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Q8X176 (PHOA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acid phosphatase
EC=3.1.3.2
Gene names
Name:phoA
ORF Names:AFUA_1G03570
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has both phosphomonoesterase and phosphodiesterase activity. Cleaves a broad range of phosphate esters.

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Enzyme regulation

Inhibited by NaF, molybdate and vanadate.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor Ref.3 Ref.4.

Induction

Repressed by phosphate. Ref.1

Post-translational modification

The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.

Biophysicochemical properties

Kinetic parameters:

KM=1.45 mM for p-nitrophenyl phophate Ref.1

KM=2.3 mM for bis-(p-nitrophenyl) phophate

pH dependence:

Optimum pH is 4-6. Active from pH 3 to 7.

Sequence caution

The sequence EAL88069.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionHydrolase
   PTMGPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacid phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 419402Acid phosphatase
PRO_0000245560
Propeptide420 – 44728Removed in mature form Potential
PRO_0000245561

Regions

Compositional bias412 – 4198Poly-Ser

Sites

Active site2151Proton donor By similarity

Amino acid modifications

Lipidation4191GPI-like-anchor amidated serine Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3291L → C AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8X176 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 4B2FB1F0ECEF0D72

FASTA44748,988
        10         20         30         40         50         60 
MKPSVATLLA TVSLVYAQTA TEKEPSLSAI ESAAASIQPY SPVSNVEGVA FNRFFQVWLE 

        70         80         90        100        110        120 
NIDYEDAAAD ENMKWLASQG ILLTNFYAVT HPSEPNYCAA VGGDTFGMDN DNFNQIPANV 

       130        140        150        160        170        180 
STVADLLDTK NIAWGEYQEH LPYPGFQGFN YSNQETYVND YVRKHNPLVL YDSVTKNSTR 

       190        200        210        220        230        240 
LRQIKNFTSF EDDLANKKLP QWAFITPNMT NDAHDTNITF GAKWERSWIA PLLNNSYFMN 

       250        260        270        280        290        300 
DTLILLTFDE DGTYSKSNKI FSVLLGGAIP DELKGTQDDT FYTHYSVIAS VSANWGLPSL 

       310        320        330        340        350        360 
GRWDCGANIL EIVANKTGYV NYDVDTTNLR LNETYPGPMS AGEYSKYSPV WPNALTRGDC 

       370        380        390        400        410        420 
SAGHGILDIV KETYANTEPT YNYSSPFPYD TASNYNTKVT ATKKNVTGTH RSSSSSSPSA 

       430        440 
SSNAAVSAVA PAAGVSGLLL GLALNLL

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus."
Bernard M., Mouyna I., Dubreucq G., Debeaupuis J.-P., Fontaine T., Vorgias C., Fuglsang C., Latge J.-P.
Microbiology 148:2819-2829(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 260-274, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[3]"Proteome analysis of Aspergillus fumigatus identifies glycosylphosphatidylinositol-anchored proteins associated to the cell wall biosynthesis."
Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M., Fudali C., Latge J.-P.
Electrophoresis 22:2812-2823(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-53; 164-176; 317-330 AND 347-350, GPI-ANCHOR.
[4]"Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins."
Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P., Ferguson M.A.J.
Glycobiology 13:169-177(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 317-323, STRUCTURE OF GPI-ANCHOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF462065 Genomic DNA. Translation: AAL66381.1.
AAHF01000007 Genomic DNA. Translation: EAL88069.1. Sequence problems.
RefSeqXP_750107.1. XM_745014.1.

3D structure databases

ProteinModelPortalQ8X176.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3507810.
KEGGafm:AFUA_1G03570.

Phylogenomic databases

eggNOGNOG11964.
HOGENOMHOG000212034.
KOK01078.
OrthoDBEOG4FV080.

Enzyme and pathway databases

BRENDA3.1.3.2. 508.

Family and domain databases

InterProIPR007312. Phosphoesterase.
[Graphical view]
PfamPF04185. Phosphoesterase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHOA_ASPFU
AccessionPrimary (citable) accession number: Q8X176
Secondary accession number(s): Q4WK63
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info