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Q540U1

- APHA_SALTM

UniProt

Q540U1 - APHA_SALTM

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Protein

Class B acid phosphatase

Gene

aphA

Organism
Salmonella typhimurium
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Dephosphorylates several organic phosphate monoesters. 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 (Probable).1 Publication

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.2 Publications

Cofactori

Binds 1 magnesium ion per subunit.1 Publication

Kineticsi

  1. KM=0.15 mM for pNPP (in the presence of 1 mM MgCl2 at 37 degrees Celsius and pH 5.6)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Nucleophile1 Publication
Metal bindingi69 – 691Magnesium1 Publication
Active sitei71 – 711Proton donor1 Publication
Metal bindingi71 – 711Magnesium; via carbonyl oxygen1 Publication
Binding sitei177 – 1771Substrate1 Publication
Metal bindingi192 – 1921Magnesium1 Publication

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Class B acid phosphataseImported (EC:3.1.3.2Imported1 Publication)
Short name:
CBAP
Gene namesi
Name:aphAImported
OrganismiSalmonella typhimurium
Taxonomic identifieri90371 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Subcellular locationi

Periplasm 1 Publication

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi177 – 1771K → N: 40-fold reduction in phosphatase activity. 5.6-fold increase in KM for pNPP in presence of 1 mM MgCl(2). 1 Publication
Mutagenesisi177 – 1771K → R: 20-fold reduction in phosphatase activity. Nearly 2-fold increase in KM for pNPP in presence of 1 mM MgCl(2). 1 Publication
Mutagenesisi196 – 1961D → N: 6-fold reduction in phosphatase activity. 10000-fold decrease in affinity for Mg(2+). 18-fold increase in KM for pNPP in presence of 1 mM MgCl(2). KM is 0.79 mM for pNPP in the presence of 10 mM MgCl(2). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 237214Class B acid phosphatase1 PublicationPRO_0000414922Add
BLAST

Proteomic databases

PRIDEiQ540U1.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 415
Beta strandi47 – 493
Helixi51 – 577
Turni58 – 603
Beta strandi65 – 684
Turni72 – 743
Helixi78 – 8811
Helixi94 – 974
Helixi99 – 1057
Turni106 – 1083
Helixi109 – 1124
Helixi117 – 12913
Beta strandi132 – 1376
Helixi147 – 1548
Turni159 – 1613
Helixi177 – 1837
Beta strandi186 – 1938
Helixi194 – 20310
Beta strandi205 – 2095
Turni225 – 2273
Beta strandi230 – 2323
Turni233 – 2364

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z5GX-ray2.00A/B/C/D24-237[»]
1Z5UX-ray2.30A/B/C/D24-237[»]
1Z88X-ray2.10A/B/C/D24-237[»]
2AUTX-ray2.25A/B/C/D24-237[»]
ProteinModelPortaliQ540U1.
SMRiQ540U1. Positions 27-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 1382Substrate binding1 Publication

Sequence similaritiesi

Belongs to the class B bacterial acid phosphatase family.By similarity

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]
PfamiPF03767. Acid_phosphat_B. 1 hit.
[Graphical view]
PIRSFiPIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01672. AphA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q540U1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKITLALSA VCLLFTLNHS ANALVSSPST LNPGTNVAKL AEQAPVHWVS
60 70 80 90 100
VAQIENSLTG RPPMAVGFDI DDTVLFSSPG FWRGKKTYSP DSDDYLKNPA
110 120 130 140 150
FWEKMNNGWD EFSIPKEVAR QLIDMHVRRG DSIYFVTGRS QTKTETVSKT
160 170 180 190 200
LADNFHIPAA NMNPVIFAGD KPEQNTKVQW LQEKNMRIFY GDSDNDITAA
210 220 230
RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY
Length:237
Mass (Da):26,315
Last modified:May 24, 2005 - v1
Checksum:i386E11DC84C16269
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181V → A in AAW22868. (PubMed:14501135)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY125468 Genomic DNA. Translation: AAM95781.1.
AY841758 Genomic DNA. Translation: AAW22868.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY125468 Genomic DNA. Translation: AAM95781.1 .
AY841758 Genomic DNA. Translation: AAW22868.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z5G X-ray 2.00 A/B/C/D 24-237 [» ]
1Z5U X-ray 2.30 A/B/C/D 24-237 [» ]
1Z88 X-ray 2.10 A/B/C/D 24-237 [» ]
2AUT X-ray 2.25 A/B/C/D 24-237 [» ]
ProteinModelPortali Q540U1.
SMRi Q540U1. Positions 27-237.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q540U1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.1000. 1 hit.
InterProi IPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view ]
Pfami PF03767. Acid_phosphat_B. 1 hit.
[Graphical view ]
PIRSFi PIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01672. AphA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Expression, purification, crystallization and preliminary X-ray diffraction studies of recombinant class B non-specific acid phosphatase of Salmonella typhimurium."
    Makde R.D., Kumar V., Gupta G.D., Jasti J., Singh T.P., Mahajan S.K.
    Acta Crystallogr. D 59:1849-1852(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-38 AND 40-46, FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, CRYSTALLIZATION.
    Strain: MD6001Imported.
  2. "Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein."
    Makde R.D., Gupta G.D., Mahajan S.K., Kumar V.
    Arch. Biochem. Biophys. 464:70-79(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-237 OF WILD-TYPE AND MUTANTS ARG/ASN-177 IN COMPLEXES WITH CAMP; PHOSPHATE AND MAGNESIUM IONS, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF LYS-177 AND ASP-196.
    Strain: MD6001.

Entry informationi

Entry nameiAPHA_SALTM
AccessioniPrimary (citable) accession number: Q540U1
Secondary accession number(s): Q5MB24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: May 24, 2005
Last modified: October 1, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3