYSQ_AGGAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismAggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Taxonomic identifier714 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeAggregatibacter

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2692693'(2'),5'-bisphosphate nucleotidase CysQ
PRO_0000142547

Regions

Region91 – 944Substrate binding By similarity

Sites

Metal binding691Magnesium 1 By similarity
Metal binding891Magnesium 1 By similarity
Metal binding891Magnesium 2 By similarity
Metal binding911Magnesium 1; via carbonyl oxygen By similarity
Metal binding921Magnesium 2 By similarity
Metal binding2161Magnesium 2 By similarity
Binding site691Substrate By similarity
Binding site2161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P70714 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 5E4232ED8021D729

FASTA26930,233
        10         20         30         40         50         60 
MPILTTHLLQ DVIEIAQQAG EHLRCFYQRS VTVRMKEDNT PVTEADLFVS QFLTEKLTAL 

        70         80         90        100        110        120 
TPQIPILSEE NCHIPLTERQ TWRSYWLIDP LDGTQQFINR TGQFSVLVSL VKDHQPVLGV 

       130        140        150        160        170        180 
IHAPMLGSTY YAMQGFGAYK HHDGQHLKLA FHDIQADNAL RIAVGSAAAA EKVRSILNKN 

       190        200        210        220        230        240 
LAYEFHICGS SGLKSTLVAD GVCDCYIRLG CTGEWDTAAS EILLAEMGGI IFDLNYQPLT 

       250        260 
YNKRESFVNP NFVMGITQDF PWDKIFHSN 

« Hide

References

[1]"The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and its adjacent region of Actinobacillus actinomycetemcomitans chromosomal DNA."
Yoshida Y., Nakano Y., Yamashita Y., Koga T.
Biochem. Biophys. Res. Commun. 230:220-225(1997) [PubMed: 9020051] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43718 / FDC Y4 / Serotype b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88189 Genomic DNA. Translation: BAA13553.1.

3D structure databases

ProteinModelPortalP70714.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR006240. Bisphos_bac.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
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_AGGAC
AccessionPrimary (citable) accession number: P70714
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families