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Q8X176

- PHOA_ASPFU

UniProt

Q8X176 - PHOA_ASPFU

Protein

Acid phosphatase

Gene

phoA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.

    Enzyme regulationi

    Inhibited by NaF, molybdate and vanadate.

    Kineticsi

    1. KM=1.45 mM for p-nitrophenyl phophate1 Publication
    2. KM=2.3 mM for bis-(p-nitrophenyl) phophate1 Publication

    pH dependencei

    Optimum pH is 4-6. Active from pH 3 to 7.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei215 – 2151Proton donorBy similarity

    GO - Molecular functioni

    1. acid phosphatase activity Source: ASPGD

    GO - Biological processi

    1. dephosphorylation Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BRENDAi3.1.3.2. 508.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acid phosphatase (EC:3.1.3.2)
    Gene namesi
    Name:phoA
    ORF Names:AFUA_1G03570
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. fungal-type cell wall Source: ASPGD
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 419402Acid phosphatasePRO_0000245560Add
    BLAST
    Propeptidei420 – 44728Removed in mature formSequence AnalysisPRO_0000245561Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis
    Lipidationi419 – 4191GPI-like-anchor amidated serineSequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Expressioni

    Inductioni

    Repressed by phosphate.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ8X176.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi412 – 4198Poly-Ser

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG11964.
    HOGENOMiHOG000212034.
    KOiK01078.
    OrthoDBiEOG7HF1TN.

    Family and domain databases

    InterProiIPR007312. Phosphoesterase.
    [Graphical view]
    PfamiPF04185. Phosphoesterase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8X176-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPSVATLLA TVSLVYAQTA TEKEPSLSAI ESAAASIQPY SPVSNVEGVA    50
    FNRFFQVWLE NIDYEDAAAD ENMKWLASQG ILLTNFYAVT HPSEPNYCAA 100
    VGGDTFGMDN DNFNQIPANV STVADLLDTK NIAWGEYQEH LPYPGFQGFN 150
    YSNQETYVND YVRKHNPLVL YDSVTKNSTR LRQIKNFTSF EDDLANKKLP 200
    QWAFITPNMT NDAHDTNITF GAKWERSWIA PLLNNSYFMN DTLILLTFDE 250
    DGTYSKSNKI FSVLLGGAIP DELKGTQDDT FYTHYSVIAS VSANWGLPSL 300
    GRWDCGANIL EIVANKTGYV NYDVDTTNLR LNETYPGPMS AGEYSKYSPV 350
    WPNALTRGDC SAGHGILDIV KETYANTEPT YNYSSPFPYD TASNYNTKVT 400
    ATKKNVTGTH RSSSSSSPSA SSNAAVSAVA PAAGVSGLLL GLALNLL 447
    Length:447
    Mass (Da):48,988
    Last modified:March 1, 2002 - v1
    Checksum:i4B2FB1F0ECEF0D72
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti329 – 3291L → C AA sequence (PubMed:11545413)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF462065 Genomic DNA. Translation: AAL66381.1.
    AAHF01000007 Genomic DNA. Translation: EAL88069.1. Sequence problems.
    RefSeqiXP_750107.1. XM_745014.1.

    Genome annotation databases

    GeneIDi3507810.
    KEGGiafm:AFUA_1G03570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF462065 Genomic DNA. Translation: AAL66381.1 .
    AAHF01000007 Genomic DNA. Translation: EAL88069.1 . Sequence problems.
    RefSeqi XP_750107.1. XM_745014.1.

    3D structure databases

    ProteinModelPortali Q8X176.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3507810.
    KEGGi afm:AFUA_1G03570.

    Phylogenomic databases

    eggNOGi NOG11964.
    HOGENOMi HOG000212034.
    KOi K01078.
    OrthoDBi EOG7HF1TN.

    Enzyme and pathway databases

    BRENDAi 3.1.3.2. 508.

    Family and domain databases

    InterProi IPR007312. Phosphoesterase.
    [Graphical view ]
    Pfami PF04185. Phosphoesterase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiPHOA_ASPFU
    AccessioniPrimary (citable) accession number: Q8X176
    Secondary accession number(s): Q4WK63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    External Data

    Dasty 3