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Q59544 (APHA_MORMO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 59. 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:
Class B acid phosphatase
Short name=CBAP
EC=3.1.3.2
Alternative name(s):
Minor phosphate-irrepressible acid phosphatase
Gene names
Name:aphA
Synonyms:napA
OrganismMorganella morganii (Proteus morganii)
Taxonomic identifier582 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Morganella

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dephosphorylates several organic phosphate monoesters including 5'-AMP, 3'-AMP, pNPP, PDP, 5'-UMP, 3'-UMP, G2P, glucose 6-P and ribose 5-P. No activity toward organic phosphate diesters. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds. Ref.1

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.1

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Enzyme regulation

Activated by ethanol. Also activated by Co2+, Zn2+ and glycerol. Inhibited by EDTA, inorganic phosphate, nucleosides and Ca2+. Unaffected by fluoride and tartrate. Ref.1

Subunit structure

Homotetramer. Ref.1

Subcellular location

Periplasm Ref.1.

Sequence similarities

Belongs to the class B bacterial acid phosphatase family.

Biophysicochemical properties

pH dependence:

Optimum pH is about 6 using pNPP as substrate. Retains more than 50% of maximal activity in the pH range 4-7. Ref.1

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionacid phosphatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1
Chain24 – 236213Class B acid phosphatase
PRO_0000024006

Regions

Region136 – 1372Substrate binding By similarity

Sites

Active site681Nucleophile By similarity
Active site701Proton donor By similarity
Metal binding681Magnesium By similarity
Metal binding701Magnesium; via carbonyl oxygen By similarity
Metal binding1911Magnesium By similarity
Binding site1761Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59544 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E5F6A38D918B74D2

FASTA23626,683
        10         20         30         40         50         60 
MRKLTLTLSA LALALSLNSV ADAKVYMPEK VSDGVTVAQL AEQHAIHWIS VEQIEESLKG 

        70         80         90        100        110        120 
QPMAVGFDID DTVLFSSPGF YRGKLEYSPN DYSYLKNPEF WEKMNNEWDK FSMPKKSGME 

       130        140        150        160        170        180 
LVQMHLKRGD TVYFITGRSK TKTETVTKYV QEGLRIPADK MNPVIFAGDE EGQNNKVSWM 

       190        200        210        220        230 
RDHKLKIYYG DADADIAAAR ELNIRGIRVL RASNSSYQPL PKAGQFGEEV VINSEY

« Hide

References

[1]"Cloning and characterization of the NapA acid phosphatase/phosphotransferase of Morganella morganii: identification of a new family of bacterial acid-phosphatase-encoding genes."
Thaller M.C., Lombardi G., Berlutti F., Schippa S., Rossolini G.M.
Microbiology 141:147-154(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-43, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT.
Strain: RS12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X78328 Genomic DNA. Translation: CAA55131.1.

3D structure databases

ProteinModelPortalQ59544.
SMRQ59544. Positions 28-236.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]
PfamPF03767. Acid_phosphat_B. 1 hit.
[Graphical view]
PIRSFPIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01672. AphA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPHA_MORMO
AccessionPrimary (citable) accession number: Q59544
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 59 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

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