Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acid phosphatase

Gene

phoA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    GO - Biological processi

    Complete GO annotation...

    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 Componenti: Chromosome 1

    Organism-specific databases

    EuPathDBiFungiDB:Afu1g03570.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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.
    InParanoidiQ8X176.
    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

            10         20         30         40         50
    MKPSVATLLA TVSLVYAQTA TEKEPSLSAI ESAAASIQPY SPVSNVEGVA
    60 70 80 90 100
    FNRFFQVWLE NIDYEDAAAD ENMKWLASQG ILLTNFYAVT HPSEPNYCAA
    110 120 130 140 150
    VGGDTFGMDN DNFNQIPANV STVADLLDTK NIAWGEYQEH LPYPGFQGFN
    160 170 180 190 200
    YSNQETYVND YVRKHNPLVL YDSVTKNSTR LRQIKNFTSF EDDLANKKLP
    210 220 230 240 250
    QWAFITPNMT NDAHDTNITF GAKWERSWIA PLLNNSYFMN DTLILLTFDE
    260 270 280 290 300
    DGTYSKSNKI FSVLLGGAIP DELKGTQDDT FYTHYSVIAS VSANWGLPSL
    310 320 330 340 350
    GRWDCGANIL EIVANKTGYV NYDVDTTNLR LNETYPGPMS AGEYSKYSPV
    360 370 380 390 400
    WPNALTRGDC SAGHGILDIV KETYANTEPT YNYSSPFPYD TASNYNTKVT
    410 420 430 440
    ATKKNVTGTH RSSSSSSPSA SSNAAVSAVA PAAGVSGLLL GLALNLL
    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. Curated

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF462065 Genomic DNA. Translation: AAL66381.1.
    AAHF01000007 Genomic DNA. Translation: EAL88069.1. Sequence problems.
    RefSeqiXP_750107.1. XM_745014.1.

    3D structure databases

    ProteinModelPortaliQ8X176.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi3507810.
    KEGGiafm:AFUA_1G03570.

    Organism-specific databases

    EuPathDBiFungiDB:Afu1g03570.

    Phylogenomic databases

    eggNOGiNOG11964.
    HOGENOMiHOG000212034.
    InParanoidiQ8X176.
    KOiK01078.
    OrthoDBiEOG7HF1TN.

    Enzyme and pathway databases

    BRENDAi3.1.3.2. 508.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    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: April 29, 2015
    This is version 67 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.