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Q8X176

- PHOA_ASPFU

UniProt

Q8X176 - PHOA_ASPFU

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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

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. cell wall organization Source: UniProtKB-KW
  2. dephosphorylation Source: GOC
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: 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-KW
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.

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.
InParanoidi Q8X176.
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

« 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: October 29, 2014
This is version 64 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